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Conserved domains on  [gi|1190792252|gb|OTA37500|]
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hypothetical protein BTJ68_02769 [Hortaea werneckii EXF-2000]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11790 super family cl36060
D-3-phosphoglycerate dehydrogenase; Provisional
467-878 0e+00

D-3-phosphoglycerate dehydrogenase; Provisional


The actual alignment was detected with superfamily member PRK11790:

Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 617.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 467 QDIKVLLLENVNKTGQDILKKQGY-QIEILKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQ 545
Cdd:PRK11790    9 DKIKFLLLEGVHQSAVEVLRAAGYtNIEYHKGALDEEELIEAIKDAHFIGIRSRTQLTEEVLAAAEKLVAIGCFCIGTNQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 546 VDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSV 625
Cdd:PRK11790   89 VDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWNKSAAGSFEVRGKTLGIVGYGHIGTQLSV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 626 LAEAMGMRVIYYDVVNLMSLGTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPA 705
Cdd:PRK11790  169 LAESLGMRVYFYDIEDKLPLGNARQVGSLEELLAQSDVVSLHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 706 LIKASQAGKLAGAALDVYPNEPAGNGPKFTNelntwteELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNFGTT 785
Cdd:PRK11790  249 LADALKSGHLAGAAIDVFPVEPKSNGDPFES-------PLRGLDNVILTPHIGGSTQEAQENIGLEVAGKLVKYSDNGST 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 786 AGAVNMPEVTLRsltiEEPNHVRVIYIHKNIPGVLRRVNEILGDH--NVDKQMTDSRGDVAYLMADISNVNISEIQQLYQ 863
Cdd:PRK11790  322 LSAVNFPEVSLP----EHPGGHRLLHIHENRPGVLAAINQIFAEQgiNIAAQYLQTDGEIGYVVIDVDADYAEEALDALK 397
                         410
                  ....*....|....*
gi 1190792252 864 SLEdlGSrIRTRVLY 878
Cdd:PRK11790  398 AIP--GT-IRARLLY 409
STE3 pfam02076
Pheromone A receptor;
32-314 3.14e-94

Pheromone A receptor;


:

Pssm-ID: 334803  Cd Length: 282  Bit Score: 297.50  E-value: 3.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252  32 FFSLLVTFLIIPPLVQHWRNRNIGATLCVFYAMIMNLMAFTNAVLWPNDDLEHWYSGSGLCDVEVKLQIAWSVAAPATLI 111
Cdd:pfam02076   1 VFSFIAFILVLPPLPWHLRARNIGACLLIFWLFLLNLIYFVNAIIWRGDDIDWAPVGYGWCDISTKLIIGASVGIPAALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 112 CVLRALANAMNTDRLSLgkTKAQRWRGYAIDLTLCVGIPLLSMVFHFIVQSKRYFLYGISGCVPTATQSYLTVGLIYVPP 191
Cdd:pfam02076  81 CIARNLYRILSTRRVTL--SRREKRRRIIIDLLICLGIPILQMALHYIVQGHRYDIFEDVGCYPAYYNTWPALVLFIIWP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 192 LLLVLVDAYFALLILYRLCRYRRTFSIILAHNDT--TKSRFLRLYILCIVWLLGIIPLSSWMLSVNL--GSQQEPYKWVE 267
Cdd:pfam02076 159 PIISLIAAVYAVLTLRRFIRRRKQFRDLLSSSNSglNKSRFLRLLALALVIILITLPLSIYLLVLNItqGPLQPWYSWSD 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1190792252 268 AHDYskWNEITMIRSNgKIVFDRFIWLGCGIMVFLTFGFGKEAVGMY 314
Cdd:pfam02076 239 VHSD--WSTILQFPSG-QWQFDRWIPVASAILFFLFFGFGKEARNMY 282
 
Name Accession Description Interval E-value
PRK11790 PRK11790
D-3-phosphoglycerate dehydrogenase; Provisional
467-878 0e+00

D-3-phosphoglycerate dehydrogenase; Provisional


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 617.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 467 QDIKVLLLENVNKTGQDILKKQGY-QIEILKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQ 545
Cdd:PRK11790    9 DKIKFLLLEGVHQSAVEVLRAAGYtNIEYHKGALDEEELIEAIKDAHFIGIRSRTQLTEEVLAAAEKLVAIGCFCIGTNQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 546 VDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSV 625
Cdd:PRK11790   89 VDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWNKSAAGSFEVRGKTLGIVGYGHIGTQLSV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 626 LAEAMGMRVIYYDVVNLMSLGTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPA 705
Cdd:PRK11790  169 LAESLGMRVYFYDIEDKLPLGNARQVGSLEELLAQSDVVSLHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 706 LIKASQAGKLAGAALDVYPNEPAGNGPKFTNelntwteELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNFGTT 785
Cdd:PRK11790  249 LADALKSGHLAGAAIDVFPVEPKSNGDPFES-------PLRGLDNVILTPHIGGSTQEAQENIGLEVAGKLVKYSDNGST 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 786 AGAVNMPEVTLRsltiEEPNHVRVIYIHKNIPGVLRRVNEILGDH--NVDKQMTDSRGDVAYLMADISNVNISEIQQLYQ 863
Cdd:PRK11790  322 LSAVNFPEVSLP----EHPGGHRLLHIHENRPGVLAAINQIFAEQgiNIAAQYLQTDGEIGYVVIDVDADYAEEALDALK 397
                         410
                  ....*....|....*
gi 1190792252 864 SLEdlGSrIRTRVLY 878
Cdd:PRK11790  398 AIP--GT-IRARLLY 409
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
469-779 0e+00

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240653  Cd Length: 304  Bit Score: 565.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 469 IKVLLLENVNKTGQDILKKQGYQIEILKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDL 548
Cdd:cd12176     1 IKILLLENIHPSADELFRAGGIEVERLKGALDEDELIEALKDVHLLGIRSKTQLTEEVLEAAPKLLAIGCFCIGTNQVDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 549 KYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAE 628
Cdd:cd12176    81 DAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRGIWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 629 AMGMRVIYYDVVNLMSLGTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIK 708
Cdd:cd12176   161 ALGMRVIFYDIAEKLPLGNARQVSSLEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAE 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1190792252 709 ASQAGKLAGAALDVYPNEPAGNGPKFTNelntwteELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNY 779
Cdd:cd12176   241 ALRSGHLAGAAVDVFPEEPASNGEPFSS-------PLQGLPNVILTPHIGGSTEEAQENIGLEVAGKLVKY 304
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism, ...
466-799 2.22e-114

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223189  Cd Length: 324  Bit Score: 352.00  E-value: 2.22e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 466 TQDIKVLLLENVNKTGQDILKKQGYQIEILKSSLPENELIEKIQDVHVIGIrSKTQLTANVLKHAKNLIVIGCFCIGTNQ 545
Cdd:COG0111     1 KMMIKVLVTDPLAPDALEELLAAYDVEVPDGPDLDEEELLEALADADALIV-SVTPVTEEVLAAAPNLKAIGRAGAGVDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 546 VDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSV 625
Cdd:COG0111    80 IDLEAATKRGILVVNAPGGNAISVAELVLALLLALARRIPDADASQRRGEWDRKAFRGTELAGKTVGIIGLGRIGRAVAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 626 LAEAMGMRVIYYDVVNLMSLGTSN---QVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVD 702
Cdd:COG0111   160 RLKAFGMKVIGYDPYSPRERAGVDgvvGVDSLDELLAEADILTLHLPLTPETRGLINAEELAKMKPGAILINAARGGVVD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 703 IPALIKASQAGKLAGAALDVYPNEPAGNGpkftnelntwtEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNF 782
Cdd:COG0111   240 EDALLAALDSGKIAGAALDVFEEEPLPAD-----------SPLWDLPNVILTPHIGGSTDEAQERVAEIVAENIVRYLAG 308
                         330
                  ....*....|....*..
gi 1190792252 783 GTTAGavNMPEVTLRSL 799
Cdd:COG0111   309 GPVVN--NAPEVDLERG 323
STE3 pfam02076
Pheromone A receptor;
32-314 3.14e-94

Pheromone A receptor;


Pssm-ID: 334803  Cd Length: 282  Bit Score: 297.50  E-value: 3.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252  32 FFSLLVTFLIIPPLVQHWRNRNIGATLCVFYAMIMNLMAFTNAVLWPNDDLEHWYSGSGLCDVEVKLQIAWSVAAPATLI 111
Cdd:pfam02076   1 VFSFIAFILVLPPLPWHLRARNIGACLLIFWLFLLNLIYFVNAIIWRGDDIDWAPVGYGWCDISTKLIIGASVGIPAALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 112 CVLRALANAMNTDRLSLgkTKAQRWRGYAIDLTLCVGIPLLSMVFHFIVQSKRYFLYGISGCVPTATQSYLTVGLIYVPP 191
Cdd:pfam02076  81 CIARNLYRILSTRRVTL--SRREKRRRIIIDLLICLGIPILQMALHYIVQGHRYDIFEDVGCYPAYYNTWPALVLFIIWP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 192 LLLVLVDAYFALLILYRLCRYRRTFSIILAHNDT--TKSRFLRLYILCIVWLLGIIPLSSWMLSVNL--GSQQEPYKWVE 267
Cdd:pfam02076 159 PIISLIAAVYAVLTLRRFIRRRKQFRDLLSSSNSglNKSRFLRLLALALVIILITLPLSIYLLVLNItqGPLQPWYSWSD 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1190792252 268 AHDYskWNEITMIRSNgKIVFDRFIWLGCGIMVFLTFGFGKEAVGMY 314
Cdd:pfam02076 239 VHSD--WSTILQFPSG-QWQFDRWIPVASAILFFLFFGFGKEARNMY 282
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
471-790 2.58e-90

D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the largest portion of the catalytic domain of 2-hydroxyacid dehydrogenases as the NAD binding domain is inserted within the structural domain.


Pssm-ID: 334054  Cd Length: 312  Bit Score: 288.42  E-value: 2.58e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 471 VLLLENVNKTGQDILKKQgYQIEILKSSLPEnELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKY 550
Cdd:pfam00389   1 VLITDPLSPEALELLKEA-AEVEVHDELLTE-ELLEKAKGADALIVRSNTPVTAEVLEAAPKLKVIARAGVGVDNIDLDA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 551 AAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAEAM 630
Cdd:pfam00389  79 ATERGILVTNVPGYNTESVAELTVGLILALARRIPEADASVRAGKWKKGGLIGLELYGKTLGVIGGGGIGGGVAAIAKAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 631 GMRVIYYDVVNLMSLGTSNQVPSLDALL------QQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIP 704
Cdd:pfam00389 159 GMGVVAYDPYPNPERAEAGGVYVLSLDLllldlpESDDVINVNPPTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 705 ALIKASQAGKLAGAALDVYPNEPAgngpkftnelntWTEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNFGT 784
Cdd:pfam00389 239 ALDALLEEGIAAAADLDVEEEPPP------------VNSPLLDLPNVILTPHIGGATEEAQENMAEEAAENLVAFLKGGP 306

                  ....*.
gi 1190792252 785 TAGAVN 790
Cdd:pfam00389 307 PPNAVN 312
7tmD_STE3 cd14966
fungal a-factor pheromone receptor STE3, member of the class D family of seven-transmembrane G ...
28-316 1.46e-87

fungal a-factor pheromone receptor STE3, member of the class D family of seven-transmembrane G protein-coupled receptors; This subfamily represents the a-factor pheromone receptor encoded by the STE3 gene, which is required for pheromone sensing and mating in haploid cells of the yeast Saccharomyces cerevisiae. The STE3-encoded seven-transmembrane domain receptor is a member of the class D GPCRs. Class D receptors are composed of two major subfamilies: Ste2 and Ste3. These two GPCRs (Ste2 and Ste3) sense the polypeptide mating pheromones, alpha-factor and a-factor, which activate a G protein-coupled receptors on the surface of the opposite yeast-mating haploid-types (MATa and MAT-alpha), respectively. Activation of these receptors by pheromones leads to activation of the mitogen-activated protein kinase (MAPK) signal transduction cascades, G1 cell cycle arrest, and polarized cell growth in the direction of the partner cell (a process called shmooing), which ultimately induces cell-cell fusion and the formation of a diploid zygote. Like all GPCRs, these pheromone mating factor receptors possess the same basic architecture of seven-transmembrane (7TM) domains and share common signaling mechanisms; however, there is no significant sequence similarity either between Ste2 and Ste3, or between these two receptors and the other 7TM GPCRs. Thus, STE2 and STE3 represent phylogenetically distinct groups.


Pssm-ID: 320097  Cd Length: 259  Bit Score: 279.00  E-value: 1.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252  28 IIFAFFSLLVTFLIIPPLVQHWRNRNIGATLCVFYAMIMNLMAFTNAVLWPNDDLEHWYSgSGLCDVEVKLQIAWSVAAP 107
Cdd:cd14966     1 IAFPIFSFLAFILVIPPLPWHLRARNVGACLLIFWLFLLNLINFVNAIIWPGDDINRAPD-KVWCDISTKLIIGASVGIP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 108 ATLICVLRALANAMNTDRLSLgkTKAQRWRGYAIDLTLCVGIPLLSMVFHFIVQSKRYFLYGISGCVPTATQSYLTVGLI 187
Cdd:cd14966    80 AASLCINRRLYRIASTRRVTL--TRADKRRRIIIDLLICLGLPILVMALHYIVQGHRYDIFEDVGCYPAIYNSWPALVLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 188 YVPPLLLVLVDAYFALLILYRLCRYRRTFSIIL--AHNDTTKSRFLRLYILCIVWLLGIIPLSSWMLsvnlgsqqepykw 265
Cdd:cd14966   158 YIWPLIISLIAAVYAVLTLRRFFRRRKQFRDLLssSNSGLTTSRFLRLMALALVEILITLPLSIYVL------------- 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1190792252 266 veahdyskwneitmirSNGKIVFDRFIWLGCGIMVFLTFGFGKEAVGMYRN 316
Cdd:cd14966   225 ----------------VLGSLELDRWIPVASAFLFFAFFGFGSEARKMYRR 259
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
470-796 6.94e-87

D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273556 [Multi-domain]  Cd Length: 525  Bit Score: 286.53  E-value: 6.94e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQGYQIEIlKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLK 549
Cdd:TIGR01327   1 KVLIADPISPDGIDILEDVGVEVDV-QTGLSREELLEIIPDYDALIVRSATKVTEEVIAAAPKLKVIGRAGVGVDNIDIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 550 YAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAEA 629
Cdd:TIGR01327  80 AATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMGTELYGKTLGVIGLGRIGSIVAKRAKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 630 MGMRVIYYDVV----NLMSLGTsNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPA 705
Cdd:TIGR01327 160 FGMKVLAYDPYispeRAEQLGV-ELVDDLDELLARADFITVHTPLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 706 LIKASQAGKLAGAALDVYPNEPAGNGPkftnelntwteeLRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNFGTT 785
Cdd:TIGR01327 239 LYEALEEGHVRAAALDVFEKEPPTDNP------------LFDLDNVIATPHLGASTREAQENVATQVAEQVLDALKGLPV 306
                         330
                  ....*....|.
gi 1190792252 786 AGAVNMPEVTL 796
Cdd:TIGR01327 307 PNAVNAPGIDA 317
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
608-695 2.97e-05

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 45.13  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252  608 GKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDV--VN-LMSLGTSNQVPSLDALLQQAD-FVTLhvpelpeT--INMISTK 681
Cdd:smart00997  23 GKNVVVAGYGDVGKGVAARLRGLGARVIVTEIdpIRaLEAAMDGFEVMKMEEAAKRADiFVTA-------TgnKDVITRE 95
                           90
                   ....*....|....
gi 1190792252  682 QFEQMKNGSYLLNA 695
Cdd:smart00997  96 HFRAMKDGAILANA 109
 
Name Accession Description Interval E-value
PRK11790 PRK11790
D-3-phosphoglycerate dehydrogenase; Provisional
467-878 0e+00

D-3-phosphoglycerate dehydrogenase; Provisional


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 617.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 467 QDIKVLLLENVNKTGQDILKKQGY-QIEILKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQ 545
Cdd:PRK11790    9 DKIKFLLLEGVHQSAVEVLRAAGYtNIEYHKGALDEEELIEAIKDAHFIGIRSRTQLTEEVLAAAEKLVAIGCFCIGTNQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 546 VDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSV 625
Cdd:PRK11790   89 VDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGWNKSAAGSFEVRGKTLGIVGYGHIGTQLSV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 626 LAEAMGMRVIYYDVVNLMSLGTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPA 705
Cdd:PRK11790  169 LAESLGMRVYFYDIEDKLPLGNARQVGSLEELLAQSDVVSLHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDA 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 706 LIKASQAGKLAGAALDVYPNEPAGNGPKFTNelntwteELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNFGTT 785
Cdd:PRK11790  249 LADALKSGHLAGAAIDVFPVEPKSNGDPFES-------PLRGLDNVILTPHIGGSTQEAQENIGLEVAGKLVKYSDNGST 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 786 AGAVNMPEVTLRsltiEEPNHVRVIYIHKNIPGVLRRVNEILGDH--NVDKQMTDSRGDVAYLMADISNVNISEIQQLYQ 863
Cdd:PRK11790  322 LSAVNFPEVSLP----EHPGGHRLLHIHENRPGVLAAINQIFAEQgiNIAAQYLQTDGEIGYVVIDVDADYAEEALDALK 397
                         410
                  ....*....|....*
gi 1190792252 864 SLEdlGSrIRTRVLY 878
Cdd:PRK11790  398 AIP--GT-IRARLLY 409
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
469-779 0e+00

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240653  Cd Length: 304  Bit Score: 565.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 469 IKVLLLENVNKTGQDILKKQGYQIEILKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDL 548
Cdd:cd12176     1 IKILLLENIHPSADELFRAGGIEVERLKGALDEDELIEALKDVHLLGIRSKTQLTEEVLEAAPKLLAIGCFCIGTNQVDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 549 KYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAE 628
Cdd:cd12176    81 DAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRGIWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 629 AMGMRVIYYDVVNLMSLGTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIK 708
Cdd:cd12176   161 ALGMRVIFYDIAEKLPLGNARQVSSLEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAE 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1190792252 709 ASQAGKLAGAALDVYPNEPAGNGPKFTNelntwteELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNY 779
Cdd:cd12176   241 ALRSGHLAGAAVDVFPEEPASNGEPFSS-------PLQGLPNVILTPHIGGSTEEAQENIGLEVAGKLVKY 304
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism, ...
466-799 2.22e-114

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223189  Cd Length: 324  Bit Score: 352.00  E-value: 2.22e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 466 TQDIKVLLLENVNKTGQDILKKQGYQIEILKSSLPENELIEKIQDVHVIGIrSKTQLTANVLKHAKNLIVIGCFCIGTNQ 545
Cdd:COG0111     1 KMMIKVLVTDPLAPDALEELLAAYDVEVPDGPDLDEEELLEALADADALIV-SVTPVTEEVLAAAPNLKAIGRAGAGVDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 546 VDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSV 625
Cdd:COG0111    80 IDLEAATKRGILVVNAPGGNAISVAELVLALLLALARRIPDADASQRRGEWDRKAFRGTELAGKTVGIIGLGRIGRAVAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 626 LAEAMGMRVIYYDVVNLMSLGTSN---QVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVD 702
Cdd:COG0111   160 RLKAFGMKVIGYDPYSPRERAGVDgvvGVDSLDELLAEADILTLHLPLTPETRGLINAEELAKMKPGAILINAARGGVVD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 703 IPALIKASQAGKLAGAALDVYPNEPAGNGpkftnelntwtEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNF 782
Cdd:COG0111   240 EDALLAALDSGKIAGAALDVFEEEPLPAD-----------SPLWDLPNVILTPHIGGSTDEAQERVAEIVAENIVRYLAG 308
                         330
                  ....*....|....*..
gi 1190792252 783 GTTAGavNMPEVTLRSL 799
Cdd:COG0111   309 GPVVN--NAPEVDLERG 323
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
470-779 7.84e-105

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240650  Cd Length: 304  Bit Score: 326.30  E-value: 7.84e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQGYQIeILKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLK 549
Cdd:cd12173     1 KVLVTDPIDEEGLELLREAGIEV-DVAPGLSEEELLAIIADADALIVRSATKVTAEVIEAAPRLKVIGRAGVGVDNIDVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 550 YAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAEA 629
Cdd:cd12173    80 AATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGRIGREVARRARA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 630 MGMRVIYYD-----------VVNLMslgtsnqvpSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRG 698
Cdd:cd12173   160 FGMKVLAYDpyisaeraaagGVELV---------SLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTARG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 699 TVVDIPALIKASQAGKLAGAALDVYPNEPagngPKFTNelntwteELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVN 778
Cdd:cd12173   231 GIVDEAALADALKSGKIAGAALDVFEQEP----PPADS-------PLLGLPNVILTPHLGASTEEAQERVAVDAAEQVLA 299

                  .
gi 1190792252 779 Y 779
Cdd:cd12173   300 V 300
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
469-779 3.63e-103

Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240628  Cd Length: 301  Bit Score: 321.79  E-value: 3.63e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 469 IKVLLLENVNKTGQDILKKQGYQIeILKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDL 548
Cdd:cd05303     1 MKILITDGIDEIAIEKLEEAGFEV-DYEPLIAKEELLEKIKDYDVLIVRSRTKVTKEVIDAAKNLKIIARAGVGLDNIDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 549 KYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAE 628
Cdd:cd05303    80 EYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLGKWNKKKYKGIELRGKTLGIIGFGRIGREVAKIAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 629 AMGMRVIYYDVVNLMSLGTSNQVP--SLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPAL 706
Cdd:cd05303   160 ALGMNVIAYDPYPKDEQAVELGVKtvSLEELLKNSDFISLHVPLTPETKHMINKKELELMKDGAIIINTSRGGVIDEEAL 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190792252 707 IKASQAGKLAGAALDVYPNEPAGNgpkftnelntwtEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNY 779
Cdd:cd05303   240 LEALKSGKLAGAALDVFENEPPPG------------SKLLELPNVSLTPHIGASTKEAQERIGEELANKIIEF 300
PRK13581 PRK13581
D-3-phosphoglycerate dehydrogenase; Provisional
470-808 3.34e-99

D-3-phosphoglycerate dehydrogenase; Provisional


Pssm-ID: 237436 [Multi-domain]  Cd Length: 526  Bit Score: 319.32  E-value: 3.34e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQGyQIEI-LKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDL 548
Cdd:PRK13581    2 KVLVSDPISPAGLEILKDAP-GVEVdVKTGLDKEELLEIIGDYDALIVRSATKVTAEVLEAAKNLKVIGRAGVGVDNVDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 549 KYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAE 628
Cdd:PRK13581   81 PAATRRGIIVVNAPTGNTISAAEHTIALMLALARNIPQAHASLKAGKWERKKFMGVELYGKTLGIIGLGRIGSEVAKRAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 629 AMGMRVIYYDV-----------VNLMslgtsnqvpSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASR 697
Cdd:PRK13581  161 AFGMKVIAYDPyisperaaqlgVELV---------SLDELLARADFITLHTPLTPETRGLIGAEELAKMKPGVRIINCAR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 698 GTVVDIPALIKASQAGKLAGAALDVYPNEPAGNGPkftnelntwteeLRNLKNIILTPHIGGSTEEAQAAIGIEVADALV 777
Cdd:PRK13581  232 GGIIDEAALAEALKSGKVAGAALDVFEKEPPTDSP------------LFELPNVVVTPHLGASTAEAQENVAIQVAEQVI 299
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1190792252 778 NYVNFGTTAGAVNMPevtlrSLTIEEPNHVR 808
Cdd:PRK13581  300 DALRGGPVPNAVNLP-----SITAEEAEKLK 325
STE3 pfam02076
Pheromone A receptor;
32-314 3.14e-94

Pheromone A receptor;


Pssm-ID: 334803  Cd Length: 282  Bit Score: 297.50  E-value: 3.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252  32 FFSLLVTFLIIPPLVQHWRNRNIGATLCVFYAMIMNLMAFTNAVLWPNDDLEHWYSGSGLCDVEVKLQIAWSVAAPATLI 111
Cdd:pfam02076   1 VFSFIAFILVLPPLPWHLRARNIGACLLIFWLFLLNLIYFVNAIIWRGDDIDWAPVGYGWCDISTKLIIGASVGIPAALL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 112 CVLRALANAMNTDRLSLgkTKAQRWRGYAIDLTLCVGIPLLSMVFHFIVQSKRYFLYGISGCVPTATQSYLTVGLIYVPP 191
Cdd:pfam02076  81 CIARNLYRILSTRRVTL--SRREKRRRIIIDLLICLGIPILQMALHYIVQGHRYDIFEDVGCYPAYYNTWPALVLFIIWP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 192 LLLVLVDAYFALLILYRLCRYRRTFSIILAHNDT--TKSRFLRLYILCIVWLLGIIPLSSWMLSVNL--GSQQEPYKWVE 267
Cdd:pfam02076 159 PIISLIAAVYAVLTLRRFIRRRKQFRDLLSSSNSglNKSRFLRLLALALVIILITLPLSIYLLVLNItqGPLQPWYSWSD 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1190792252 268 AHDYskWNEITMIRSNgKIVFDRFIWLGCGIMVFLTFGFGKEAVGMY 314
Cdd:pfam02076 239 VHSD--WSTILQFPSG-QWQFDRWIPVASAILFFLFFGFGKEARNMY 282
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
470-781 9.73e-93

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240649  Cd Length: 306  Bit Score: 294.40  E-value: 9.73e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVL----LLENVNKTGQDILKKQGYQIEILKS--SLPENELIEKIQDVHVIgIRSKTQLTANVLKHAKNLIVIGCFCIGT 543
Cdd:cd12172     1 KVLvtprSFSKYSEEAKELLEAAGFEVVLNPLgrPLTEEELIELLKDADGV-IAGLDPITEEVLAAAPRLKVISRYGVGY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 544 NQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSaGCwEVRGKTLGIVGYGHVGSQL 623
Cdd:cd12172    80 DNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLMLALARQIPQADREVRAGGWDRPV-GT-ELYGKTLGIIGLGRIGKAV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 624 SVLAEAMGMRVIYYDVVNLMSLGTSNQVP--SLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVV 701
Cdd:cd12172   158 ARRLSGFGMKVLAYDPYPDEEFAKEHGVEfvSLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 702 DIPALIKASQAGKLAGAALDVYPNEPagngPKFTNelntwteELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVN 781
Cdd:cd12172   238 DEEALYEALKSGRIAGAALDVFEEEP----PPADS-------PLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDVLA 306
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
470-779 1.20e-90

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622  Cd Length: 302  Bit Score: 288.76  E-value: 1.20e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQ-DILKKQGYQIeILKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDL 548
Cdd:cd05198     1 KVLVLEPLFPPEAlEALEATGFEV-IVADDLLADELEALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 549 KYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQG-VWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLA 627
Cdd:cd05198    80 DAAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGwGWLWAGFPGYELEGKTVGIVGLGRIGQRVAKRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 628 EAMGMRVIYYDVVNLMSLGTSN--QVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPA 705
Cdd:cd05198   160 QAFGMKVLYYDRTRKPEPEEDLgfRVVSLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGGLVDEDA 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190792252 706 LIKASQAGKLAGAALDVYPNEPAGNGpkftnelntwtEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNY 779
Cdd:cd05198   240 LLRALKSGKIAGAALDVFEPEPLPAD-----------HPLLELPNVILTPHIAGYTEEARERMAEIAVENLERF 302
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
471-790 2.58e-90

D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the largest portion of the catalytic domain of 2-hydroxyacid dehydrogenases as the NAD binding domain is inserted within the structural domain.


Pssm-ID: 334054  Cd Length: 312  Bit Score: 288.42  E-value: 2.58e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 471 VLLLENVNKTGQDILKKQgYQIEILKSSLPEnELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKY 550
Cdd:pfam00389   1 VLITDPLSPEALELLKEA-AEVEVHDELLTE-ELLEKAKGADALIVRSNTPVTAEVLEAAPKLKVIARAGVGVDNIDLDA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 551 AAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAEAM 630
Cdd:pfam00389  79 ATERGILVTNVPGYNTESVAELTVGLILALARRIPEADASVRAGKWKKGGLIGLELYGKTLGVIGGGGIGGGVAAIAKAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 631 GMRVIYYDVVNLMSLGTSNQVPSLDALL------QQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIP 704
Cdd:pfam00389 159 GMGVVAYDPYPNPERAEAGGVYVLSLDLllldlpESDDVINVNPPTTMKTGVIIINEARGMLKDAVAIINAAGGGVIDEA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 705 ALIKASQAGKLAGAALDVYPNEPAgngpkftnelntWTEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNFGT 784
Cdd:pfam00389 239 ALDALLEEGIAAAADLDVEEEPPP------------VNSPLLDLPNVILTPHIGGATEEAQENMAEEAAENLVAFLKGGP 306

                  ....*.
gi 1190792252 785 TAGAVN 790
Cdd:pfam00389 307 PPNAVN 312
7tmD_STE3 cd14966
fungal a-factor pheromone receptor STE3, member of the class D family of seven-transmembrane G ...
28-316 1.46e-87

fungal a-factor pheromone receptor STE3, member of the class D family of seven-transmembrane G protein-coupled receptors; This subfamily represents the a-factor pheromone receptor encoded by the STE3 gene, which is required for pheromone sensing and mating in haploid cells of the yeast Saccharomyces cerevisiae. The STE3-encoded seven-transmembrane domain receptor is a member of the class D GPCRs. Class D receptors are composed of two major subfamilies: Ste2 and Ste3. These two GPCRs (Ste2 and Ste3) sense the polypeptide mating pheromones, alpha-factor and a-factor, which activate a G protein-coupled receptors on the surface of the opposite yeast-mating haploid-types (MATa and MAT-alpha), respectively. Activation of these receptors by pheromones leads to activation of the mitogen-activated protein kinase (MAPK) signal transduction cascades, G1 cell cycle arrest, and polarized cell growth in the direction of the partner cell (a process called shmooing), which ultimately induces cell-cell fusion and the formation of a diploid zygote. Like all GPCRs, these pheromone mating factor receptors possess the same basic architecture of seven-transmembrane (7TM) domains and share common signaling mechanisms; however, there is no significant sequence similarity either between Ste2 and Ste3, or between these two receptors and the other 7TM GPCRs. Thus, STE2 and STE3 represent phylogenetically distinct groups.


Pssm-ID: 320097  Cd Length: 259  Bit Score: 279.00  E-value: 1.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252  28 IIFAFFSLLVTFLIIPPLVQHWRNRNIGATLCVFYAMIMNLMAFTNAVLWPNDDLEHWYSgSGLCDVEVKLQIAWSVAAP 107
Cdd:cd14966     1 IAFPIFSFLAFILVIPPLPWHLRARNVGACLLIFWLFLLNLINFVNAIIWPGDDINRAPD-KVWCDISTKLIIGASVGIP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 108 ATLICVLRALANAMNTDRLSLgkTKAQRWRGYAIDLTLCVGIPLLSMVFHFIVQSKRYFLYGISGCVPTATQSYLTVGLI 187
Cdd:cd14966    80 AASLCINRRLYRIASTRRVTL--TRADKRRRIIIDLLICLGLPILVMALHYIVQGHRYDIFEDVGCYPAIYNSWPALVLV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 188 YVPPLLLVLVDAYFALLILYRLCRYRRTFSIIL--AHNDTTKSRFLRLYILCIVWLLGIIPLSSWMLsvnlgsqqepykw 265
Cdd:cd14966   158 YIWPLIISLIAAVYAVLTLRRFFRRRKQFRDLLssSNSGLTTSRFLRLMALALVEILITLPLSIYVL------------- 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1190792252 266 veahdyskwneitmirSNGKIVFDRFIWLGCGIMVFLTFGFGKEAVGMYRN 316
Cdd:cd14966   225 ----------------VLGSLELDRWIPVASAFLFFAFFGFGSEARKMYRR 259
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
470-796 6.94e-87

D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273556 [Multi-domain]  Cd Length: 525  Bit Score: 286.53  E-value: 6.94e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQGYQIEIlKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLK 549
Cdd:TIGR01327   1 KVLIADPISPDGIDILEDVGVEVDV-QTGLSREELLEIIPDYDALIVRSATKVTEEVIAAAPKLKVIGRAGVGVDNIDIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 550 YAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAEA 629
Cdd:TIGR01327  80 AATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMGTELYGKTLGVIGLGRIGSIVAKRAKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 630 MGMRVIYYDVV----NLMSLGTsNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPA 705
Cdd:TIGR01327 160 FGMKVLAYDPYispeRAEQLGV-ELVDDLDELLARADFITVHTPLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 706 LIKASQAGKLAGAALDVYPNEPAGNGPkftnelntwteeLRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNFGTT 785
Cdd:TIGR01327 239 LYEALEEGHVRAAALDVFEKEPPTDNP------------LFDLDNVIATPHLGASTREAQENVATQVAEQVLDALKGLPV 306
                         330
                  ....*....|.
gi 1190792252 786 AGAVNMPEVTL 796
Cdd:TIGR01327 307 PNAVNAPGIDA 317
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
487-790 3.36e-84

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223980  Cd Length: 324  Bit Score: 272.57  E-value: 3.36e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 487 KQGYQIEILKSSL-PENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFSN 565
Cdd:COG1052    20 KEKFEVERYEDDLtPDTELAERLKDADAVITFVNDRIDAEVLEKLPGLKLIATRSAGYDNVDLEAAKERGITVTNVPGYS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 566 SRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCW----EVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVVN 641
Cdd:COG1052   100 TEAVAEHAVALILALARRIHEGDRRVREGNWSLSGGPDPllgfDLRGKTLGIIGLGRIGQAVARRLKGFGMKVLYYDRSP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 642 LMSLGTSNQVP--SLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAA 719
Cdd:COG1052   180 NPEAEKELGARyvDLDELLAESDIISLHCPLTPETRHLINAEELAKMKPGAILVNTARGGLVDEQALIDALKSGKIAGAG 259
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1190792252 720 LDVYPNEPAGNGPKFTnelntwteELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNFGTTAGAVN 790
Cdd:COG1052   260 LDVFENEPALFDHPLL--------RLDNFPNVVLTPHIASATEEARKAMAELALENLEAFFDGGVPPNEVN 322
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
470-781 1.68e-77

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240655  Cd Length: 317  Bit Score: 254.47  E-value: 1.68e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQgYQIEILKS--SLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVD 547
Cdd:cd12178     2 KVLVTGWIPKEALEELEEN-FEVTYYDGlgLISKEELLERIADYDALITPLSTPVDKEIIDAAKNLKIIANYGAGFDNID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 548 LKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQI--GDRnnELHQGVWNKVSAGCW---EVRGKTLGIVGYGHVGSQ 622
Cdd:cd12178    81 VDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRIaeGDR--LMRRGGFLGWAPLFFlghELAGKTLGIIGMGRIGQA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 623 LSVLAEAMGMRVIYYDVVNLMS-----LGTSnQVPsLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASR 697
Cdd:cd12178   159 VARRAKAFGMKILYYNRHRLSEetekeLGAT-YVD-LDELLKESDFVSLHAPYTPETHHLIDAAAFKLMKPTAYLINAAR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 698 GTVVDIPALIKASQAGKLAGAALDVYPNEPAGNgpkftnelntwtEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALV 777
Cdd:cd12178   237 GPLVDEKALVDALKTGEIAGAALDVFEFEPEVS------------PELKKLDNVILTPHIGNATVEARDAMAKEAADNII 304

                  ....
gi 1190792252 778 NYVN 781
Cdd:cd12178   305 SFLE 308
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
470-774 1.09e-72

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240652  Cd Length: 311  Bit Score: 240.94  E-value: 1.09e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQGYQI---EILKSSlPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQV 546
Cdd:cd12175     1 KVLFLGPEFPDAEELLRALLPPApgvEVVTAA-ELDEEAALLADADVLVPGMRKVIDAELLAAAPRLRLIQQPGVGLDGV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 547 DLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVW-NKVSAGCWEVRGKTLGIVGYGHVGSQLSV 625
Cdd:cd12175    80 DLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAGRWgRPEGRPSRELSGKTVGIVGLGNIGRAVAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 626 LAEAMGMRVIYYDVVNL---MSLGTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVD 702
Cdd:cd12175   160 RLRGFGVEVIYYDRFRDpeaEEKDLGVRYVELDELLAESDVVSLHVPLTPETRHLIGAEELAAMKPGAILINTARGGLVD 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190792252 703 IPALIKASQAGKLAGAALDVYPNEP-AGNGPkftnelntwteeLRNLKNIILTPHIGGSTEEAQAAIGIEVAD 774
Cdd:cd12175   240 EEALLAALRSGHLAGAGLDVFWQEPlPPDDP------------LLRLDNVILTPHIAGVTDESYQRMAAIVAE 300
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
470-790 8.27e-72

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240651  Cd Length: 305  Bit Score: 238.61  E-value: 8.27e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQGYQIeilKSSLPENE--LIEKIQDVHVIGIrsktqltanvlkhAKNLIVIGCFCIGTNQVD 547
Cdd:cd12174     2 KILTANKISKKGLERFKKDKYEV---KEDALEDPdaLIVRSDKLHDMDF-------------APSLKAIARAGAGVNNID 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 548 LKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNN--------ELHQGVWN--KVSAGcWEVRGKTLGIVGYG 617
Cdd:cd12174    66 VDAASKRGIVVFNTPGANANAVAELVIAMMLALSRNIIQAIKwvtngdgdDISKGVEKgkKQFVG-TELRGKTLGVIGLG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 618 HVGSQLSVLAEAMGMRVIYYDVV-------NLMSLGTsnQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGS 690
Cdd:cd12174   145 NIGRLVANAALALGMKVIGYDPYlsveaawKLSVEVQ--RVTSLEELLATADYITLHVPLTDETRGLINAELLAKMKPGA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 691 YLLNASRGTVVDIPALIKASQAGKLaGAALDVYPnEPAGngpkftnelntwteeLRNLKNIILTPHIGGSTEEAQAAIGI 770
Cdd:cd12174   223 ILLNFARGEIVDEEALLEALDEGKL-GGYVTDFP-EPAL---------------LGHLPNVIATPHLGASTEEAEENCAV 285
                         330       340
                  ....*....|....*....|
gi 1190792252 771 EVADALVNYVNFGTTAGAVN 790
Cdd:cd12174   286 MAARQIMDFLETGNITNSVN 305
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
500-780 9.78e-72

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240639  Cd Length: 307  Bit Score: 238.51  E-value: 9.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 500 PENELIEKIQDVHVIgIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIIS 579
Cdd:cd12162    34 SPEEVVERIKDADIV-ITNKVVLDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 580 LARQIGDRNNELHQGVWNKVSAGC------WEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDvvnlmSLGTSNQVP- 652
Cdd:cd12162   113 LARLVAYHNDVVKAGEWQKSPDFCfwdypiIELAGKTLGIIGYGNIGQAVARIARAFGMKVLFAE-----RKGAPPLREg 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 653 --SLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPagn 730
Cdd:cd12162   188 yvSLDELLAQSDVISLHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEP--- 264
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1190792252 731 gPKFTNELntwteeLRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYV 780
Cdd:cd12162   265 -PRADNPL------LKAAPNLIITPHIAWASREARQRLMDILVDNIKAFL 307
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
500-764 1.67e-69

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240648  Cd Length: 310  Bit Score: 232.43  E-value: 1.67e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 500 PENELIEKIQDVHVIgIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIIS 579
Cdd:cd12171    36 PEEELLEALKDADIL-ITHFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 580 LARQIGDRNNELHQGVW-----NKVSAGCwEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYD-VVNLMSLGTSN-QVP 652
Cdd:cd12171   115 ETRNIARAHAALKDGEWrkdyyNYDGYGP-ELRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDpYVDPEKIEADGvKKV 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 653 SLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPAGNGP 732
Cdd:cd12171   194 SLEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEEPLPADH 273
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1190792252 733 kftnelntwteELRNLKNIILTPHIGGSTEEA 764
Cdd:cd12171   274 -----------PLLKLDNVTLTPHIAGATRDV 294
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
482-764 8.48e-67

C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.


Pssm-ID: 240624  Cd Length: 312  Bit Score: 225.09  E-value: 8.48e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 482 QDILKKQGYQIEILKSSLPEnELIEKIQDVHVIGIRSkTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNS 561
Cdd:cd05299    17 REVLEEAGVELVDAQSRTED-ELIEAAADADALLVQY-APVTAEVIEALPRLKVIVRYGVGVDNVDVAAATERGIPVCNV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 562 PFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWN-KVSAGCWEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVV 640
Cdd:cd05299    95 PDYCTEEVADHALALILALARKLPFLDRAVRAGGWDwTVGGPIRRLRGLTLGLVGFGRIGRAVAKRAKAFGFRVIAYDPY 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 641 ---NLMSLGTSnQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAG 717
Cdd:cd05299   175 vpdGVAALGGV-RVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVNTARGGLVDEAALARALKSGRIAG 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1190792252 718 AALDVYPNEPAgngpkftnelnTWTEELRNLKNIILTPHIGGSTEEA 764
Cdd:cd05299   254 AALDVLEEEPP-----------PADSPLLSAPNVILTPHAAWYSEES 289
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
487-778 2.17e-64

D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase, HPR) catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. In humans, HPR deficiency causes primary hyperoxaluria type 2, characterized by over-excretion of L-glycerate and oxalate in the urine, possibly due to an imbalance in competition with L-lactate dehydrogenase, another formate dehydrogenase (FDH)-like enzyme. GDH, like FDH and other members of the D-specific hydroxyacid dehydrogenase family that also includes L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase, typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form, despite often low sequence identity. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240626  Cd Length: 309  Bit Score: 218.42  E-value: 2.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 487 KQGYQIEIL--KSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFS 564
Cdd:cd05301    18 REGFEVEVWdeDRPLPREELLEAAKGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVTNTPDV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 565 NSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCW---EVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYD--- 638
Cdd:cd05301    98 LTDATADLAFALLLAAARRVVEGDRFVRAGEWKGWSPTLLlgtDLHGKTLGIVGMGRIGQAVARRAKGFGMKILYHNrsr 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 639 -VVNLMSLGTsnQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAG 717
Cdd:cd05301   178 kPEAEEELGA--RYVSLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVDEDALVEALKSGKIAG 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1190792252 718 AALDVYPNEPAGNGPkftnelntwteELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVN 778
Cdd:cd05301   256 AGLDVFEPEPLPADH-----------PLLTLPNVVLLPHIGSATVETRTAMAELAADNLLA 305
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
574-758 3.21e-59

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 335114 [Multi-domain]  Cd Length: 176  Bit Score: 199.24  E-value: 3.21e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 574 IGEIISLARQIGDRNNELHQGVWNKVSAGC-WEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVVNLMSLGTSN-QV 651
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRWARRNALLgRELSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEELGaRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 652 PSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPAGNG 731
Cdd:pfam02826  81 VSLDELLAESDIVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEEEPLPAD 160
                         170       180
                  ....*....|....*....|....*..
gi 1190792252 732 pkftnelntwtEELRNLKNIILTPHIG 758
Cdd:pfam02826 161 -----------HPLLDLPNVILTPHIA 176
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
470-763 2.48e-58

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240656  Cd Length: 306  Bit Score: 201.75  E-value: 2.48e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQGYQIEiLKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLK 549
Cdd:cd12179     1 KILIIDKNHPSLTELLEALGFEVD-YDPTISREEILAIIPQYDGLIIRSRFPIDKEFIEKATNLKFIARAGAGLENIDLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 550 YAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAEA 629
Cdd:cd12179    80 YAKEKGIELFNAPEGNRDAVGEHALGMLLALFNKLNRADQEVRNGIWDREGNRGVELMGKTVGIIGYGNMGKAFAKRLSG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 630 MGMRVIYYDVVNLMSLGTSNQVpSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKA 709
Cdd:cd12179   160 FGCKVIAYDKYKNFGDAYAEQV-SLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKA 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1190792252 710 SQAGKLAGAALDVYPNEpagngpKFTNE----LNTWTEELRNLKNIILTPHIGGSTEE 763
Cdd:cd12179   239 LKSGKILGACLDVLEYE------KASFEsifnQPEAFEYLIKSPKVILTPHIAGWTFE 290
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
484-781 3.36e-56

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240620  Cd Length: 323  Bit Score: 196.37  E-value: 3.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 484 ILKKQGYQIEILKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPF 563
Cdd:cd01619    19 ILKAGGVDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDNIDLDYAKELGIGVTNVPE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 564 SNSRSVAEQMIGEIISLARQIGdRNNELHQGVWNKVSAGCW-EVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVVnl 642
Cdd:cd01619    99 YSPNAVAEHTIALILALLRNRK-YIDERDKNQDLQDAGVIGrELEDQTVGVVGTGKIGRAVAQRAKGFGMKVIAYDPF-- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 643 mslgTSNQVP-------SLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKL 715
Cdd:cd01619   176 ----RNPELEdkgvkyvSLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVDTEALIEALDSGKI 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1190792252 716 AGAALDVYPNE-----PAGNGPKFTNELNtwtEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVN 781
Cdd:cd01619   252 FGAGLDVLEDEtpdllKDLEGEIFKDALN---ALLGRRPNVIITPHTAFYTDDALKNMVEISCENIVDFLE 319
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
485-781 5.87e-55

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240654  Cd Length: 321  Bit Score: 192.92  E-value: 5.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 485 LKKQGYQIEI-LKSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSP- 562
Cdd:cd12177    21 LKKIGYVDRFeVPPDISGKALAEKLKGYDIIIASVTPNFDKEFFEYNDGLKLIARHGIGYDNVDLKAATEHGVIVTRVPg 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 563 FSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGC-WEVRGKTLGIVGYGHVGSQLS-VLAEAMGMRVIYYD-- 638
Cdd:cd12177   101 AVERDAVAEHAVALILTVLRKINQASEAVKEGKWTERANFVgHELSGKTVGIIGYGNIGSRVAeILKEGFNAKVLAYDpy 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 639 --VVNLMSLGTsnQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLA 716
Cdd:cd12177   181 vsEEVIKKKGA--KPVSLEELLAESDIISLHAPLTEETYHMINEKAFSKMKKGVILVNTARGELIDEEALIEALKSGKIA 258
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1190792252 717 GAALDVYPNEPAG-NGPkftnelntwteeLRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVN 781
Cdd:cd12177   259 GAGLDVLEEEPIKaDHP------------LLHYENVVITPHIGAYTYESLYGMGEKVVDDIEDFLA 312
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
486-789 3.68e-54

D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240662  Cd Length: 329  Bit Score: 190.82  E-value: 3.68e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 486 KKQGYQIEILKSSL-PENelIEKIQDVHVIGIRSKTQLTANVLKHAKNLiviGCFCI-----GTNQVDLKYAAENGIAVF 559
Cdd:cd12186    21 KEHPVEVDTTTELLtPET--VDLAKGYDGVVVQQTLPYDEEVYEKLAEY---GIKQIalrsaGVDMIDLDLAKENGLKIT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 560 NSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQG--VWNKVSAGcWEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYY 637
Cdd:cd12186    96 NVPAYSPRAIAEFAVTQALNLLRNTPEIDRRVAKGdfRWAPGLIG-REIRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAY 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 638 DVVN---LMSLGTSnqVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGK 714
Cdd:cd12186   175 DPYPnpeLEKFLLY--YDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGK 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 715 LAGAALDVYPNEPA-----GNGPKFTNELntwTEELRNLKNIILTPHIGGSTEEAQAAIgIEVA-DALVNYVNFGTTAGA 788
Cdd:cd12186   253 IAGAALDTYENETGyfnkdWSGKEIEDEV---LKELIAMPNVLITPHIAFYTDTAVKNM-VEISlDDALEIIEGGTSENE 328

                  .
gi 1190792252 789 V 789
Cdd:cd12186   329 V 329
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
470-783 3.94e-54

D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified as an enzyme that interconverts benzoylformate and D-mandelate, is a D-2-hydroxyacid dehydrogenase family member that catalyzes the conversion of c3-branched 2-ketoacids. D-ManDH exhibits broad substrate specificities for 2-ketoacids with large hydrophobic side chains, particularly those with C3-branched side chains. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Glycerate dehydrogenase catalyzes the reaction (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240645  Cd Length: 321  Bit Score: 190.45  E-value: 3.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVnKTGQDILKKQGYQIEILKSSLPE-NELIEKIQ-----DVHVIGIRSKT-----QLTANVLKH-AKNLIVIG 537
Cdd:cd12168     3 KVLLLGDP-IHAHDEWKELSSIAEVIYPTSGTrEEFIEALKegkygDFVAIYRTFGSagetgPFDEELISPlPPSLKIIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 538 CFCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWN--KVSAGCWEVRGKTLGIVG 615
Cdd:cd12168    82 HAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRgfLDLTLAHDPRGKTLGILG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 616 YGHVGSQLSVLAEAMGMRVIYYDVVNLMSL---GTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYL 692
Cdd:cd12168   162 LGGIGKAIARKAAAFGMKIIYHNRSRLPEElekALATYYVSLDELLAQSDVVSLNCPLTAATRHLINKKEFAKMKDGVII 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 693 LNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPAGNgpkftnelntwtEELRNLKNIILTPHIGGSTEEAQAAIGIEV 772
Cdd:cd12168   242 VNTARGAVIDEDALVDALESGKVASAGLDVFENEPEVN------------PGLLKMPNVTLLPHMGTLTVETQEKMEELV 309
                         330
                  ....*....|.
gi 1190792252 773 ADALVNYVNFG 783
Cdd:cd12168   310 LENIEAFLETG 320
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
489-781 5.40e-53

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240642  Cd Length: 314  Bit Score: 187.07  E-value: 5.40e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 489 GYQIEIL-KSSLPENELIEKIqDVHVIGIRSKtqltANVLKHAKNLIVIGCFCIGTNQVDLKYAAEnGIAVFNSpFSNSR 567
Cdd:cd12165    21 GLYAEVPeLPDEAAEEALEDA-DVLVGGRLTK----EEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANN-HGNSP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 568 SVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCW---EVRGKTLGIVGYGHVGSQLSVLAEAMGMRVI--------- 635
Cdd:cd12165    94 AVAEHALALILALAKRIVEYDNDLRRGIWHGRAGEEPeskELRGKTVGILGYGHIGREIARLLKAFGMRVIgvsrspked 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 636 -YYDVVNLMSlgtsnqvpSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGK 714
Cdd:cd12165   174 eGADFVGTLS--------DLDEALEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERP 245
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190792252 715 LAGAALDVYPNEPAGNGPKFTNELntwteELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVN 781
Cdd:cd12165   246 IAGAAIDVWWRYPSRGDPVAPSRY-----PFHELPNVIMSPHNAGWTEETFRRRIDEAAENIRRYLR 307
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
470-764 1.92e-52

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, aka Hydroxypyruvate Reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240638  Cd Length: 315  Bit Score: 185.50  E-value: 1.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDI------LKKQGYQIEIL-KSSLPENELIEKIQDVHVIGIrSKTQLTANVLKHAKNLIVIGCFCIG 542
Cdd:cd12161     1 KIVLLEPLGVSEEKIeelaapLEEQGHEFVYYdTKTTDTAELIERSKDADIVMI-ANMPLPGEVIEACKNLKMISVAFTG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 543 TNQVDLKYAAENGIAVFNSP-FSNSrSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCwEVRGKTLGIVGYGHVGS 621
Cdd:cd12161    80 VDHVDLEACKERGITVSNAAgYSTE-AVAELTIGLAIDLLRNIVPCDAAVRAGGTKAGLIGR-ELAGKTVGIVGTGAIGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 622 QLSVLAEAMGMRVIYYDVV---NLMSLGTSnQVpSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRG 698
Cdd:cd12161   158 RVARLFKAFGCKVLAYSRSekeEAKALGIE-YV-SLDELLAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARG 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1190792252 699 TVVDIPALIKASQAGKLAGAALDVYPNEP--AGNGPkftnelntwteeLRNLKNIILTPHIGGSTEEA 764
Cdd:cd12161   236 PVVDNEALADALNEGKIAGAGIDVFDMEPplPADYP------------LLHAPNTILTPHVAFATEEA 291
PRK13243 PRK13243
glyoxylate reductase; Reviewed
470-797 2.12e-51

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 183.46  E-value: 2.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQgYQIEILK--SSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVD 547
Cdd:PRK13243    4 KVFITREIPENGIEMLEEH-FEVEVWEdeREIPREVLLEKVRDVDALVTMLSERIDCEVFEAAPRLRIVANYAVGYDNID 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 548 LKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGcW--------EVRGKTLGIVGYGHV 619
Cdd:PRK13243   83 VEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGVA-WhplmflgyDVYGKTIGIIGFGRI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 620 GSQLSVLAEAMGMRVIYYDVVNL----MSLGTsnQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNA 695
Cdd:PRK13243  162 GQAVARRAKGFGMRILYYSRTRKpeaeKELGA--EYRPLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVNT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 696 SRGTVVDIPALIKASQAGKLAGAALDVYPNEPAGNgpkftnelntwtEELRNLKNIILTPHIGGSTEEAQAAIGIEVADA 775
Cdd:PRK13243  240 ARGKVVDTKALVKALKEGWIAGAGLDVFEEEPYYN------------EELFSLKNVVLAPHIGSATFEAREGMAELVAEN 307
                         330       340
                  ....*....|....*....|..
gi 1190792252 776 LVNYVNFGTTAGAVNMPEVTLR 797
Cdd:PRK13243  308 LIAFKRGEVPPTLVNREVVKVR 329
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
506-806 7.10e-51

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240635  Cd Length: 343  Bit Score: 181.96  E-value: 7.10e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 506 EKIQDVHVIGIRSKTQLTANVLKHAKnLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQig 585
Cdd:cd12158    32 EDLKDADVLLVRSVTKVNEALLEGSK-VKFVGTATIGTDHIDTDYLKERGIGFANAPGCNANSVAEYVLSALLVLAQR-- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 586 drnnelhqgvwnkvsaGCWEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVvNLMSLGTSNQVPSLDALLQQADFVT 665
Cdd:cd12158   109 ----------------QGFSLKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDP-PRAEAEGDPGFVSLEELLAEADIIT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 666 LHVP-----ELPeTINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPAGNgpkftnelnt 740
Cdd:cd12158   172 LHVPltrdgEHP-TYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEPEID---------- 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1190792252 741 wtEELRNLKNiILTPHIGGSTEEAQAAiGIE-VADALVNYVNF-GTTAGAVNMPEVTLRSLTIEEPNH 806
Cdd:cd12158   241 --LELLDKVD-IATPHIAGYSLEGKAR-GTEmIYEALCQFLGLkARKSLSDLLPAPALPSITLDGSLD 304
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
505-768 1.56e-50

D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240663  Cd Length: 329  Bit Score: 180.55  E-value: 1.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 505 IEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQI 584
Cdd:cd12187    36 VEEFKDAEVISVFVYSRLDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 585 GDRNNELHQGVWNKVSAGCWEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVVNLMSLGTSNQVP--SLDALLQQAD 662
Cdd:cd12187   116 REAIERTRRGDFSQAGLRGFELAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGFRyvSLEELLQESD 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 663 FVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPA-------GNGPKFT 735
Cdd:cd12187   196 IISLHVPYTPQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEVlreeaelFREDVSP 275
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1190792252 736 NELNTWTE--ELRNLKNIILTPHIGGSTEEAQAAI 768
Cdd:cd12187   276 EDLKKLLAdhALLRKPNVIITPHVAYNTKEALERI 310
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
510-779 4.37e-50

Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; Hydroxy(phenyl)pyruvate reductase (HPPR) catalyzes the NADP-dependent reduction of hydroxyphenylpyruvates, hydroxypyruvate, or pyruvate to its respective lactate. HPPR acts as a dimer and is related to D-isomer-specific 2-hydroxyacid dehydrogenases, a superfamily that includes groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240633  Cd Length: 301  Bit Score: 178.43  E-value: 4.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 510 DVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQI--GDR 587
Cdd:cd12156    42 RIRAVVTNGETGLSAALIAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIpaADR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 588 nnelhqgvwnKVSAGCWE---------VRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYdvvnlmslGTSNQ-------V 651
Cdd:cd12156   122 ----------FVRAGRWPkgafpltrkVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYH--------GRRPKpdvpyryY 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 652 PSLDALLQQADFVTLHVPELPETINMISTKQFEQM-KNGsYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPagN 730
Cdd:cd12156   184 ASLLELAAESDVLVVACPGGPATRHLVNAEVLEALgPDG-VLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP--N 260
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1190792252 731 GPkftnelntwtEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNY 779
Cdd:cd12156   261 VP----------AALLDLDNVVLTPHIASATVETRRAMGDLVLANLEAF 299
PRK06487 PRK06487
glycerate dehydrogenase; Provisional
485-779 1.05e-49

glycerate dehydrogenase; Provisional


Pssm-ID: 180588  Cd Length: 317  Bit Score: 177.97  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 485 LKKQGYQIEILKSSLPEnELIEKIQDVHVIgIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFS 564
Cdd:PRK06487   21 LEQAFDELQLHDATTPE-QVAERLRGAQVA-ISNKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 565 NSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSA------GCWEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYD 638
Cdd:PRK06487   99 GTPSVAQHTLALLLALATRLPDYQQAVAAGRWQQSSQfclldfPIVELEGKTLGLLGHGELGGAVARLAEAFGMRVLIGQ 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 639 VVNlmSLGTSNQVPsLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGA 718
Cdd:PRK06487  179 LPG--RPARPDRLP-LDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGA 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1190792252 719 ALDVYPNEPAGNGpkftNELNTWteelrNLKNIILTPHIGGSTEEAQAAIGIEVADALVNY 779
Cdd:PRK06487  256 ATDVLSVEPPVNG----NPLLAP-----DIPRLIVTPHSAWGSREARQRIVGQLAENARAF 307
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
499-781 1.10e-49

Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240646  Cd Length: 308  Bit Score: 177.70  E-value: 1.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 499 LPENELIEKIQDVHVI-GIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPfSNSRSVAEQMIGEI 577
Cdd:cd12169    35 LDEDALAERLAPFDAIvLMRERTPFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCGTG-GGPTATAELTWALI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 578 ISLARQIGDRNNELHQGVWNKVSAGcwEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYdvvnlmslgTSN-------- 649
Cdd:cd12169   114 LALARNLPEEDAALRAGGWQTTLGT--GLAGKTLGIVGLGRIGARVARIGQAFGMRVIAW---------SSNltaeraaa 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 650 ----QVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPN 725
Cdd:cd12169   183 agveAAVSKEELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAALDVFDV 262
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1190792252 726 EPAgngPKftnelntwTEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVN 781
Cdd:cd12169   263 EPL---PA--------DHPLRGLPNVLLTPHIGYVTEEAYEGFYGQAVENIAAWLA 307
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
470-768 1.11e-45

Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.


Pssm-ID: 240625  Cd Length: 313  Bit Score: 166.54  E-value: 1.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQGYQIEILKSSlpENELIEKIQDVHVI-GIRsktqLTANVLKHAKNLIVIGCFCIGTNQVDL 548
Cdd:cd05300     2 KILVLSPLDDEHLERLRAAAPGAELRVVT--AEELTEELADADVLlGNP----PLPELLPAAPRLRWIQSTSAGVDALLF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 549 KYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKvSAGCWEVRGKTLGIVGYGHVGSQLSVLAE 628
Cdd:cd05300    76 PELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPRYARNQAERRWQR-RGPVRELAGKTVLIVGLGDIGREIARRAK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 629 AMGMRVI-----------YYDVVNLMSlgtsnqvpSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASR 697
Cdd:cd05300   155 AFGMRVIgvrrsgrpappVVDEVYTPD--------ELDELLPEADYVVNALPLTPETRGLFNAERFAAMKPGAVLINVGR 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190792252 698 GTVVDIPALIKASQAGKLAGAALDVYPNEPAgngPKftnelntwTEELRNLKNIILTPHIGG---STEEAQAAI 768
Cdd:cd05300   227 GSVVDEDALIEALESGRIAGAALDVFEEEPL---PA--------DSPLWDLPNVIITPHISGdspSYPERVVEI 289
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
473-781 4.11e-45

NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of a formate anion to carbon dioxide coupled with the reduction of NAD+ to NADH. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family have 2 highly similar subdomains of the alpha/beta form, with NAD binding occurring in the cleft between subdomains. NAD contacts are primarily to the Rossmann-fold NAD-binding domain which is inserted within the linear sequence of the more diverse flavodoxin-like catalytic subdomain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production from C1 compounds such as methanol, and in the stress responses of plants. NAD-dependent FDH is useful in cofactor regeneration in asymmetrical biocatalytic reduction processes, where FDH irreversibly oxidizes formate to carbon dioxide, while reducing the oxidized form of the cofactor to the reduced form.


Pssm-ID: 240627  Cd Length: 348  Bit Score: 165.96  E-value: 4.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 473 LLENV-NKTG-QDILKKQGYQIEILKSSLPENELIEK-IQDVHVIgIrskTQ------LTANVLKHAKNLIVIGCFCIGT 543
Cdd:cd05302    20 LLGCVeNELGlRKWLESQGHELVVTSDKDGPDSELEKhLPDADVV-I---STpfhpayMTAERIAKAKNLKLALTAGIGS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 544 NQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWN--KVSAGCWEVRGKTLGIVGYGHVGS 621
Cdd:cd05302    96 DHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGWNvaDVVKRAYDLEGKTVGTVGAGRIGL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 622 QLSVLAEAMGMRVIYYDVVNLMS-----LGTSnQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNAS 696
Cdd:cd05302   176 RVLRRLKPFDVHLLYYDRHRLPEevekeLGLT-RHADLEDMVSKCDVVTINCPLHPETEGLFNKELLSKMKKGAYLVNTA 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 697 RGTVVDIPALIKASQAGKLAGAALDVYPNEPAgngPKftnelntwTEELRNLKNIILTPHIGGSTEEAQAAIGIEVADAL 776
Cdd:cd05302   255 RGKICDREAVAEALESGHLAGYAGDVWFPQPA---PK--------DHPWRTMPNNAMTPHISGTTLDAQARYAAGTKEIL 323

                  ....*
gi 1190792252 777 VNYVN 781
Cdd:cd05302   324 ERFFE 328
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
553-780 5.03e-43

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240644  Cd Length: 330  Bit Score: 159.26  E-value: 5.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 553 ENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSA--GCWEVRGKTLGIVGYGHVGSQLSVLAEAM 630
Cdd:cd12167    93 ERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRDWGWPTrrGGRGLYGRTVGIVGFGRIGRAVVELLRPF 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 631 GMRVIYYD----VVNLMSLGTsnQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPAL 706
Cdd:cd12167   173 GLRVLVYDpylpAAEAAALGV--ELVSLDELLARSDVVSLHAPLTPETRGMIDARLLALMRDGATFINTARGALVDEAAL 250
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190792252 707 IKASQAGKLaGAALDVYPNEPAGNGpkftnelntwtEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYV 780
Cdd:cd12167   251 LAELRSGRL-RAALDVTDPEPLPPD-----------SPLRTLPNVLLTPHIAGSTGDERRRLGDYALDELERFL 312
PRK06932 PRK06932
glycerate dehydrogenase; Provisional
497-783 5.12e-43

glycerate dehydrogenase; Provisional


Pssm-ID: 235890  Cd Length: 314  Bit Score: 158.81  E-value: 5.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 497 SSLPEnELIEKIQDVHVIgIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGE 576
Cdd:PRK06932   32 HTSAE-QTIERAKDADIV-ITSKVLFTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGM 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 577 IISLARQIGDRNNELHQGVWNKVSAGCW------EVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVVNlMSLGTSNQ 650
Cdd:PRK06932  110 IFALKHSLMGWYRDQLSDRWATCKQFCYfdypitDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAEHKG-ASVCREGY 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 651 VPsLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPagn 730
Cdd:PRK06932  189 TP-FEEVLKQADIVTLHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEP--- 264
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1190792252 731 gPKFTNELntwTEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNYVNFG 783
Cdd:PRK06932  265 -PEKDNPL---IQAAKRLPNLLITPHIAWASDSAVTTLVNKVAQNIEEFVQQG 313
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
521-768 7.94e-43

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2-domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240659  Cd Length: 328  Bit Score: 158.76  E-value: 7.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 521 QLTANVLK--HAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIgdrnnelHQGvWNK 598
Cdd:cd12183    55 DLDAPVLEklAELGVKLIALRCAGFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKI-------HRA-YNR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 599 VSAGCW--------EVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVV---NLMSLGTsnQVPSLDALLQQADFVTLH 667
Cdd:cd12183   127 VREGNFsldgllgfDLHGKTVGVIGTGKIGQAFARILKGFGCRVLAYDPYpnpELAKLGV--EYVDLDELLAESDIISLH 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 668 VPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEpagnGPKF---------TNEL 738
Cdd:cd12183   205 CPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEE----AGLFfedhsdeiiQDDV 280
                         250       260       270
                  ....*....|....*....|....*....|
gi 1190792252 739 ntwTEELRNLKNIILTPHIGGSTEEAQAAI 768
Cdd:cd12183   281 ---LARLLSFPNVLITGHQAFFTKEALTNI 307
PRK08410 PRK08410
2-hydroxyacid dehydrogenase; Provisional
501-764 5.63e-42

2-hydroxyacid dehydrogenase; Provisional


Pssm-ID: 181414  Cd Length: 311  Bit Score: 155.53  E-value: 5.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 501 ENELIEKIQDVHVIgIRSKTQLTANVLKHAKNLIVIgcfCI---GTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEI 577
Cdd:PRK08410   33 PEEVIERIKDANII-ITNKVVIDKEVLSQLPNLKLI---CItatGTNNVDIEYAKKKGIAVKNVAGYSTESVAQHTFAML 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 578 ISLARQIGDRNNELHQGVWNK------VSAGCWEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDvvnlmSLGTSNQV 651
Cdd:PRK08410  109 LSLLGRINYYDRYVKSGEYSEspifthISRPLGEIKGKKWGIIGLGTIGKRVAKIAQAFGAKVVYYS-----TSGKNKNE 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 652 P----SLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAgKLAGAALDVYPNEP 727
Cdd:PRK08410  184 EyervSLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGRGGIVNEKDLAKALDE-KDIYAGLDVLEKEP 262
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1190792252 728 AGNGPKFTNelntwteeLRNLKNIILTPHIGGSTEEA 764
Cdd:PRK08410  263 MEKNHPLLS--------IKNKEKLLITPHIAWASKEA 291
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
486-764 3.57e-40

Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, NAD-binding and catalytic domains; This group contains various putative dehydrogenases related to D-lactate dehydrogenase (LDH), (R)-2-hydroxyglutarate dehydrogenase (HGDH), and related enzymes, members of the 2-hydroxyacid dehydrogenases family. LDH catalyzes the interconversion of pyruvate and lactate, and HGDH catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Despite often low sequence identity within this 2-hydroxyacid dehydrogenase family, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240661  Cd Length: 322  Bit Score: 150.82  E-value: 3.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 486 KKQGYQIEILKSSL-PEN-ELIEKIQDVHVIGirsKTQLTANVLK--HAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNS 561
Cdd:cd12185    21 KEYNVEVTLTKEPLtLENaHLAEGYDGISILG---KSKISAELLEklKEAGVKYISTRSIGYDHIDLDAAKELGIKVSNV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 562 PFSnSRSVAEQMIGEIISLARQIgdrNNELHQGVWNKVSAGCW---EVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYD 638
Cdd:cd12185    98 TYS-PNSVADYTVMLMLMALRKY---KQIMKRAEVNDYSLGGLqgrELRNLTVGVIGTGRIGQAVIKNLSGFGCKILAYD 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 639 VVNLMSLGTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGA 718
Cdd:cd12185   174 PYPNEEVKKYAEYVDLDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGGA 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1190792252 719 ALDVYPNEpagNGPKFTN----EL-NTWTEELRNLKNIILTPHIGGSTEEA 764
Cdd:cd12185   254 ALDVIEGE---DGIYYNDrkgdILsNRELAILRSFPNVILTPHMAFYTDQA 301
PRK07574 PRK07574
formate dehydrogenase; Provisional
522-781 3.85e-40

formate dehydrogenase; Provisional


Pssm-ID: 181041  Cd Length: 385  Bit Score: 152.52  E-value: 3.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 522 LTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWN--KV 599
Cdd:PRK07574  104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGGWNiaDC 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 600 SAGCWEVRGKTLGIVGYGHVGsqLSVLA--EAMGMRVIYYDVVNLMS-----LGTSNQvPSLDALLQQADFVTLHVPELP 672
Cdd:PRK07574  184 VSRSYDLEGMTVGIVGAGRIG--LAVLRrlKPFDVKLHYTDRHRLPEeveqeLGLTYH-VSFDSLVSVCDVVTIHCPLHP 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 673 ETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDV-YPNEPAGNGPkftnelntWteelRNLKNI 751
Cdd:PRK07574  261 ETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVwFPQPAPADHP--------W----RTMPRN 328
                         250       260       270
                  ....*....|....*....|....*....|
gi 1190792252 752 ILTPHIGGSTEEAQAAIGIEVADALVNYVN 781
Cdd:PRK07574  329 GMTPHISGTTLSAQARYAAGTREILECFFE 358
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
483-780 1.12e-39

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634  Cd Length: 318  Bit Score: 149.36  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 483 DILKKQGYQIEIL-KSSLPENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNS 561
Cdd:cd12157    16 ELLKPHCEVISNQtDEPLSREELLRRCKDADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 562 PFSNSRSVAEQMIGEIISLARQI--GDRNneLHQGVWnkvsaGCWEVR-------GKTLGIVGYGHVGSQLSVLAEAMGM 632
Cdd:cd12157    96 PDLLTEPTAELTIGLLIGLGRHIlaGDRF--VRSGKF-----GGWRPKfygtgldGKTVGILGMGALGRAIARRLSGFGA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 633 RVIYYDVVNL-----MSLGTSNQvpSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALI 707
Cdd:cd12157   169 TLLYYDPHPLdqaeeQALNLRRV--ELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 708 KASQAGKLAGAALDVYPNEP--------AGNGPKFTNELNTwteelrnlkniILTPHIGGSTEEAQAAIGIEVADALVNY 779
Cdd:cd12157   247 EALKSGHLGGYAADVFEMEDwarpdrprSIPQELLDQHDRT-----------VFTPHIGSAVDEVRLEIELEAALNILQA 315

                  .
gi 1190792252 780 V 780
Cdd:cd12157   316 L 316
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
470-784 9.26e-39

Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240632  Cd Length: 314  Bit Score: 146.57  E-value: 9.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENVNKTGQDILKKQGYQIEILKSSlpENELIEKIQDVHVIgIRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLK 549
Cdd:cd12155     1 KKLLTLDYGDEKEEQIEDLGYDVDVVFED--ELSDEEDLEDIEIL-YGYNPDFDELDLAKMKNLKWIQLYSAGVDYLPLE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 550 YAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIgdrnNELHQGVWNKVsagcW-------EVRGKTLGIVGYGHVGSQ 622
Cdd:cd12155    78 YIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGL----KKAYKNQKEKK----WkmdssllELYGKTILFLGTGSIGQE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 623 LSVLAEAMGMRVIYydvVNlmslgTS-------NQVPSLDAL---LQQADFVTLHVPELPETINMISTKQFEQMKNGSYL 692
Cdd:cd12155   150 IAKRLKAFGMKVIG---VN-----TSgrdveyfDKCYPLEELdevLKEADIVVNVLPLTEETHHLFDEAFFEQMKKGALF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 693 LNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPAgngPKfTNELntWteelrNLKNIILTPHIGGSTEEAQAAIGIEV 772
Cdd:cd12155   222 INVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPL---PK-DSPL--W-----DLDNVLITPHISGVSEHFNERLFDIF 290
                         330
                  ....*....|..
gi 1190792252 773 ADALVNYVNFGT 784
Cdd:cd12155   291 YENLKSFLEDGE 302
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
486-789 1.38e-36

(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic domains; (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. HGDH is a member of the D-2-hydroxyacid NAD(+)-dependent dehydrogenase family; these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240660  Cd Length: 330  Bit Score: 140.89  E-value: 1.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 486 KKQGYQIEILKSSLpENELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFC--IGTNQVDLKYAAENGIAVFNSPF 563
Cdd:cd12184    21 KKFGYDLTLVEEYL-NDENVHLAKGHDAVIVRGNCFADKENLEIYKEYGIKYVFTrtVGFNHIDLEAAKELGFKMARVPS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 564 SNSRSVAEQMIGEIISLARQIGDRNNELHQGVWnKVSAGCW--EVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVVN 641
Cdd:cd12184   100 YSPNAIAELAFTLAMTLSRHTAYTASRTANKNF-KVDPFMFskEIRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYP 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 642 LMSLG-TSNQVpSLDALLQQADFVTLHVPELP-ETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAA 719
Cdd:cd12184   179 SDAAKdVVTFV-SLDELLKKSDIISLHVPYIKgKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFG 257
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190792252 720 LDVYPNEPAGNGPKFTNEL--NTWTEELRNL-KNIILTPHIGGSTEEAqAAIGIEVA-DALVNYVNFGTTAGAV 789
Cdd:cd12184   258 TDVLNNEKEIFFKDFDGDKieDPVVEKLLDLyPRVLLTPHIGSYTDEA-LSNMIETSyENLKEYLETGDCKNKI 330
PRK00257 PRK00257
erythronate-4-phosphate dehydrogenase; Validated
508-759 4.33e-35

erythronate-4-phosphate dehydrogenase; Validated


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 137.86  E-value: 4.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 508 IQDVHVIGIRSKTQLTANVLKHAKNLIVIGCfCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDR 587
Cdd:PRK00257   35 VRDADVLLVRSVTRVDRALLEGSRVRFVGTC-TIGTDHLDLDYFAEAGITWSSAPGCNARGVVDYVLGSLLTLAEREGVD 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 588 NNElhqgvwnkvsagcwevrgKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVVNLMSLGTSNQVpSLDALLQQADFVTLH 667
Cdd:PRK00257  114 LAE------------------RTYGVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQEAEGDGDFV-SLERILEECDVISLH 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 668 VPELPE----TINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPAGNgpkftnelntwtE 743
Cdd:PRK00257  175 TPLTKEgehpTRHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEPQID------------L 242
                         250
                  ....*....|....*.
gi 1190792252 744 ELRNLKnIILTPHIGG 759
Cdd:PRK00257  243 ELADLC-TIATPHIAG 257
PLN03139 PLN03139
formate dehydrogenase; Provisional
482-779 2.55e-32

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 129.58  E-value: 2.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 482 QDILKKQGYQ-IEILKSSLPENELIEKIQDVHVIgIRSK---TQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIA 557
Cdd:PLN03139   68 RDWLESQGHQyIVTDDKEGPDCELEKHIPDLHVL-ITTPfhpAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 558 VFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWN--KVSAGCWEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVI 635
Cdd:PLN03139  147 VAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEWNvaGIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLL 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 636 YYDVVNLMS-----LGtSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKAS 710
Cdd:PLN03139  227 YHDRLKMDPelekeTG-AKFEEDLDAMLPKCDVVVINTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADAC 305
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1190792252 711 QAGKLAGAALDVYPNEPAGNGpkftnelNTWteelRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNY 779
Cdd:PLN03139  306 SSGHIGGYGGDVWYPQPAPKD-------HPW----RYMPNHAMTPHISGTTIDAQLRYAAGVKDMLDRY 363
PRK15409 PRK15409
bifunctional glyoxylate/hydroxypyruvate reductase B; Provisional
516-794 3.13e-30

bifunctional glyoxylate/hydroxypyruvate reductase B; Provisional


Pssm-ID: 185307  Cd Length: 323  Bit Score: 122.17  E-value: 3.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 516 IRSKTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGV 595
Cdd:PRK15409   50 LGSGEKVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGE 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 596 WNKVSAGCW---EVRGKTLGIVGYGHVGSQLSVLAE-AMGMRVIYYDVVNLMSLGT--SNQVPSLDALLQQADFVTLHVP 669
Cdd:PRK15409  130 WTASIGPDWfgtDVHHKTLGIVGMGRIGMALAQRAHfGFNMPILYNARRHHKEAEErfNARYCDLDTLLQESDFVCIILP 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 670 ELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPAgngPKftnelntwTEELRNLK 749
Cdd:PRK15409  210 LTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEPL---SV--------DSPLLSLP 278
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1190792252 750 NIILTPHIGGSTEEAQAAIGIEVADALVNYVNFGTTAGAVNmPEV 794
Cdd:PRK15409  279 NVVAVPHIGSATHETRYNMAACAVDNLIDALQGKVEKNCVN-PQV 322
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
472-790 2.57e-29

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 119.46  E-value: 2.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 472 LLLENVNKTgqdilkkQGYQIEILKSSLPENELIEKIqdVHVIGIRSKTQLTAnvlkhaknlivigcfciGTNQVDLKYA 551
Cdd:PRK08605   35 LTDDNVEEV-------EGFDGLSLSQQIPLSEAIYKL--LNELGIKQIAQRSA-----------------GFDTYDLELA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 552 AENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGD--RNNELHQGVWNKvsagcwEVRGKTLG-----IVGYGHVGSQL- 623
Cdd:PRK08605   89 TKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQiqTKVREHDFRWEP------PILSRSIKdlkvaVIGTGRIGLAVa 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 624 SVLAEAMGMRVIYYDVV-NLMSLGTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVD 702
Cdd:PRK08605  163 KIFAKGYGSDVVAYDPFpNAKAATYVDYKDTIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKKGAVFVNCARGSLVD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 703 IPALIKASQAGKLAGAALDVYPNEpagnGPKFT-----NELN-TWTEELRNLKNIILTPHIGGSTEEAQAAIGIEVADAL 776
Cdd:PRK08605  243 TKALLDALDNGLIKGAALDTYEFE----RPLFPsdqrgQTINdPLLESLINREDVILTPHIAFYTDAAVKNLIVDALDAT 318
                         330
                  ....*....|....
gi 1190792252 777 VNYVNFGTTAGAVN 790
Cdd:PRK08605  319 LEVLQTGTTRLRVN 332
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
542-790 2.63e-28

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 116.55  E-value: 2.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 542 GTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGD--RNNELHQGVWnKVSAGCWEVRGKTLGIVGYGHV 619
Cdd:PRK12480   79 GFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDieRRVQAHDFTW-QAEIMSKPVKNMTVAIIGTGRI 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 620 GSQLSVLAEAMGMRVIYYDVVNLMSLGTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGT 699
Cdd:PRK12480  158 GAATAKIYAGFGATITAYDAYPNKDLDFLTYKDSVKEAIKDADIISLHVPANKESYHLFDKAMFDHVKKGAILVNAARGA 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 700 VVDIPALIKASQAGKLAGAALDVYPNEpagnGPKFTN-------ELNTWTEELRNlKNIILTPHIGGSTEEAQAAIGIEV 772
Cdd:PRK12480  238 VINTPDLIAAVNDGTLLGAAIDTYENE----AAYFTNdwtnkdiDDKTLLELIEH-ERILVTPHIAFFSDEAVQNLVEGG 312
                         250
                  ....*....|....*...
gi 1190792252 773 ADALVNYVNFGTTAGAVN 790
Cdd:PRK12480  313 LNAALSVINTGTCETRLN 330
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
469-780 6.32e-27

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 113.46  E-value: 6.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 469 IKVLLLENVnKTGQDILKKQGYQIEILKSSLPENELiekiQDVHVIGIRSKTQLTANVLKhAKNLIVIGCFCIGTNQVDL 548
Cdd:PRK15438    1 MKILVDENM-PYARELFSRLGEVKAVPGRPIPVAQL----ADADALMVRSVTKVNESLLA-GKPIKFVGTATAGTDHVDE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 549 KYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGdrnnelhqgvwnkvsagcWEVRGKTLGIVGYGHVGSQLSVLAE 628
Cdd:PRK15438   75 AWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDG------------------FSLHDRTVGIVGVGNVGRRLQARLE 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 629 AMGMRVIYYDVVNlMSLGTSNQVPSLDALLQQADFVTLHVPELPE----TINMISTKQFEQMKNGSYLLNASRGTVVDIP 704
Cdd:PRK15438  137 ALGIKTLLCDPPR-ADRGDEGDFRSLDELVQEADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNT 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1190792252 705 ALIKASQAGKLAGAALDVYPNEPagngpkftnELNTwteELRNlKNIILTPHIGGSTEEAQAAIGIEVADALVNYV 780
Cdd:PRK15438  216 ALLTCLNEGQKLSVVLDVWEGEP---------ELNV---ELLK-KVDIGTPHIAGYTLEGKARGTTQVFEAYSKFI 278
PLN02928 PLN02928
oxidoreductase family protein
500-775 2.42e-25

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 108.23  E-value: 2.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 500 PENELIEKIQDVHVIGIRSkTQLTANVLKHAKNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPFS---NSRSVAEQMIGE 576
Cdd:PLN02928   51 AREDVPDVIANYDICVPKM-MRLDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEgtgNAASCAEMAIYL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 577 IISLARqigdRNNELHQGVWNKVSAGCW--EVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYY------DVVNLMSLGTS 648
Cdd:PLN02928  130 MLGLLR----KQNEMQISLKARRLGEPIgdTLFGKTVFILGYGAIGIELAKRLRPFGVKLLATrrswtsEPEDGLLIPNG 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 649 NQVPSLD---------ALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAA 719
Cdd:PLN02928  206 DVDDLVDekgghediyEFAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLA 285
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1190792252 720 LDVypnepagngpkftnelnTWTE------ELRNLKNIILTPHIGGSTEEAQAAIGIEVADA 775
Cdd:PLN02928  286 IDV-----------------AWSEpfdpddPILKHPNVIITPHVAGVTEYSYRSMGKIVGDA 330
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
566-769 3.16e-25

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240636  Cd Length: 303  Bit Score: 106.97  E-value: 3.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 566 SRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWeVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIyydVVNLM-- 643
Cdd:cd12159    84 AETVAEHALALLLAGLRQLPARARATTWDPAEEDDLVTL-LRGSTVAIVGAGGIGRALIPLLAPFGAKVI---AVNRSgr 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 644 -SLGTSNQVPS--LDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAAL 720
Cdd:cd12159   160 pVEGADETVPAdrLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAAL 239
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1190792252 721 DVYPNEPAGNG-PkftnelnTWTEElrnlkNIILTPHIGGSTEEAQAAIG 769
Cdd:cd12159   240 DVTDPEPLPDGhP-------LWSLP-----NALITPHVANTPEVIRPLLA 277
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
562-763 8.05e-25

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240640  Cd Length: 334  Bit Score: 106.20  E-value: 8.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 562 PFSNSR-----SVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGcWEVR---GKTLGIVGYGHVGSQLSVLAEAMGMR 633
Cdd:cd12163    80 PLCTASgihgpQIAEWVIGTWLVLSHHFLQYIELQKEQTWGRRQEA-YSVEdsvGKRVGILGYGSIGRQTARLAQALGME 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 634 VIYYdvvNLMSLGT--SNQ-----VP--------------------SLDALL-QQADFVTLHVPELPETINMISTKQFEQ 685
Cdd:cd12163   159 VYAY---TRSPRPTpeSRKddgyiVPgtgdpdgsipsawfsgtdkaSLHEFLrQDLDLLVVSLPLTPATKHLLGAEEFEI 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 686 M-KNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEP--AGNgpkftnelntwteELRNLKNIILTPHIGGSTE 762
Cdd:cd12163   236 LaKRKTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEPlpADH-------------PLWSAPNVIITPHVSWQTQ 302

                  .
gi 1190792252 763 E 763
Cdd:cd12163   303 E 303
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
564-779 3.02e-24

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240657  Cd Length: 308  Bit Score: 103.96  E-value: 3.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 564 SNSRSVAEQMIGEIISLARQIgdrnnelhQGVWNKvSAGCWE------VRGKTLGIVGYGHVGSQLSVLAEAMGMRVIyy 637
Cdd:cd12180    94 VAAEAIAEFVLAAILAAAKRL--------PEIWVK-GAEQWRreplgsLAGSTLGIVGFGAIGQALARRALALGMRVL-- 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 638 dvvnlmSLGTSNQ---------VPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIK 708
Cdd:cd12180   163 ------ALRRSGRpsdvpgveaAADLAELFARSDHLVLAAPLTPETRHLINADVLAQAKPGLHLINIARGGLVDQEALLE 236
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1190792252 709 ASQAGKLAGAALDVYPNEPAGNGpkftnelntwtEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALVNY 779
Cdd:cd12180   237 ALDSGRISLASLDVTDPEPLPEG-----------HPLYTHPRVRLSPHTSAIAPDGRRNLADRFLENLARY 296
PRK06436 PRK06436
glycerate dehydrogenase; Provisional
531-782 1.85e-22

glycerate dehydrogenase; Provisional


Pssm-ID: 235800  Cd Length: 303  Bit Score: 98.80  E-value: 1.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 531 KNLIVIGCFCIGTNQVDLKYAAENGIAVFNSPfSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCweVRGKT 610
Cdd:PRK06436   48 KKTKMIQSLSAGVDHIDVSGIPENVVLCSNAG-AYSISVAEHAFALLLAWAKNICENNYNMKNGNFKQSPTKL--LYNKS 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 611 LGIVGYGHVGSQLSVLAEAMGMRVIYYdVVNLMSLGTSNQVPSLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGS 690
Cdd:PRK06436  125 LGILGYGGIGRRVALLAKAFGMNIYAY-TRSYVNDGISSIYMEPEDIMKKSDFVLISLPLTDETRGMINSKMLSLFRKGL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 691 YLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPAgngpkfTNElntwteelRNLKNIILTPHIGG--STEEAQAAI 768
Cdd:PRK06436  204 AIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPI------ITE--------TNPDNVILSPHVAGgmSGEIMQPAV 269
                         250
                  ....*....|....
gi 1190792252 769 gievADALVNYVNF 782
Cdd:PRK06436  270 ----ALAFENIKNF 279
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
527-761 8.30e-22

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240643  Cd Length: 300  Bit Score: 96.51  E-value: 8.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 527 LKHAKNLIVIGCFCIGTNQVdLKYAAEnGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEv 606
Cdd:cd12166    55 LRALPRLRVVQTLSAGYDGV-LPLLPE-GVTLCNARGVHDASTAELAVALILASLRGLPRFVRAQARGRWEPRRTPSLA- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 607 rGKTLGIVGYGHVGSQLSVLAEAMGMRVIyydvvnlmSLGTS----NQVPS---LDALLQQADFVTLHVPELPETINMIS 679
Cdd:cd12166   132 -DRRVLIVGYGSIGRAIERRLAPFEVRVT--------RVARTarpgEQVHGideLPALLPEADVVVLIVPLTDETRGLVD 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 680 TKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAgAALDVYPNE--PAGNgpkftnelntwteELRNLKNIILTPHI 757
Cdd:cd12166   203 AEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEplPPGH-------------PLWSAPGVLITPHV 268

                  ....
gi 1190792252 758 GGST 761
Cdd:cd12166   269 GGAT 272
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
470-779 1.09e-21

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240647  Cd Length: 294  Bit Score: 96.22  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 470 KVLLLENV--NKTGQDILKKQGYQIEILKSSlPEN--ELIEKIQDVHVIGIRSKTQLTANVLKHAKNLIVIGCFCI---- 541
Cdd:cd12170     3 KIVAIDPTglNEEAEEELKKYAEEVVFYDDI-PESdeEIIERIGDADCVLVSYTTQIDEEVLEACPNIKYIGMCCSlyse 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 542 -GTNqVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDrnnelHQgvWNKVSAgcwEVRGKTLGIVGYGHVG 620
Cdd:cd12170    82 eSAN-VDIAAARENGITVTGIRDYGDEGVVEYVISELIRLLHGFGG-----KQ--WKEEPR---ELTGLKVGIIGLGTTG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 621 SQLSVLAEAMGMRVIYYD---VVNLMSLGTSNQvpSLDALLQQADFVTLHvpeLPETINMISTKQFEQMKNGSYLLNASR 697
Cdd:cd12170   151 QMIADALSFFGADVYYYSrtrKPDAEAKGIRYL--PLNELLKTVDVICTC---LPKNVILLGEEEFELLGDGKILFNTSL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 698 GTVVDIPALIKASQAGKLAgaaldVYPNEPAGNGPkftnelntwTEELRNLKNIILTPHIGGSTEEAQAAIGIEVADALV 777
Cdd:cd12170   226 GPSFEVEALKKWLKASGYN-----IFDCDTAGALG---------DEELLRYPNVICTNKSAGWTRQAFERLSQKVLANLE 291

                  ..
gi 1190792252 778 NY 779
Cdd:cd12170   292 EY 293
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
610-767 8.37e-20

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240641  Cd Length: 306  Bit Score: 91.02  E-value: 8.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 610 TLGIVGYGHVGSQ-LSVLAeAMGMRVIyydvvnlmslGTSN---QVP---------SLDALLQQADFVTLHVPELPETIN 676
Cdd:cd12164   134 RVGVLGLGELGAAvARRLA-ALGFPVS----------GWSRspkDIEgvtcfhgeeGLDAFLAQTDILVCLLPLTPETRG 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 677 MISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPAGNGPKFtnelntWTEElrnlkNIILTPH 756
Cdd:cd12164   203 ILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLPADHPL------WRHP-----RVTVTPH 271
                         170
                  ....*....|.
gi 1190792252 757 IGGSTEEAQAA 767
Cdd:cd12164   272 IAAITDPDSAA 282
PLN02306 PLN02306
hydroxypyruvate reductase
541-768 1.04e-18

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 89.15  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 541 IGTNQVDLKYAAENGIAVFNSPFSNSRSVAEQMIGEIISLARQIGDRNNELHQGVWNKvsagcWE--------VRGKTLG 612
Cdd:PLN02306   95 VGYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYEG-----WLphlfvgnlLKGQTVG 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 613 IVGYGHVGSQLS-VLAEAMGMRVIYYDVVNLMSLG------------------TSNQVPSLDALLQQADFVTLHvPELPE 673
Cdd:PLN02306  170 VIGAGRIGSAYArMMVEGFKMNLIYYDLYQSTRLEkfvtaygqflkangeqpvTWKRASSMEEVLREADVISLH-PVLDK 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 674 TI-NMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPAgngpkftnelntWTEELRNLKNII 752
Cdd:PLN02306  249 TTyHLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEPY------------MKPGLADMKNAV 316
                         250
                  ....*....|....*....
gi 1190792252 753 LTPHIGGS---TEEAQAAI 768
Cdd:PLN02306  317 VVPHIASAskwTREGMATL 335
ACT_3PGDH cd04901
C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in ...
808-877 2.08e-18

C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria; The C-terminal ACT (regulatory) domain of D-3-Phosphoglycerate Dehydrogenase (3PGDH) found in fungi and bacteria. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In Escherichia coli, the SerA 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. In the homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153173 [Multi-domain]  Cd Length: 69  Bit Score: 79.86  E-value: 2.08e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1190792252 808 RVIYIHKNIPGVLRRVNEILGDH--NVDKQMTDSRGDVAYLMADISNVNISEiqqLYQSLEDLGSRIRTRVL 877
Cdd:cd04901     1 RILHIHKNVPGVLGQINTILAEHniNIAAQYLQTRGEIGYVVIDIDSEVSEE---LLEALRAIPGTIRVRLL 69
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
501-756 7.65e-18

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 84.97  E-value: 7.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 501 ENELIEKIQDVHVIgIRSKTQLTANVLKHAK--NLIVIGCFCIGTNQVDLK-YAAENGIAVFNSP-------FSNSRSVA 570
Cdd:cd12154    55 VVTLAKALWSLDVV-LKVKEPLTNAEYALIQklGDRLLFTYTIGADHRDLTeALARAGLTAIAVEgvelpllTSNSIGAG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 571 EQMIGEI-ISLARQIGDRnnelhqgvwnkvSAGCWEVRGKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDV--VNLMSLGT 647
Cdd:cd12154   134 ELSVQFIaRFLEVQQPGR------------LGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDInvEALEQLEE 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 648 --SNQVPSLDALLQQADFVTLHVPELPETINMISTKQ-FEQMKNGSYLLNASRGTVVDIPA----LIKASQAGKLAGAAL 720
Cdd:cd12154   202 lgGKNVEELEEALAEADVIVTTTLLPGKRAGILVPEElVEQMKPGSVIVNVAVGAVGCVQAlhtqLLEEGHGVVHYGDVN 281
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1190792252 721 DVYPNEPAGngpkftnelNTWTEELRNLKNII--LTPH 756
Cdd:cd12154   282 MPGPGCAMG---------VPWDATLRLAANTLpaLVKL 310
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
566-768 1.24e-16

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240637  Cd Length: 310  Bit Score: 81.65  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 566 SRSVAEQMIGEIISLARQIGDRNNELHQGVWNKVSAGCWEVRGK----TLG-----IVGYGHVGSQLSVLAEAMGMRVIy 636
Cdd:cd12160    92 DGTVAEHTLALILAAVRRLDEMREAQREHRWAGELGGLQPLRPAgrltTLLgarvlIWGFGSIGQRLAPLLTALGARVT- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 637 yDVVNlmSLGTSNQVP-----SLDALLQQADFVTLHVPELPETINMISTKQFEQMKNGSYLLNASRGTVVDIPALIKASQ 711
Cdd:cd12160   171 -GVAR--SAGERAGFPvvaedELPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALE 247
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1190792252 712 AGKLAGAALDVYPNEPAGNGPKftnelntwteeLRNLKNIILTPHI-GGSTEEAQAAI 768
Cdd:cd12160   248 SGRLGGAALDVTATEPLPASSP-----------LWDAPNLILTPHAaGGRPQGAEELI 294
ghrA PRK15469
bifunctional glyoxylate/hydroxypyruvate reductase A; Provisional
610-767 5.94e-12

bifunctional glyoxylate/hydroxypyruvate reductase A; Provisional


Pssm-ID: 185366  Cd Length: 312  Bit Score: 67.51  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 610 TLGIVGYGHVGSQLSVLAEAMGMRVIYYDvvnlMSLGTSNQVPS------LDALLQQADFVTLHVPELPETINMISTKQF 683
Cdd:PRK15469  138 TIGILGAGVLGSKVAQSLQTWGFPLRCWS----RSRKSWPGVQSfagreeLSAFLSQTRVLINLLPNTPETVGIINQQLL 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 684 EQMKNGSYLLNASRGTVVDIPALIKASQAGKLAGAALDVYPNEPagngpkFTNELNTWTEelrnlKNIILTPHIGGSTEE 763
Cdd:PRK15469  214 EQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSREP------LPPESPLWQH-----PRVAITPHVAAVTRP 282

                  ....
gi 1190792252 764 AQAA 767
Cdd:PRK15469  283 AEAV 286
ACT_3PGDH-like cd04879
ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate ...
808-877 7.57e-09

ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); ACT_3PGDH-like: The ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with or without an extended C-terminal (xct) region found in various bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback controlled by the end product L-serine in an allosteric manner. In the Escherichia coli homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. This CD also includes the C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillus, and Treponema species. LSD enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in E. coli, and other Enterobacteriales, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153151 [Multi-domain]  Cd Length: 71  Bit Score: 52.85  E-value: 7.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190792252 808 RVIYIHKNIPGVLRRVNEILGDHNVD-KQM---TDSRGDVAYLMADISNVnISEiqQLYQSLEDLGSRIRTRVL 877
Cdd:cd04879     1 RLLIVHKDVPGVIGKVGTILGEHGINiAAMqvgRKEKGGIAYMVLDVDSP-VPE--EVLEELKALPGIIRVRLI 71
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
27-267 2.85e-06

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


Pssm-ID: 341315 [Multi-domain]  Cd Length: 268  Bit Score: 49.75  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252  27 AIIFAFFSLLVTFLIIPPLVQHWRnrnigaTLCVFYAMIMNLMA--FTNAVLWPNDD-----LEHWYSGSGLCDVEVKLq 99
Cdd:cd14964     5 LILFTVLGLLGTLFVLLSFVKDRK------TPRSTRLLLASLAAcfLLASLVVLVLTfglglTEVSSRNTFLCYLVALL- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 100 iaWSVAAPATlICVLRALANAMNTDRLSLGKTKAQRWRGYAIDLTL-CVGIPLLSMVFHFIVQSK--RYFLYGISGCVPT 176
Cdd:cd14964    78 --WYLGLLAS-ILTLLVLSYHRHFMLKGRKKKTSFKRIGKTLVIILgTWGVSMLLSVLPLVGKGAigRYNGSLTGSCYLI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 177 ATQSYLTVGLIYVPPLLLVLVDAYFALLILYRLCRYRRTFSIILAHNDTTKSR-FLRLYILCIVWLLGIIPLSSWMLSVN 255
Cdd:cd14964   155 CTTIALTVGFLLVSFVLPLVACLYIFVRIVLRLSRRVQKGRSSASKNTDKNLRaAKSLLILIITFLLCWLPFSIVFILQA 234
                         250
                  ....*....|..
gi 1190792252 256 LGSQQEPYKWVE 267
Cdd:cd14964   235 LLRAGQILNLLT 246
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
608-695 2.97e-05

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 45.13  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252  608 GKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDV--VN-LMSLGTSNQVPSLDALLQQAD-FVTLhvpelpeT--INMISTK 681
Cdd:smart00997  23 GKNVVVAGYGDVGKGVAARLRGLGARVIVTEIdpIRaLEAAMDGFEVMKMEEAAKRADiFVTA-------TgnKDVITRE 95
                           90
                   ....*....|....
gi 1190792252  682 QFEQMKNGSYLLNA 695
Cdd:smart00997  96 HFRAMKDGAILANA 109
ahcY TIGR00936
adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the ...
608-706 7.02e-04

adenosylhomocysteinase; This enzyme hydrolyzes adenosylhomocysteine as part of a cycle for the regeneration of the methyl donor S-adenosylmethionine. Species that lack this enzyme are likely to have adenosylhomocysteine nucleosidase (EC 3.2.2.9), an enzyme which also acts as 5'-methyladenosine nucleosidase (see TIGR01704). [Energy metabolism, Amino acids and amines]


Pssm-ID: 213572  Cd Length: 407  Bit Score: 42.78  E-value: 7.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 608 GKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDVvnlmslgtsNQVPSLDALLQQADFVTL----HVPELPET----INMIS 679
Cdd:TIGR00936 196 GKTVVVAGYGWCGKGIAMRARGMGARVIVTEV---------DPIRALEAAMDGFRVMTMeeaaKIGDIFITatgnKDVIR 266
                          90       100
                  ....*....|....*....|....*...
gi 1190792252 680 TKQFEQMKNGSYLLNASRGTV-VDIPAL 706
Cdd:TIGR00936 267 GEHFENMKDGAIVANIGHFDVeIDVKAL 294
SAHH cd00401
S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine ...
608-706 1.25e-03

S-Adenosylhomocysteine Hydrolase, NAD-binding and catalytic domains; S-adenosyl-L-homocysteine hydrolase (SAHH, AdoHycase) catalyzes the hydrolysis of S-adenosyl-L-homocysteine (AdoHyc) to form adenosine (Ado) and homocysteine (Hcy). The equilibrium lies far on the side of AdoHyc synthesis, but in nature the removal of Ado and Hyc is sufficiently fast, so that the net reaction is in the direction of hydrolysis. Since AdoHyc is a potent inhibitor of S-adenosyl-L-methionine dependent methyltransferases, AdoHycase plays a critical role in the modulation of the activity of various methyltransferases. The enzyme forms homotetramers, with each monomer binding one molecule of NAD+.


Pssm-ID: 240619  Cd Length: 402  Bit Score: 42.06  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 608 GKTLGIVGYGHVGSQLSVLAEAMGMRVIY---------------YDVVnlmslgtsnqvPSLDALlQQAD-FVTLhvpel 671
Cdd:cd00401   195 GKVVVVAGYGWVGKGCAMRARGLGARVIVtevdpicalqaamdgFEVM-----------PMEEAA-KIGDiFVTA----- 257
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1190792252 672 peT--INMISTKQFEQMKNGSYLLNASRGTV-VDIPAL 706
Cdd:cd00401   258 --TgnKDVIRGEHFEKMKDGAILCNAGHFDVeIDVAAL 293
SAM1 COG0499
S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];
608-706 4.62e-03

S-adenosylhomocysteine hydrolase [Coenzyme transport and metabolism];


Pssm-ID: 223573  Cd Length: 420  Bit Score: 40.32  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 608 GKTLGIVGYGHVGSQLSVLAEAMGMRVIYYDV--VN-LMSLGTSNQVPSLDALLQQAD-FVTLhvpelpeT--INMISTK 681
Cdd:COG0499   209 GKNVVVAGYGWVGRGIAMRLRGMGARVIVTEVdpIRaLEAAMDGFRVMTMEEAAKTGDiFVTA-------TgnKDVIRKE 281
                          90       100
                  ....*....|....*....|....*.
gi 1190792252 682 QFEQMKNGSYLLNASRGTV-VDIPAL 706
Cdd:COG0499   282 HFEKMKDGAILANAGHFDVeIDVAGL 307
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
807-869 4.65e-03

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5.


Pssm-ID: 334705 [Multi-domain]  Cd Length: 66  Bit Score: 36.13  E-value: 4.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1190792252 807 VRVIYIHKNIPGVLRRVNEILGDHNVDKQMTDSR--GDVAYLMADISNVNISEIQQLYQSLEDLG 869
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALAERGINITSIEQRpsGDKGGIVFVVIVVDEEDLEEVLEALKKLE 65
PRK08577 PRK08577
hypothetical protein; Provisional
793-867 7.42e-03

hypothetical protein; Provisional


Pssm-ID: 236301  Cd Length: 136  Bit Score: 37.28  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190792252 793 EVTLRSLTIEEPNHVRVIYIHKNIPGVLRRVNEILGDHNVDKQMTDS----RGDVA--YLMADISN--VNISEIQQLYQS 864
Cdd:PRK08577   43 EIHLEPIALPGKKLVEIELVVEDRPGVLAKITGLLAEHGVDILATECeelkRGELAecVIIVDLSKsdIDLEELEEELKK 122

                  ...
gi 1190792252 865 LED 867
Cdd:PRK08577  123 LEE 125
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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