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Conserved domains on  [gi|1333656855|ref|XP_023495332|]
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alpha-aminoadipic semialdehyde synthase, mitochondrial isoform X2 [Equus caballus]

Protein Classification

alpha-aminoadipic semialdehyde synthase( domain architecture ID 10879610)

mitochondrial alpha-aminoadipic semialdehyde synthase (LKR/SDH) is a bifunctional enzyme that catalyzes the first two steps in lysine degradation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LKR_SDH_like cd12189
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ...
 25-466 0e+00

bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases. Along with formate dehydrogenase and similar enzymes, SDH consists paired domains resembling Rossmann folds in which the NAD-binding domain is inserted within the linear sequence of the catalytic domain. In this bifunctional enzyme, the LKR domain is N-terminal of the SDH domain. These proteins have a close match to the active site motif of SDHs, and an NAD-binding site motif that is a partial match to that found in SDH and other FDH-related proteins.


:

Pssm-ID: 240665 [Multi-domain]  Cd Length: 433  Bit Score: 777.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  25 VMALRREDVNAWERRAPLAPRHIKGIT-QLGYKVLIQPSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSK 103
Cdd:cd12189     1 VIGIRREDKNIWERRAPLTPSHVRELVkKPGVKVLVQPSNRRAFPDQEYEAAGAIIQEDLSDADLILGVKEPPIDKLLPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 104 KTYAFFSHTIKAQEANMSLLDEILKQEIRLIDYEKMVDHRGLRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHIG 183
Cdd:cd12189    81 KTYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMIDILHGLGLRLLALGYSTPFLHIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 184 MAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQDIFNELPCEYVEPHELKEVCQTG-DLRKVYG 262
Cdd:cd12189   161 RAYNYPSLEEAKQAVRDAGYEIALGGLPKSLGPLVFVFTGSGNVSQGAQEIFEELPHEYVEPSDLPELAKSGaDRNKVYG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 263 TVLSRHHHLVRKTDGVYDPVEYDKYPERYMSRFSTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLAPgkfsdagvegc 342
Cdd:cd12189   241 CVVTPEDYLERKDGGPFDRADYYANPELYESVFHEKIAPYLSVLINGIYWDPRFPRLLTNEQLQALLRP----------- 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 343 PALPHRLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAELPIEATEYFGDMLYPY 422
Cdd:cd12189   310 PAGPHRLLAIADISCDIGGSIEFLTKATTIDSPFYVYDPDTDKIHDSVSGDGILVMSVDNLPAELPREASEHFGDALLPY 389

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1333656855 423 VEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQKLR 466
Cdd:cd12189   390 VPDLAKSDASKPLEESELPPVLRRATIASNGKLTPKYEYIQELR 433
Sacchrp_dh_C pfam16653
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ...
 601-727 1.45e-55

Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


:

Pssm-ID: 465219  Cd Length: 255  Bit Score: 190.97  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 601 GLDPGLDHMLAMETIDKAKEVGATIESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPATYLLNGKVVNVAGGgs 680
Cdd:pfam16653   1 GLDPGIDHMFAIKAIDDVNAKGGKIESFLSYCGGLPAPETSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGS-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1333656855 681 flDVVTPMDYFPGLNLEGYPNRDSTKYAEIYGIPSAHTLLRGTLRYK 727
Cdd:pfam16653  79 --ELMEPIYIRPGFAFEGYPNRDSLPHEELYSLPEAKTLYRGTLRYP 123
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 482-597 4.75e-25

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


:

Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 100.36  E-value: 4.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 482 VLVLGTGYISEPVLEYLSRDDNI-EITVGSDMKNQIEQLGKK---YNINPVSVDIGKQEEKLGSLVATQDLVISLLPYVL 557
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFDVdRITVADRTLEKAQALAAKlggVRFIAVAVDADNYEAVLAALLKEGDLVVNLSPPTL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1333656855 558 HPLVAKACITNKVNMITASYITPALKELEKSVSDAGITVI 597
Cdd:pfam03435  81 SLDVLKACIETGVHYVDTSYLREAVLALHEKAKDAGVTAV 120
 
Name Accession Description Interval E-value
LKR_SDH_like cd12189
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ...
 25-466 0e+00

bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases. Along with formate dehydrogenase and similar enzymes, SDH consists paired domains resembling Rossmann folds in which the NAD-binding domain is inserted within the linear sequence of the catalytic domain. In this bifunctional enzyme, the LKR domain is N-terminal of the SDH domain. These proteins have a close match to the active site motif of SDHs, and an NAD-binding site motif that is a partial match to that found in SDH and other FDH-related proteins.


Pssm-ID: 240665 [Multi-domain]  Cd Length: 433  Bit Score: 777.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  25 VMALRREDVNAWERRAPLAPRHIKGIT-QLGYKVLIQPSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSK 103
Cdd:cd12189     1 VIGIRREDKNIWERRAPLTPSHVRELVkKPGVKVLVQPSNRRAFPDQEYEAAGAIIQEDLSDADLILGVKEPPIDKLLPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 104 KTYAFFSHTIKAQEANMSLLDEILKQEIRLIDYEKMVDHRGLRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHIG 183
Cdd:cd12189    81 KTYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMIDILHGLGLRLLALGYSTPFLHIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 184 MAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQDIFNELPCEYVEPHELKEVCQTG-DLRKVYG 262
Cdd:cd12189   161 RAYNYPSLEEAKQAVRDAGYEIALGGLPKSLGPLVFVFTGSGNVSQGAQEIFEELPHEYVEPSDLPELAKSGaDRNKVYG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 263 TVLSRHHHLVRKTDGVYDPVEYDKYPERYMSRFSTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLAPgkfsdagvegc 342
Cdd:cd12189   241 CVVTPEDYLERKDGGPFDRADYYANPELYESVFHEKIAPYLSVLINGIYWDPRFPRLLTNEQLQALLRP----------- 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 343 PALPHRLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAELPIEATEYFGDMLYPY 422
Cdd:cd12189   310 PAGPHRLLAIADISCDIGGSIEFLTKATTIDSPFYVYDPDTDKIHDSVSGDGILVMSVDNLPAELPREASEHFGDALLPY 389

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1333656855 423 VEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQKLR 466
Cdd:cd12189   390 VPDLAKSDASKPLEESELPPVLRRATIASNGKLTPKYEYIQELR 433
PLN02819 PLN02819
lysine-ketoglutarate reductase/saccharopine dehydrogenase
 25-731 0e+00

lysine-ketoglutarate reductase/saccharopine dehydrogenase


Pssm-ID: 215439 [Multi-domain]  Cd Length: 1042  Bit Score: 604.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855   25 VMALRREDVNAWERRAPLAPRHIKGITQLGY-----KVLIQPSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEK 99
Cdd:PLN02819     7 VVGILAETVNKWERRAPLTPSHCARLLHSGKdrtvsRIIVQPSSKRIHHDAQYEDVGCEISEDLSDCGLILGVKQPKLEM 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  100 LMSKKTYAFFSHTIKAQEANMSLLDEILKQEIRLIDYEKMVDHRGLRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPF 179
Cdd:PLN02819    87 LLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKYAGRAGMIDFFRGLGQRLLSLGYSTPF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  180 MHIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQDIFNELPCEYVEPHELKEVCQ------ 253
Cdd:PLN02819   167 LSLGSSYMYSSLAAAKAAVISVGEEIASSGLPLGICPLVFVFTGSGNVSQGAQEIFKLLPHTFVEPSKLPELKGisqnki 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  254 -TGDLRKVYGTVLSRHHHLVRKTDG-VYDPVEYDKYPERYMSRFSTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLAP 331
Cdd:PLN02819   247 sTKRVYQVYGCVVTSQDMVEHKDPSkQFDKADYYAHPEHYNPVFHEKIAPYASVIVNCMYWEKRFPRLLTTKQLQDLTRK 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  332 GkfsdagveGCPalphrLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAELPIEA 411
Cdd:PLN02819   327 G--------GCP-----LVGVCDITCDIGGSIEFLNKTTSIEKPFFRYNPSNNSYHDDMDGDGILCMAVDILPTEFAKEA 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  412 TEYFGDMLYPYVEEMIlsDATQPLEsqnFSPVVRDAVITSNGTLPDKYKYIQKLRES--RERTQTLSGTKK--------- 480
Cdd:PLN02819   394 SQHFGNILSPFVGSLA--SMKELAE---LPSHLRRACIAHRGSLTPLFEYIPRMRNSnaELAQDTVSSQSTfnilvslsg 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855      --------------------------------------------------------------------------------
Cdd:PLN02819   469 hlfdkflinealdvieaaggsfhlakcqvgqsadaesyselevgaddkevldqiidsltrlanpnedyispareankifl 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  481 ----------------------KVLVLGTGYISEPVLEYLSR-------------DDNIEITVGSD-MKNQIEQLGKKYN 524
Cdd:PLN02819   549 kigkvqqenecnekaevtkksqNVLILGAGRVCRPAAEYLASvktisyygddseePTDVHVIVASLyLKDAKETVEGIEN 628

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  525 INPVSVDIgKQEEKLGSLVATQDLVISLLPYVLHPLVAKACITNKVNMITASYITPALKELEKSVSDAGITVIGELGLDP 604
Cdd:PLN02819   629 AEAVQLDV-SDSESLLKYVSQVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITILCEMGLDP 707

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  605 GLDHMLAMETIDKAKEVGATIESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPATYLLNGKVVNVAGGGSFLDV 684
Cdd:PLN02819   708 GIDHMMAMKMIDDAHERGGKVKSFTSYCGGLPSPEAANNPLAYKFSWNPAGAIKAGQNPAVYKSNGQIIHVDGENLFASA 787

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*....
gi 1333656855  685 VT-PMDYFPGLNLEGYPNRDSTKYAEIYGI-PSAHTLLRGTLRYKILSS 731
Cdd:PLN02819   788 VRfRLPNLPAFALECLPNRDSLVYGELYGIeKEAATIFRGTLRYEGFSM 836
Sacchrp_dh_C pfam16653
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ...
 601-727 1.45e-55

Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 465219  Cd Length: 255  Bit Score: 190.97  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 601 GLDPGLDHMLAMETIDKAKEVGATIESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPATYLLNGKVVNVAGGgs 680
Cdd:pfam16653   1 GLDPGIDHMFAIKAIDDVNAKGGKIESFLSYCGGLPAPETSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGS-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1333656855 681 flDVVTPMDYFPGLNLEGYPNRDSTKYAEIYGIPSAHTLLRGTLRYK 727
Cdd:pfam16653  79 --ELMEPIYIRPGFAFEGYPNRDSLPHEELYSLPEAKTLYRGTLRYP 123
Lys9 COG1748
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ...
 505-726 1.57e-37

Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441354 [Multi-domain]  Cd Length: 352  Bit Score: 143.82  E-value: 1.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 505 EITVGSDMKNQIEQLGKKY-NINPVSVDIGkQEEKLGSLVATQDLVISLLPYVLHPLVAKACITNKVNMITASYITPALK 583
Cdd:COG1748     2 EVTLADRSLEKAEALAASGpKVEAAQLDAS-DPEALAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEPETE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 584 ---ELEKSVSDAGITVIGELGLDPGLDHMLAMETIDKAKEvgatIESYVSYCGGLPAPEhsDNPLRYKFSWSPVGVLMNI 660
Cdd:COG1748    81 aklALDELAKEAGVTAIPGCGLAPGLSNVLAAYAADRFDE----IDSIDIRVGGLPGYP--SNPLNYGTTWSPEGVIREY 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333656855 661 MQPATYLLNGKVVnvagggsfldVVTPMD-----YFPGL-NLEGYPNRDSTKY-AEIYgiPSAHTLLRGTLRY 726
Cdd:COG1748   155 TNPARAIEDGKWV----------EVPPLSeretiDFPGVgRYEAYNTDGELETlPETY--PGVKTVRFKTGRY 215
AlaDh_PNT_N pfam05222
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ...
 27-157 1.49e-31

Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 461595 [Multi-domain]  Cd Length: 135  Bit Score: 119.45  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  27 ALRREdVNAWERRAPLAPRHIKGITQLGYKVLIQPSN--RRAIHDKDYVKAGGILQ----EDISEACLILGVKRP--PEE 98
Cdd:pfam05222   1 GVPKE-IKPGERRVALTPAGVKKLVKLGHEVLVESGAglGAGFSDEAYEAAGAEIVdtaaEVWAEADLILKVKEPqpEEY 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  99 KLMSK-KTYAFFSHTIkaqeANMSLLDEILKQEIRLIDYEKMVDHRGLRVVAFGQWAGVA 157
Cdd:pfam05222  80 ALLREgQTLITFLHPA----ANPELLEALAAKGVTAIAYETVPRSRGQSLDALSSMANIA 135
AlaDh_PNT_N smart01003
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ...
 27-155 4.65e-26

Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214967 [Multi-domain]  Cd Length: 133  Bit Score: 104.03  E-value: 4.65e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855   27 ALRREDVNaWERRAPLAPRHIKGITQLGYKVLIQPSN--RRAIHDKDYVKAGGILQED---ISEACLILGVKRP-PEEKL 100
Cdd:smart01003   1 GVPKEIKP-GERRVALTPAGVKKLVKLGHEVLVESGAgeGAGFSDEAYEAAGAEIVDTaevWADADIILKVKEPsPEELA 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333656855  101 MSKKTYAFFSHtiKAQEANMSLLDEILKQEIRLIDYEKMV-DHRGLRVVAFGQWAG 155
Cdd:smart01003  80 LLREGQILFGY--LHPAANPELLEALAAKGVTAIAYETVPrISRAQSLDALSSMAE 133
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 482-597 4.75e-25

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 100.36  E-value: 4.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 482 VLVLGTGYISEPVLEYLSRDDNI-EITVGSDMKNQIEQLGKK---YNINPVSVDIGKQEEKLGSLVATQDLVISLLPYVL 557
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFDVdRITVADRTLEKAQALAAKlggVRFIAVAVDADNYEAVLAALLKEGDLVVNLSPPTL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1333656855 558 HPLVAKACITNKVNMITASYITPALKELEKSVSDAGITVI 597
Cdd:pfam03435  81 SLDVLKACIETGVHYVDTSYLREAVLALHEKAKDAGVTAV 120
 
Name Accession Description Interval E-value
LKR_SDH_like cd12189
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ...
 25-466 0e+00

bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases. Along with formate dehydrogenase and similar enzymes, SDH consists paired domains resembling Rossmann folds in which the NAD-binding domain is inserted within the linear sequence of the catalytic domain. In this bifunctional enzyme, the LKR domain is N-terminal of the SDH domain. These proteins have a close match to the active site motif of SDHs, and an NAD-binding site motif that is a partial match to that found in SDH and other FDH-related proteins.


Pssm-ID: 240665 [Multi-domain]  Cd Length: 433  Bit Score: 777.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  25 VMALRREDVNAWERRAPLAPRHIKGIT-QLGYKVLIQPSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSK 103
Cdd:cd12189     1 VIGIRREDKNIWERRAPLTPSHVRELVkKPGVKVLVQPSNRRAFPDQEYEAAGAIIQEDLSDADLILGVKEPPIDKLLPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 104 KTYAFFSHTIKAQEANMSLLDEILKQEIRLIDYEKMVDHRGLRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHIG 183
Cdd:cd12189    81 KTYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMIDILHGLGLRLLALGYSTPFLHIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 184 MAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQDIFNELPCEYVEPHELKEVCQTG-DLRKVYG 262
Cdd:cd12189   161 RAYNYPSLEEAKQAVRDAGYEIALGGLPKSLGPLVFVFTGSGNVSQGAQEIFEELPHEYVEPSDLPELAKSGaDRNKVYG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 263 TVLSRHHHLVRKTDGVYDPVEYDKYPERYMSRFSTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLAPgkfsdagvegc 342
Cdd:cd12189   241 CVVTPEDYLERKDGGPFDRADYYANPELYESVFHEKIAPYLSVLINGIYWDPRFPRLLTNEQLQALLRP----------- 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 343 PALPHRLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAELPIEATEYFGDMLYPY 422
Cdd:cd12189   310 PAGPHRLLAIADISCDIGGSIEFLTKATTIDSPFYVYDPDTDKIHDSVSGDGILVMSVDNLPAELPREASEHFGDALLPY 389

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1333656855 423 VEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQKLR 466
Cdd:cd12189   390 VPDLAKSDASKPLEESELPPVLRRATIASNGKLTPKYEYIQELR 433
PLN02819 PLN02819
lysine-ketoglutarate reductase/saccharopine dehydrogenase
 25-731 0e+00

lysine-ketoglutarate reductase/saccharopine dehydrogenase


Pssm-ID: 215439 [Multi-domain]  Cd Length: 1042  Bit Score: 604.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855   25 VMALRREDVNAWERRAPLAPRHIKGITQLGY-----KVLIQPSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEK 99
Cdd:PLN02819     7 VVGILAETVNKWERRAPLTPSHCARLLHSGKdrtvsRIIVQPSSKRIHHDAQYEDVGCEISEDLSDCGLILGVKQPKLEM 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  100 LMSKKTYAFFSHTIKAQEANMSLLDEILKQEIRLIDYEKMVDHRGLRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPF 179
Cdd:PLN02819    87 LLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKYAGRAGMIDFFRGLGQRLLSLGYSTPF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  180 MHIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQDIFNELPCEYVEPHELKEVCQ------ 253
Cdd:PLN02819   167 LSLGSSYMYSSLAAAKAAVISVGEEIASSGLPLGICPLVFVFTGSGNVSQGAQEIFKLLPHTFVEPSKLPELKGisqnki 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  254 -TGDLRKVYGTVLSRHHHLVRKTDG-VYDPVEYDKYPERYMSRFSTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLAP 331
Cdd:PLN02819   247 sTKRVYQVYGCVVTSQDMVEHKDPSkQFDKADYYAHPEHYNPVFHEKIAPYASVIVNCMYWEKRFPRLLTTKQLQDLTRK 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  332 GkfsdagveGCPalphrLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAELPIEA 411
Cdd:PLN02819   327 G--------GCP-----LVGVCDITCDIGGSIEFLNKTTSIEKPFFRYNPSNNSYHDDMDGDGILCMAVDILPTEFAKEA 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  412 TEYFGDMLYPYVEEMIlsDATQPLEsqnFSPVVRDAVITSNGTLPDKYKYIQKLRES--RERTQTLSGTKK--------- 480
Cdd:PLN02819   394 SQHFGNILSPFVGSLA--SMKELAE---LPSHLRRACIAHRGSLTPLFEYIPRMRNSnaELAQDTVSSQSTfnilvslsg 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855      --------------------------------------------------------------------------------
Cdd:PLN02819   469 hlfdkflinealdvieaaggsfhlakcqvgqsadaesyselevgaddkevldqiidsltrlanpnedyispareankifl 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  481 ----------------------KVLVLGTGYISEPVLEYLSR-------------DDNIEITVGSD-MKNQIEQLGKKYN 524
Cdd:PLN02819   549 kigkvqqenecnekaevtkksqNVLILGAGRVCRPAAEYLASvktisyygddseePTDVHVIVASLyLKDAKETVEGIEN 628

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  525 INPVSVDIgKQEEKLGSLVATQDLVISLLPYVLHPLVAKACITNKVNMITASYITPALKELEKSVSDAGITVIGELGLDP 604
Cdd:PLN02819   629 AEAVQLDV-SDSESLLKYVSQVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITILCEMGLDP 707

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  605 GLDHMLAMETIDKAKEVGATIESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPATYLLNGKVVNVAGGGSFLDV 684
Cdd:PLN02819   708 GIDHMMAMKMIDDAHERGGKVKSFTSYCGGLPSPEAANNPLAYKFSWNPAGAIKAGQNPAVYKSNGQIIHVDGENLFASA 787

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*....
gi 1333656855  685 VT-PMDYFPGLNLEGYPNRDSTKYAEIYGI-PSAHTLLRGTLRYKILSS 731
Cdd:PLN02819   788 VRfRLPNLPAFALECLPNRDSLVYGELYGIeKEAATIFRGTLRYEGFSM 836
SDH_like cd05199
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ...
 25-424 2.65e-90

Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related proteins, including bifunctional lysine ketoglutarate reductase/SDH enzymes and N(5)-(carboxyethyl)ornithine synthases. SDH catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SDH is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure. Bifunctional lysine ketoglutarate reductase/SDH protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases.


Pssm-ID: 240623 [Multi-domain]  Cd Length: 319  Bit Score: 285.67  E-value: 2.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  25 VMALRREDVNAWERRAPLAPRHIKGITQLGY--KVLIQPSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMS 102
Cdd:cd05199     1 KIGIIREGKTPPDRRVPLTPEQCKELQAKYPgvEIFVQPSPVRCFKDEEYRAAGIEVVEDLSDCDILLGVKEVPIEQLIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 103 KKTYAFFSHTIKAQEANMSLLDEILKQEIRLIDYEKMVDHRGLRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFmhi 182
Cdd:cd05199    81 NKTYFFFSHTIKKQPYNRKLLQTILEKNITLIDYEVLVDEQGKRVIAFGRYAGIVGAYNGLRAYGKKTGLFDLKRAH--- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 183 gmahnyrnssqavqAVRDAGYEISLGLmPKSIGPLTFVFTGTGNVSKGAQDIFNELPCEYVEPHELKEVcqtgdlrkvyg 262
Cdd:cd05199   158 --------------ECSDLEELIAELK-KVGLPPPKIVITGSGRVGSGAAEVLKALGIKEVSPEDFLTV----------- 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 263 tvlsrhhhlvrktdgvydpveydkyperymsrfsTDIapyttcLINGIYWEQNTPRLLTRQDAQSLlapgKFsdagvegc 342
Cdd:cd05199   212 ----------------------------------ADI------LINGHYWDKRAPRLFTKEDLKKP----DF-------- 239

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 343 palphRLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAELPIEATEYFGDMLYPY 422
Cdd:cd05199   240 -----KIRVIADVTCDIHGSIPSTLRASTIADPVYDYDPTTNKEVAFSSPDSITVMAVDNLPCELPRDASEDFGEQLIKS 314


                  ..
gi 1333656855 423 VE 424
Cdd:cd05199   315 VL 316
Sacchrp_dh_C pfam16653
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ...
 601-727 1.45e-55

Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 465219  Cd Length: 255  Bit Score: 190.97  E-value: 1.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 601 GLDPGLDHMLAMETIDKAKEVGATIESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPATYLLNGKVVNVAGGgs 680
Cdd:pfam16653   1 GLDPGIDHMFAIKAIDDVNAKGGKIESFLSYCGGLPAPETSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGS-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1333656855 681 flDVVTPMDYFPGLNLEGYPNRDSTKYAEIYGIPSAHTLLRGTLRYK 727
Cdd:pfam16653  79 --ELMEPIYIRPGFAFEGYPNRDSLPHEELYSLPEAKTLYRGTLRYP 123
Lys9 COG1748
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ...
 505-726 1.57e-37

Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441354 [Multi-domain]  Cd Length: 352  Bit Score: 143.82  E-value: 1.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 505 EITVGSDMKNQIEQLGKKY-NINPVSVDIGkQEEKLGSLVATQDLVISLLPYVLHPLVAKACITNKVNMITASYITPALK 583
Cdd:COG1748     2 EVTLADRSLEKAEALAASGpKVEAAQLDAS-DPEALAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEPETE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 584 ---ELEKSVSDAGITVIGELGLDPGLDHMLAMETIDKAKEvgatIESYVSYCGGLPAPEhsDNPLRYKFSWSPVGVLMNI 660
Cdd:COG1748    81 aklALDELAKEAGVTAIPGCGLAPGLSNVLAAYAADRFDE----IDSIDIRVGGLPGYP--SNPLNYGTTWSPEGVIREY 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333656855 661 MQPATYLLNGKVVnvagggsfldVVTPMD-----YFPGL-NLEGYPNRDSTKY-AEIYgiPSAHTLLRGTLRY 726
Cdd:COG1748   155 TNPARAIEDGKWV----------EVPPLSeretiDFPGVgRYEAYNTDGELETlPETY--PGVKTVRFKTGRY 215
AlaDh_PNT_N pfam05222
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ...
 27-157 1.49e-31

Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 461595 [Multi-domain]  Cd Length: 135  Bit Score: 119.45  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  27 ALRREdVNAWERRAPLAPRHIKGITQLGYKVLIQPSN--RRAIHDKDYVKAGGILQ----EDISEACLILGVKRP--PEE 98
Cdd:pfam05222   1 GVPKE-IKPGERRVALTPAGVKKLVKLGHEVLVESGAglGAGFSDEAYEAAGAEIVdtaaEVWAEADLILKVKEPqpEEY 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  99 KLMSK-KTYAFFSHTIkaqeANMSLLDEILKQEIRLIDYEKMVDHRGLRVVAFGQWAGVA 157
Cdd:pfam05222  80 ALLREgQTLITFLHPA----ANPELLEALAAKGVTAIAYETVPRSRGQSLDALSSMANIA 135
SDH cd12188
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ...
 30-425 1.14e-28

Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SHD is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure.


Pssm-ID: 240664 [Multi-domain]  Cd Length: 351  Bit Score: 118.10  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  30 REDVNAWERRAPLAPRHIKGITQLGYKVLIQPSNRRAIHDKDYVKAGGILQEDIS-----EACLILGVKRPPEEKLMSKK 104
Cdd:cd12188     6 RAETKPLERRTALTPTTAKKLLDAGFKVTVERSPQRIFPDEEYEAVGCELVPAGSwvnapKDAIILGLKELPEDTFPLPH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 105 TYAFFSHTIKAQEAnmslLDEILKQEIR----LIDYEKMVDHRGLRVVAFGQWAGVAGMinilhGMGLRLLA--LGHHTP 178
Cdd:cd12188    86 RHIYFAHAYKGQAG----WKDVLSRFARgggtLLDLEYLVDDDGRRVAAFGYWAGFAGA-----ALGLLAWAhqQLGPVT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 179 FmhiGMAHNYRNSSQAVQAVRDAgyEISLGLMPKS--IGPLtfvftgtGNVSKGAQDIFNELPCEyVEPHELKEVCQTGD 256
Cdd:cd12188   157 L---PPVSPYPNEEALVADVKKA--LATGGRKPRAlvIGAL-------GRCGSGAVDLLEAAGIE-VTKWDMAETKAGGP 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 257 lrkvygtvlsrhhhlvrktdgvydpveydkYPERYMSrfstDIapyttcLINGIYWEQNTPRLLTRQDaqsLLAPGkfsd 336
Cdd:cd12188   224 ------------------------------FPEILDH----DI------FVNCIYLSKPIPPFLTPEM---LQAPG---- 256

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 337 agvegcpalpHRLVAICDISADTGGS---IEFMTECTTIEHPfcmydadqhIIHDSVEGSGILMCSIDNLPAELPIEATE 413
Cdd:cd12188   257 ----------RRLRVIGDVSCDPTNPynpIPIYDVATTFDKP---------TLRVPTGGPPLDVIAIDHLPSLLPRESSE 317

                         410
                  ....*....|..
gi 1333656855 414 YFGDMLYPYVEE 425
Cdd:cd12188   318 DFSNDLLPSLLE 329
AlaDh_PNT_N smart01003
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ...
 27-155 4.65e-26

Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214967 [Multi-domain]  Cd Length: 133  Bit Score: 104.03  E-value: 4.65e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855   27 ALRREDVNaWERRAPLAPRHIKGITQLGYKVLIQPSN--RRAIHDKDYVKAGGILQED---ISEACLILGVKRP-PEEKL 100
Cdd:smart01003   1 GVPKEIKP-GERRVALTPAGVKKLVKLGHEVLVESGAgeGAGFSDEAYEAAGAEIVDTaevWADADIILKVKEPsPEELA 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333656855  101 MSKKTYAFFSHtiKAQEANMSLLDEILKQEIRLIDYEKMV-DHRGLRVVAFGQWAG 155
Cdd:smart01003  80 LLREGQILFGY--LHPAANPELLEALAAKGVTAIAYETVPrISRAQSLDALSSMAE 133
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 482-597 4.75e-25

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 100.36  E-value: 4.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 482 VLVLGTGYISEPVLEYLSRDDNI-EITVGSDMKNQIEQLGKK---YNINPVSVDIGKQEEKLGSLVATQDLVISLLPYVL 557
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFDVdRITVADRTLEKAQALAAKlggVRFIAVAVDADNYEAVLAALLKEGDLVVNLSPPTL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1333656855 558 HPLVAKACITNKVNMITASYITPALKELEKSVSDAGITVI 597
Cdd:pfam03435  81 SLDVLKACIETGVHYVDTSYLREAVLALHEKAKDAGVTAV 120
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 197-385 2.87e-22

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 93.73  E-value: 2.87e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  197 AVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQDIFNELPCE----YVEPHELKEVcqtgdlRKVYGTVLsrhhhlv 272
Cdd:smart01002   1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEvtvlDVRPARLRQL------ESLLGARF------- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  273 rktdgvydpveydkYPERYMSRFSTDIAPYTTCLINGIYWE-QNTPRLLTRQDAQSLlAPGkfsdagvegcpalphrlVA 351
Cdd:smart01002  68 --------------TTLYSQAELLEEAVKEADLVIGAVLIPgAKAPKLVTREMVKSM-KPG-----------------SV 115

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1333656855  352 ICDISADTGGSIEFmTECTTIEHPFCMYDADQHI 385
Cdd:smart01002 116 IVDVAADQGGCIET-SRPTTHDDPTYVVDGVVHY 148
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 37-427 2.11e-11

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 65.89  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  37 ERRAPLAPRHIKGITQLGYKVLIQ--PSNRRAIHDKDYVKAGGIL----QEDISEACLILGVKRPPE-EKLMSKKTYAFF 109
Cdd:cd01620    12 EFRVALTPSFVKKLVANGFKVYIEtgAGSGAGFSDEDYLQAGAQIvpaaSKEAYSADIIVKLKEPEFaEYDLIKKGQLLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 110 SHTIKAQEAnmSLLDEILKQEIRLIDYEKMVDHRGLRVVAFGQWAGVAGMInilhgMGLRLLALGHhtpfmhiGMAHNYR 189
Cdd:cd01620    92 TFLHAATNR--GVVEVLMRKKLTAYALEDLENDFRPRLAPNSNIAGYAGVQ-----LGAYELARIQ-------GGRMGGA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 190 NSSqavqavrdagyeislglmpksiGPLTFVFTGTGNVSKGAQDIFNELpceyvephelkevcqtGDLRKVYGTVLSRHH 269
Cdd:cd01620   158 GGV----------------------PPAKVLIIGAGVVGLGAAKIAKKL----------------GANVLVYDIKEEKLK 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 270 HLvrKTDGVYDPVEYDKY-PERYMSRfsTDIapyttcLINGIYWE-QNTPRLLTrqdaQSLLAPGKfsdagvegcpalPH 347
Cdd:cd01620   200 GV--ETLGGSRLRYSQKEeLEKELKQ--TDI------LINAILVDgPRAPILIM----EELVGPMK------------RG 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 348 RLvaICDISADTGGSIEfMTECTTIEHPfcmydadqhiihdSVEGSGILMCSIDNLPAELPIEATEYFGDMLYPYVEEMI 427
Cdd:cd01620   254 AV--IVDLAADQGGNDE-TSIPTTEGVP-------------TYEVDGVVIYGVDNMPSLVPREASELLSKNLLPYLVKLA 317
ceo_syn cd12181
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ...
 37-429 5.96e-08

N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) catalyzes the NADP-dependent conversion of N5-(L-1-carboxyethyl)-L-ornithine to L-ornithine + pyruvate. Ornithine plays a key role in the urea cycle, which in mammals is used in arginine biosynthesis, and is a precursor in polyamine synthesis. ceo_syn is related to the NAD-dependent L-alanine dehydrogenases. Like formate dehydrogenase and related enzymes, ceo_syn is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. These ceo_syn proteins have a partially conserved NAD-binding motif and active site residues that are characteristic of related enzymes such as Saccharopine Dehydrogenase.


Pssm-ID: 240658 [Multi-domain]  Cd Length: 295  Bit Score: 54.93  E-value: 5.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  37 ERRAPLAPRHIKGItQLGYKVLIQPS--NRRAIHDKDYVKAG-GIL--QEDISEACLILGVKrPPEEKLMSKK---TYAF 108
Cdd:cd12181    13 EKRVPLLPADLERI-PLREQLYFEEGygERLGISDEEYAALGaGIVsrEEILAKCDVICDPK-PGDADYLEILegqILWG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 109 FSHTIKAQEANMSLLDEILkqeiRLIDYEKMVDHRGLRVVAFGQWAGVAGMINILHGMGLRllalghhtpfmhigmahny 188
Cdd:cd12181    91 WVHCVQDKEITQLAIDKKL----TLIAWEDMFEWSKIGRHVFYKNNELAGYAAVLHALQLY------------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 189 rnssqavqavrdagyeislGLMPKSigPLTFVFTGTGNVSKGAQDIFNelpceyvepHELKEVcqtgdlrKVYGtvlSRH 268
Cdd:cd12181   148 -------------------GITPYR--QTKVAVLGFGNTARGAIRALK---------LGGADV-------TVYT---RRT 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 269 HHLVRKtdgvydpvEYDKYperymsrfstDIapyttcLINGIYWEQNTP-RLLTRQDaQSLLAPGKFsdagvegcpalph 347
Cdd:cd12181   188 EALFKE--------ELSEY----------DI------IVNCILQDTDRPdHIIYEED-LKRLKPGAL------------- 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855 348 rlvaICDISADTGGSIEFmTECTTIEHPfcMYDADqHIIHDSVegsgilmcsiDNLPAELPIEATEYFGDMLYPYVEEMI 427
Cdd:cd12181   230 ----IIDVSCDEGMGIEF-AKPTTFDDP--IYKVD-GIDYYAV----------DHTPSLFYRSASRSISKALAPYLDTVI 291


                  ..
gi 1333656855 428 LS 429
Cdd:cd12181   292 EG 293
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 37-98 5.72e-05

Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.


Pssm-ID: 240629 [Multi-domain]  Cd Length: 363  Bit Score: 45.86  E-value: 5.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333656855  37 ERRAPLAPRHIKGITQLGYKVLIQP-SNRRA-IHDKDYVKAGGIL---QEDISEACLILGVKRPPEE 98
Cdd:cd05304    13 ERRVALTPETVKKLVKLGFEVLVESgAGEAAgFSDEAYEEAGAEIvsdAEELAQADIVLKVRPPSEE 79
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 37-144 5.69e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 39.70  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333656855  37 ERRAPLAPRHIKGITQLGYKVLIQ-----PSNrraIHDKDYVKAGGIL---QEDI-SEACLILGVKRP-PEE-KLMSKKT 105
Cdd:cd05305    13 ENRVALTPAGVAELVAAGHEVLVEkgaglGSG---FSDEEYSEAGAEIvptAEEVwAKADLIVKVKEPlPEEyDLLREGQ 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1333656855 106 --YAFFsHtIKAQEAnmsLLDEILKQEIRLIDYEKMVDHRG 144
Cdd:cd05305    90 ilFTYL-H-LAADKE---LTEALLEKKVTAIAYETIEDEDG 125
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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