|
Name |
Accession |
Description |
Interval |
E-value |
| LKR_SDH_like |
cd12189 |
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ... |
19-460 |
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: 775.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 19 VMALRREDVNAWERRAPLAPRHIKGIT-NLGYKVLIQPSNRRAIHDKEYVKAGGILQEDISEACLILGVKRPPEEKLMSK 97
Cdd:cd12189 1 VIGIRREDKNIWERRAPLTPSHVRELVkKPGVKVLVQPSNRRAFPDQEYEAAGAIIQEDLSDADLILGVKEPPIDKLLPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 98 KTYAFFSHTIKAQEANMGLLDEILRQEIRLIDYEKMVDHRGTRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHIG 177
Cdd:cd12189 81 KTYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMIDILHGLGLRLLALGYSTPFLHIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 178 MAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEIFNELPCEYVEPHELKEVSQNG-DLRKVYG 256
Cdd:cd12189 161 RAYNYPSLEEAKQAVRDAGYEIALGGLPKSLGPLVFVFTGSGNVSQGAQEIFEELPHEYVEPSDLPELAKSGaDRNKVYG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 257 TVLSRHHHLVRKTDGVYDPVEYDKYPERYISRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDVQSLLVPgkssvagvegc 336
Cdd:cd12189 241 CVVTPEDYLERKDGGPFDRADYYANPELYESVFHEKIAPYLSVLINGIYWDPRFPRLLTNEQLQALLRP----------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 337 PALPHKLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATEYFGDMLYPY 416
Cdd:cd12189 310 PAGPHRLLAIADISCDIGGSIEFLTKATTIDSPFYVYDPDTDKIHDSVSGDGILVMSVDNLPAELPREASEHFGDALLPY 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1952982102 417 VEEMILSDATQPLESQNFSPVVRDAVITSNGVLPDKYKYIQKLR 460
Cdd:cd12189 390 VPDLAKSDASKPLEESELPPVLRRATIASNGKLTPKYEYIQELR 433
|
|
| PLN02819 |
PLN02819 |
lysine-ketoglutarate reductase/saccharopine dehydrogenase |
19-910 |
0e+00 |
|
lysine-ketoglutarate reductase/saccharopine dehydrogenase
Pssm-ID: 215439 [Multi-domain] Cd Length: 1042 Bit Score: 715.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 19 VMALRREDVNAWERRAPLAPRHIKGITNLGY-----KVLIQPSNRRAIHDKEYVKAGGILQEDISEACLILGVKRPPEEK 93
Cdd:PLN02819 7 VVGILAETVNKWERRAPLTPSHCARLLHSGKdrtvsRIIVQPSSKRIHHDAQYEDVGCEISEDLSDCGLILGVKQPKLEM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 94 LMSKKTYAFFSHTIKAQEANMGLLDEILRQEIRLIDYEKMVDHRGTRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPF 173
Cdd:PLN02819 87 LLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKYAGRAGMIDFFRGLGQRLLSLGYSTPF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 174 MHIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEIFNELPCEYVEPHELKEVSQ------ 247
Cdd:PLN02819 167 LSLGSSYMYSSLAAAKAAVISVGEEIASSGLPLGICPLVFVFTGSGNVSQGAQEIFKLLPHTFVEPSKLPELKGisqnki 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 248 -NGDLRKVYGTVLSRHHHLVRKTDG-VYDPVEYDKYPERYISRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDVQSLLVP 325
Cdd:PLN02819 247 sTKRVYQVYGCVVTSQDMVEHKDPSkQFDKADYYAHPEHYNPVFHEKIAPYASVIVNCMYWEKRFPRLLTTKQLQDLTRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 326 GkssvagveGCPalphkLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEA 405
Cdd:PLN02819 327 G--------GCP-----LVGVCDITCDIGGSIEFLNKTTSIEKPFFRYNPSNNSYHDDMDGDGILCMAVDILPTEFAKEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 406 TEYFGDMLYPYVEEMIlsDATQPLEsqnFSPVVRDAVITSNGVLPDKYKYIQKLRES-RELAQ-------------SLS- 470
Cdd:PLN02819 394 SQHFGNILSPFVGSLA--SMKELAE---LPSHLRRACIAHRGSLTPLFEYIPRMRNSnAELAQdtvssqstfnilvSLSg 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 --------------------------------------------------------------------------------
Cdd:PLN02819 469 hlfdkflinealdvieaaggsfhlakcqvgqsadaesyselevgaddkevldqiidsltrlanpnedyispareankifl 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 471 ----------------MGTK-KRVLVLGSGYVSEPVLEYLSR-------------DNRIDITVGSD-MKDQIEQLGKKYN 519
Cdd:PLN02819 549 kigkvqqenecnekaeVTKKsQNVLILGAGRVCRPAAEYLASvktisyygddseePTDVHVIVASLyLKDAKETVEGIEN 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 520 INPVSMDISkQEEKLSSLVAKQDLVISLLPYALHPLVAKACIRSKVDMITASYITPELKELEKSVEDAGITVIGELGLDP 599
Cdd:PLN02819 629 AEAVQLDVS-DSESLLKYVSQVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITILCEMGLDP 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 600 GLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSDNPLRYKFSWSPLGVLTNMMQPATYLLDGKVVTVAGGIPFLDA 679
Cdd:PLN02819 708 GIDHMMAMKMIDDAHERGGKVKSFTSYCGGLPSPEAANNPLAYKFSWNPAGAIKAGQNPAVYKSNGQIIHVDGENLFASA 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 680 VT-PMGYFPGLNLEGYPNRDSTQYAATYGI-PTVRTLLRGTLRYQGYARALTGFMKLGLISRDAAPALRAEAHPvTWKEL 757
Cdd:PLN02819 788 VRfRLPNLPAFALECLPNRDSLVYGELYGIeKEAATIFRGTLRYEGFSMIMATLSKLGLFDSENHPLLSTGKRT-TYGAL 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 758 LCDLVGISPSSKHDVL--REAVFEKL-----GRDN-TQLEAAE---WLGLLGDEQVPQA-ESVVDALSKHLARKLSYGPG 825
Cdd:PLN02819 867 LDALLLQDGHNENGPLagEEEISKRLaklghSKNReTAAKAAKtivFLGLDEETEVPKScKSIFDVTCYRMEEKLAYSGN 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 826 EKDMIVMRDSFGIRHP-SGHLENKIIDLVVYGD-ANG--FSAMAKTVGLPTAMAAKMLLDGEIKAKGLMGPFSKDIYEPI 901
Cdd:PLN02819 947 EQDMVLLHHEVEVEFPdSKRIEKHSATLLEFGEiKNGrtTTAMAKTVGIPAAIGALLLLEGKIKTRGVLRPLEPEVYVPA 1026
|
....*....
gi 1952982102 902 LERIKAEGI 910
Cdd:PLN02819 1027 LEILQAYGI 1035
|
|
| Sacchrp_dh_C |
pfam16653 |
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ... |
596-910 |
1.40e-91 |
|
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: 290.35 E-value: 1.40e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 596 GLDPGLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSDNPLRYKFSWSPLGVLTNMMQPATYLLDGKVVTVAGGip 675
Cdd:pfam16653 1 GLDPGIDHMFAIKAIDDVNAKGGKIESFLSYCGGLPAPETSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 676 flDAVTPMGYFPGLNLEGYPNRDSTQYAATYGIPTVRTLLRGTLRYQGYARALTGFMKLGLISRDAAPALraeahpvtwk 755
Cdd:pfam16653 79 --ELMEPIYIRPGFAFEGYPNRDSLPHEELYSLPEAKTLYRGTLRYPGFDEAIKSLVELGLLSEEPKVSL---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 756 ellcdlvgispsskhdvlreavfeklgrdntqleaaEWLGLlgdeqvpqaESVVDALSKHLARKLSYGPGEKDMIVMRDS 835
Cdd:pfam16653 147 ------------------------------------EWLLF---------SGPLDVLAALLEDKLSLGPGERDMVVLQHE 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952982102 836 FGIRHPsghlENKIIDLVVYGD--ANGFSAMAKTVGLPTAMAAKMLLDGEIKAKGLMGPFS-KDIYEPILERIKAEGI 910
Cdd:pfam16653 182 FDGKKG----ERRTYTLVDYGDheEVGPSAMARTVGVPAAIAALLILDGKIKNKGVVNPEEdPEIYEPFLEELEKRGI 255
|
|
| Lys9 |
COG1748 |
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ... |
500-915 |
7.77e-64 |
|
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: 219.32 E-value: 7.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 500 DITVGSDMKDQIEQLGKKY-NINPVSMDISkQEEKLSSLVAKQDLVISLLPYALHPLVAKACIRSKVDMITASYITPELK 578
Cdd:COG1748 2 EVTLADRSLEKAEALAASGpKVEAAQLDAS-DPEALAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEPETE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 579 ---ELEKSVEDAGITVIGELGLDPGLDHMLAMETIDKAKEvgatIESYISYCGGLPAPEhsDNPLRYKFSWSPLGVLTNM 655
Cdd:COG1748 81 aklALDELAKEAGVTAIPGCGLAPGLSNVLAAYAADRFDE----IDSIDIRVGGLPGYP--SNPLNYGTTWSPEGVIREY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 656 MQPATYLLDGKVVTVAggiPFLDAVTPmgYFPGL-NLEGYPNRDSTQYAATYgIPTVRTLLRGTLRYQGYARALTGFMKL 734
Cdd:COG1748 155 TNPARAIEDGKWVEVP---PLSERETI--DFPGVgRYEAYNTDGELETLPET-YPGVKTVRFKTGRYPGHLNHLKVLVDL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 735 GLISRDaapalraeahPVTWKellcdlvgispsskhdvlreavfeklgrdntqleaaewlgllGDEQVPqaesvVDALSK 814
Cdd:COG1748 229 GLTDDE----------PVEVE------------------------------------------GVEVSP-----RDVLKA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 815 HLARKLSYGPGEKDMIVMRDSF-GIRHpsGHLENKIIDLVVYGDAN-GFSAMAKTVGLPTAMAAKMLLDGEIKAKGLMGP 892
Cdd:COG1748 252 ILPDPLPLGPTDKDVVVIGVVVkGTKD--GKRETYVYNLVDHEDAEtGSTAMAYTTGVPAAIAAELLLEGKIPKPGVVNP 329
|
410 420
....*....|....*....|....
gi 1952982102 893 fsKDIY-EPILERIKAEGIVYTTQ 915
Cdd:COG1748 330 --EQLDpDPFLEELAKRGIPIEEE 351
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
21-151 |
3.48e-30 |
|
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: 115.99 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 21 ALRREdVNAWERRAPLAPRHIKGITNLGYKVLIQPSN--RRAIHDKEYVKAGGILQ----EDISEACLILGVKRP--PEE 92
Cdd:pfam05222 1 GVPKE-IKPGERRVALTPAGVKKLVKLGHEVLVESGAglGAGFSDEAYEAAGAEIVdtaaEVWAEADLILKVKEPqpEEY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 93 KLMSK-KTYAFFSHTIkaqeANMGLLDEILRQEIRLIDYEKMVDHRGTRVVAFGQWAGVA 151
Cdd:pfam05222 80 ALLREgQTLITFLHPA----ANPELLEALAAKGVTAIAYETVPRSRGQSLDALSSMANIA 135
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
21-149 |
1.17e-24 |
|
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: 100.18 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 21 ALRREDVNaWERRAPLAPRHIKGITNLGYKVLIQPSN--RRAIHDKEYVKAGGILQED---ISEACLILGVKRP-PEEKL 94
Cdd:smart01003 1 GVPKEIKP-GERRVALTPAGVKKLVKLGHEVLVESGAgeGAGFSDEAYEAAGAEIVDTaevWADADIILKVKEPsPEELA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952982102 95 MSKKTYAFFSHtiKAQEANMGLLDEILRQEIRLIDYEKMV-DHRGTRVVAFGQWAG 149
Cdd:smart01003 80 LLREGQILFGY--LHPAANPELLEALAAKGVTAIAYETVPrISRAQSLDALSSMAE 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LKR_SDH_like |
cd12189 |
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ... |
19-460 |
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: 775.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 19 VMALRREDVNAWERRAPLAPRHIKGIT-NLGYKVLIQPSNRRAIHDKEYVKAGGILQEDISEACLILGVKRPPEEKLMSK 97
Cdd:cd12189 1 VIGIRREDKNIWERRAPLTPSHVRELVkKPGVKVLVQPSNRRAFPDQEYEAAGAIIQEDLSDADLILGVKEPPIDKLLPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 98 KTYAFFSHTIKAQEANMGLLDEILRQEIRLIDYEKMVDHRGTRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHIG 177
Cdd:cd12189 81 KTYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMIDILHGLGLRLLALGYSTPFLHIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 178 MAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEIFNELPCEYVEPHELKEVSQNG-DLRKVYG 256
Cdd:cd12189 161 RAYNYPSLEEAKQAVRDAGYEIALGGLPKSLGPLVFVFTGSGNVSQGAQEIFEELPHEYVEPSDLPELAKSGaDRNKVYG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 257 TVLSRHHHLVRKTDGVYDPVEYDKYPERYISRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDVQSLLVPgkssvagvegc 336
Cdd:cd12189 241 CVVTPEDYLERKDGGPFDRADYYANPELYESVFHEKIAPYLSVLINGIYWDPRFPRLLTNEQLQALLRP----------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 337 PALPHKLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATEYFGDMLYPY 416
Cdd:cd12189 310 PAGPHRLLAIADISCDIGGSIEFLTKATTIDSPFYVYDPDTDKIHDSVSGDGILVMSVDNLPAELPREASEHFGDALLPY 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1952982102 417 VEEMILSDATQPLESQNFSPVVRDAVITSNGVLPDKYKYIQKLR 460
Cdd:cd12189 390 VPDLAKSDASKPLEESELPPVLRRATIASNGKLTPKYEYIQELR 433
|
|
| PLN02819 |
PLN02819 |
lysine-ketoglutarate reductase/saccharopine dehydrogenase |
19-910 |
0e+00 |
|
lysine-ketoglutarate reductase/saccharopine dehydrogenase
Pssm-ID: 215439 [Multi-domain] Cd Length: 1042 Bit Score: 715.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 19 VMALRREDVNAWERRAPLAPRHIKGITNLGY-----KVLIQPSNRRAIHDKEYVKAGGILQEDISEACLILGVKRPPEEK 93
Cdd:PLN02819 7 VVGILAETVNKWERRAPLTPSHCARLLHSGKdrtvsRIIVQPSSKRIHHDAQYEDVGCEISEDLSDCGLILGVKQPKLEM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 94 LMSKKTYAFFSHTIKAQEANMGLLDEILRQEIRLIDYEKMVDHRGTRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPF 173
Cdd:PLN02819 87 LLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKYAGRAGMIDFFRGLGQRLLSLGYSTPF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 174 MHIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEIFNELPCEYVEPHELKEVSQ------ 247
Cdd:PLN02819 167 LSLGSSYMYSSLAAAKAAVISVGEEIASSGLPLGICPLVFVFTGSGNVSQGAQEIFKLLPHTFVEPSKLPELKGisqnki 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 248 -NGDLRKVYGTVLSRHHHLVRKTDG-VYDPVEYDKYPERYISRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDVQSLLVP 325
Cdd:PLN02819 247 sTKRVYQVYGCVVTSQDMVEHKDPSkQFDKADYYAHPEHYNPVFHEKIAPYASVIVNCMYWEKRFPRLLTTKQLQDLTRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 326 GkssvagveGCPalphkLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEA 405
Cdd:PLN02819 327 G--------GCP-----LVGVCDITCDIGGSIEFLNKTTSIEKPFFRYNPSNNSYHDDMDGDGILCMAVDILPTEFAKEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 406 TEYFGDMLYPYVEEMIlsDATQPLEsqnFSPVVRDAVITSNGVLPDKYKYIQKLRES-RELAQ-------------SLS- 470
Cdd:PLN02819 394 SQHFGNILSPFVGSLA--SMKELAE---LPSHLRRACIAHRGSLTPLFEYIPRMRNSnAELAQdtvssqstfnilvSLSg 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 --------------------------------------------------------------------------------
Cdd:PLN02819 469 hlfdkflinealdvieaaggsfhlakcqvgqsadaesyselevgaddkevldqiidsltrlanpnedyispareankifl 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 471 ----------------MGTK-KRVLVLGSGYVSEPVLEYLSR-------------DNRIDITVGSD-MKDQIEQLGKKYN 519
Cdd:PLN02819 549 kigkvqqenecnekaeVTKKsQNVLILGAGRVCRPAAEYLASvktisyygddseePTDVHVIVASLyLKDAKETVEGIEN 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 520 INPVSMDISkQEEKLSSLVAKQDLVISLLPYALHPLVAKACIRSKVDMITASYITPELKELEKSVEDAGITVIGELGLDP 599
Cdd:PLN02819 629 AEAVQLDVS-DSESLLKYVSQVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITILCEMGLDP 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 600 GLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSDNPLRYKFSWSPLGVLTNMMQPATYLLDGKVVTVAGGIPFLDA 679
Cdd:PLN02819 708 GIDHMMAMKMIDDAHERGGKVKSFTSYCGGLPSPEAANNPLAYKFSWNPAGAIKAGQNPAVYKSNGQIIHVDGENLFASA 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 680 VT-PMGYFPGLNLEGYPNRDSTQYAATYGI-PTVRTLLRGTLRYQGYARALTGFMKLGLISRDAAPALRAEAHPvTWKEL 757
Cdd:PLN02819 788 VRfRLPNLPAFALECLPNRDSLVYGELYGIeKEAATIFRGTLRYEGFSMIMATLSKLGLFDSENHPLLSTGKRT-TYGAL 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 758 LCDLVGISPSSKHDVL--REAVFEKL-----GRDN-TQLEAAE---WLGLLGDEQVPQA-ESVVDALSKHLARKLSYGPG 825
Cdd:PLN02819 867 LDALLLQDGHNENGPLagEEEISKRLaklghSKNReTAAKAAKtivFLGLDEETEVPKScKSIFDVTCYRMEEKLAYSGN 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 826 EKDMIVMRDSFGIRHP-SGHLENKIIDLVVYGD-ANG--FSAMAKTVGLPTAMAAKMLLDGEIKAKGLMGPFSKDIYEPI 901
Cdd:PLN02819 947 EQDMVLLHHEVEVEFPdSKRIEKHSATLLEFGEiKNGrtTTAMAKTVGIPAAIGALLLLEGKIKTRGVLRPLEPEVYVPA 1026
|
....*....
gi 1952982102 902 LERIKAEGI 910
Cdd:PLN02819 1027 LEILQAYGI 1035
|
|
| Sacchrp_dh_C |
pfam16653 |
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ... |
596-910 |
1.40e-91 |
|
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: 290.35 E-value: 1.40e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 596 GLDPGLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSDNPLRYKFSWSPLGVLTNMMQPATYLLDGKVVTVAGGip 675
Cdd:pfam16653 1 GLDPGIDHMFAIKAIDDVNAKGGKIESFLSYCGGLPAPETSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 676 flDAVTPMGYFPGLNLEGYPNRDSTQYAATYGIPTVRTLLRGTLRYQGYARALTGFMKLGLISRDAAPALraeahpvtwk 755
Cdd:pfam16653 79 --ELMEPIYIRPGFAFEGYPNRDSLPHEELYSLPEAKTLYRGTLRYPGFDEAIKSLVELGLLSEEPKVSL---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 756 ellcdlvgispsskhdvlreavfeklgrdntqleaaEWLGLlgdeqvpqaESVVDALSKHLARKLSYGPGEKDMIVMRDS 835
Cdd:pfam16653 147 ------------------------------------EWLLF---------SGPLDVLAALLEDKLSLGPGERDMVVLQHE 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952982102 836 FGIRHPsghlENKIIDLVVYGD--ANGFSAMAKTVGLPTAMAAKMLLDGEIKAKGLMGPFS-KDIYEPILERIKAEGI 910
Cdd:pfam16653 182 FDGKKG----ERRTYTLVDYGDheEVGPSAMARTVGVPAAIAALLILDGKIKNKGVVNPEEdPEIYEPFLEELEKRGI 255
|
|
| SDH_like |
cd05199 |
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ... |
19-418 |
7.87e-89 |
|
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: 7.87e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 19 VMALRREDVNAWERRAPLAPRHIKGITNLGY--KVLIQPSNRRAIHDKEYVKAGGILQEDISEACLILGVKRPPEEKLMS 96
Cdd:cd05199 1 KIGIIREGKTPPDRRVPLTPEQCKELQAKYPgvEIFVQPSPVRCFKDEEYRAAGIEVVEDLSDCDILLGVKEVPIEQLIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 97 KKTYAFFSHTIKAQEANMGLLDEILRQEIRLIDYEKMVDHRGTRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFmhi 176
Cdd:cd05199 81 NKTYFFFSHTIKKQPYNRKLLQTILEKNITLIDYEVLVDEQGKRVIAFGRYAGIVGAYNGLRAYGKKTGLFDLKRAH--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 177 gmahnyrnssqavqAVRDAGYEISLGLmPKSIGPLTFVFTGTGNVSKGAQEIFNELPCEYVEPHELKEVsqngdlrkvyg 256
Cdd:cd05199 158 --------------ECSDLEELIAELK-KVGLPPPKIVITGSGRVGSGAAEVLKALGIKEVSPEDFLTV----------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 257 tvlsrhhhlvrktdgvydpveydkyperyisrfnTDIapyttcLINGIYWEQNTPRLLTRQDVQSllvpgkssvagvegc 336
Cdd:cd05199 212 ----------------------------------ADI------LINGHYWDKRAPRLFTKEDLKK--------------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 337 palPH-KLVAICDISADTGGSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATEYFGDMLYP 415
Cdd:cd05199 237 ---PDfKIRVIADVTCDIHGSIPSTLRASTIADPVYDYDPTTNKEVAFSSPDSITVMAVDNLPCELPRDASEDFGEQLIK 313
|
...
gi 1952982102 416 YVE 418
Cdd:cd05199 314 SVL 316
|
|
| Lys9 |
COG1748 |
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ... |
500-915 |
7.77e-64 |
|
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: 219.32 E-value: 7.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 500 DITVGSDMKDQIEQLGKKY-NINPVSMDISkQEEKLSSLVAKQDLVISLLPYALHPLVAKACIRSKVDMITASYITPELK 578
Cdd:COG1748 2 EVTLADRSLEKAEALAASGpKVEAAQLDAS-DPEALAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEPETE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 579 ---ELEKSVEDAGITVIGELGLDPGLDHMLAMETIDKAKEvgatIESYISYCGGLPAPEhsDNPLRYKFSWSPLGVLTNM 655
Cdd:COG1748 81 aklALDELAKEAGVTAIPGCGLAPGLSNVLAAYAADRFDE----IDSIDIRVGGLPGYP--SNPLNYGTTWSPEGVIREY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 656 MQPATYLLDGKVVTVAggiPFLDAVTPmgYFPGL-NLEGYPNRDSTQYAATYgIPTVRTLLRGTLRYQGYARALTGFMKL 734
Cdd:COG1748 155 TNPARAIEDGKWVEVP---PLSERETI--DFPGVgRYEAYNTDGELETLPET-YPGVKTVRFKTGRYPGHLNHLKVLVDL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 735 GLISRDaapalraeahPVTWKellcdlvgispsskhdvlreavfeklgrdntqleaaewlgllGDEQVPqaesvVDALSK 814
Cdd:COG1748 229 GLTDDE----------PVEVE------------------------------------------GVEVSP-----RDVLKA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 815 HLARKLSYGPGEKDMIVMRDSF-GIRHpsGHLENKIIDLVVYGDAN-GFSAMAKTVGLPTAMAAKMLLDGEIKAKGLMGP 892
Cdd:COG1748 252 ILPDPLPLGPTDKDVVVIGVVVkGTKD--GKRETYVYNLVDHEDAEtGSTAMAYTTGVPAAIAAELLLEGKIPKPGVVNP 329
|
410 420
....*....|....*....|....
gi 1952982102 893 fsKDIY-EPILERIKAEGIVYTTQ 915
Cdd:COG1748 330 --EQLDpDPFLEELAKRGIPIEEE 351
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
21-151 |
3.48e-30 |
|
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: 115.99 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 21 ALRREdVNAWERRAPLAPRHIKGITNLGYKVLIQPSN--RRAIHDKEYVKAGGILQ----EDISEACLILGVKRP--PEE 92
Cdd:pfam05222 1 GVPKE-IKPGERRVALTPAGVKKLVKLGHEVLVESGAglGAGFSDEAYEAAGAEIVdtaaEVWAEADLILKVKEPqpEEY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 93 KLMSK-KTYAFFSHTIkaqeANMGLLDEILRQEIRLIDYEKMVDHRGTRVVAFGQWAGVA 151
Cdd:pfam05222 80 ALLREgQTLITFLHPA----ANPELLEALAAKGVTAIAYETVPRSRGQSLDALSSMANIA 135
|
|
| SDH |
cd12188 |
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ... |
24-419 |
3.92e-29 |
|
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: 119.64 E-value: 3.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 24 REDVNAWERRAPLAPRHIKGITNLGYKVLIQPSNRRAIHDKEYVKAGGILQEDIS-----EACLILGVKRPPEEKLMSKK 98
Cdd:cd12188 6 RAETKPLERRTALTPTTAKKLLDAGFKVTVERSPQRIFPDEEYEAVGCELVPAGSwvnapKDAIILGLKELPEDTFPLPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 99 TYAFFSHTIKAQEANMGLLDEILRQEIRLIDYEKMVDHRGTRVVAFGQWAGVAGMinilhGMGLRLLA--LGHHTPFmhi 176
Cdd:cd12188 86 RHIYFAHAYKGQAGWKDVLSRFARGGGTLLDLEYLVDDDGRRVAAFGYWAGFAGA-----ALGLLAWAhqQLGPVTL--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 177 GMAHNYRNSSQAVQAVRDAgyEISLGLMPKS--IGPLtfvftgtGNVSKGAQEIFNELPCEyVEPHELKEVSQNGDlrkv 254
Cdd:cd12188 158 PPVSPYPNEEALVADVKKA--LATGGRKPRAlvIGAL-------GRCGSGAVDLLEAAGIE-VTKWDMAETKAGGP---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 255 ygtvlsrhhhlvrktdgvydpveydkYPEryISRFntDIapyttcLINGIYWEQNTPRLLTRQDVQSllvPGkssvagve 334
Cdd:cd12188 224 --------------------------FPE--ILDH--DI------FVNCIYLSKPIPPFLTPEMLQA---PG-------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 335 gcpalpHKLVAICDISADTGGS---IEFMTECTTIEHPfcmydadqhIIHDSVEGSGILMCSIDNLPAQLPIEATEYFGD 411
Cdd:cd12188 257 ------RRLRVIGDVSCDPTNPynpIPIYDVATTFDKP---------TLRVPTGGPPLDVIAIDHLPSLLPRESSEDFSN 321
|
....*...
gi 1952982102 412 MLYPYVEE 419
Cdd:cd12188 322 DLLPSLLE 329
|
|
| Sacchrp_dh_NADP |
pfam03435 |
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ... |
477-592 |
2.80e-26 |
|
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: 104.21 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 477 VLVLGSGYVSEPVLEYLSRDNRID-ITVGSDMKDQIEQLGKK---YNINPVSMDISKQEEKLSSLVAKQDLVISLLPYAL 552
Cdd:pfam03435 1 VLIIGAGSVGQGVAPLLARHFDVDrITVADRTLEKAQALAAKlggVRFIAVAVDADNYEAVLAALLKEGDLVVNLSPPTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1952982102 553 HPLVAKACIRSKVDMITASYITPELKELEKSVEDAGITVI 592
Cdd:pfam03435 81 SLDVLKACIETGVHYVDTSYLREAVLALHEKAKDAGVTAV 120
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
21-149 |
1.17e-24 |
|
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: 100.18 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 21 ALRREDVNaWERRAPLAPRHIKGITNLGYKVLIQPSN--RRAIHDKEYVKAGGILQED---ISEACLILGVKRP-PEEKL 94
Cdd:smart01003 1 GVPKEIKP-GERRVALTPAGVKKLVKLGHEVLVESGAgeGAGFSDEAYEAAGAEIVDTaevWADADIILKVKEPsPEELA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952982102 95 MSKKTYAFFSHtiKAQEANMGLLDEILRQEIRLIDYEKMV-DHRGTRVVAFGQWAG 149
Cdd:smart01003 80 LLREGQILFGY--LHPAANPELLEALAAKGVTAIAYETVPrISRAQSLDALSSMAE 133
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
191-379 |
1.06e-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: 95.27 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 191 AVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEIFNELPCE----YVEPHELKEVSQngdlrkVYGTVLsrhhhlv 266
Cdd:smart01002 1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEvtvlDVRPARLRQLES------LLGARF------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 267 rktdgvydpveydkYPERYISRFNTDIAPYTTCLINGIYWE-QNTPRLLTRQDVQSLlVPGksSVagvegcpalphklva 345
Cdd:smart01002 68 --------------TTLYSQAELLEEAVKEADLVIGAVLIPgAKAPKLVTREMVKSM-KPG--SV--------------- 115
|
170 180 190
....*....|....*....|....*....|....
gi 1952982102 346 ICDISADTGGSIEFmTECTTIEHPFCMYDADQHI 379
Cdd:smart01002 116 IVDVAADQGGCIET-SRPTTHDDPTYVVDGVVHY 148
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
31-421 |
1.35e-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: 66.66 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 31 ERRAPLAPRHIKGITNLGYKVLIQ--PSNRRAIHDKEYVKAGGIL----QEDISEACLILGVKRPPE-EKLMSKKTYAFF 103
Cdd:cd01620 12 EFRVALTPSFVKKLVANGFKVYIEtgAGSGAGFSDEDYLQAGAQIvpaaSKEAYSADIIVKLKEPEFaEYDLIKKGQLLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 104 SHTIKAQEAnmGLLDEILRQEIRLIDYEKMVDHRGTRVVAFGQWAGVAGMInilhgMGLRLLALGHhtpfmhiGMAHNYR 183
Cdd:cd01620 92 TFLHAATNR--GVVEVLMRKKLTAYALEDLENDFRPRLAPNSNIAGYAGVQ-----LGAYELARIQ-------GGRMGGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 184 NSSqavqavrdagyeislglmpksiGPLTFVFTGTGNVSKGAQEIFnelpceyvepHELKEVSQNGDLRkvygtVLSRHH 263
Cdd:cd01620 158 GGV----------------------PPAKVLIIGAGVVGLGAAKIA----------KKLGANVLVYDIK-----EEKLKG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 264 hlvRKTDGVYDPVEYDKY-PERYISRfnTDIapyttcLINGIYWE-QNTPRLLTRQDVqSLLVPGksSVagvegcpalph 341
Cdd:cd01620 201 ---VETLGGSRLRYSQKEeLEKELKQ--TDI------LINAILVDgPRAPILIMEELV-GPMKRG--AV----------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 342 klvaICDISADTGGSIEfMTECTTIEHPfcmydadqhiihdSVEGSGILMCSIDNLPAQLPIEATEYFGDMLYPYVEEMI 421
Cdd:cd01620 256 ----IVDLAADQGGNDE-TSIPTTEGVP-------------TYEVDGVVIYGVDNMPSLVPREASELLSKNLLPYLVKLA 317
|
|
| ceo_syn |
cd12181 |
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ... |
31-423 |
9.07e-07 |
|
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: 51.46 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 31 ERRAPLAPRHIKGItNLGYKVLIQPS--NRRAIHDKEYVKAG-GIL--QEDISEACLILGVKrPPEEKLMSKK------- 98
Cdd:cd12181 13 EKRVPLLPADLERI-PLREQLYFEEGygERLGISDEEYAALGaGIVsrEEILAKCDVICDPK-PGDADYLEILegqilwg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 99 -TYAFFSHTIKaqeanmgllDEILRQEIRLIDYEKMVDHRGTRVVAFGQWAGVAGMINILHGMGLRllalghhtpfmhig 177
Cdd:cd12181 91 wVHCVQDKEIT---------QLAIDKKLTLIAWEDMFEWSKIGRHVFYKNNELAGYAAVLHALQLY-------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 178 mahnyrnssqavqavrdagyeislGLMPKSigPLTFVFTGTGNVSKGAQEIFNelpceyvepHELKEVsqngdlrKVYGt 257
Cdd:cd12181 148 ------------------------GITPYR--QTKVAVLGFGNTARGAIRALK---------LGGADV-------TVYT- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 258 vlSRHHHLVRKtdgvydpvEYDKYperyisrfntDIapyttcLINGIYWEQNTP-RLLTRQDvQSLLVPGkssvagvegc 336
Cdd:cd12181 185 --RRTEALFKE--------ELSEY----------DI------IVNCILQDTDRPdHIIYEED-LKRLKPG---------- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 337 pALphklvaICDISADTGGSIEFmTECTTIEHPfcMYDADqHIIHDSVegsgilmcsiDNLPAQLPIEATEYFGDMLYPY 416
Cdd:cd12181 228 -AL------IIDVSCDEGMGIEF-AKPTTFDDP--IYKVD-GIDYYAV----------DHTPSLFYRSASRSISKALAPY 286
|
....*..
gi 1952982102 417 VEEMILS 423
Cdd:cd12181 287 LDTVIEG 293
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
31-92 |
1.69e-04 |
|
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: 44.70 E-value: 1.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952982102 31 ERRAPLAPRHIKGITNLGYKVLIQP-SNRRA-IHDKEYVKAGGIL---QEDISEACLILGVKRPPEE 92
Cdd:cd05304 13 ERRVALTPETVKKLVKLGFEVLVESgAGEAAgFSDEAYEEAGAEIvsdAEELAQADIVLKVRPPSEE 79
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
473-672 |
1.49e-03 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 41.45 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 473 TKKRVLVLGSGYVSEPVLEYLSRDNRIDITVGSDM-KDQIEQLGKKYNINPVSmDISKqeeklssLVAKQ--DLVISLLP 549
Cdd:COG0673 2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRdPERAEAFAEEYGVRVYT-DYEE-------LLADPdiDAVVIATP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 550 YALHPLVAKACIRSKVDM-----ITASYitPELKELEKSVEDAGITV-IGELG-LDPGldHMLAMETIDkAKEVGATIES 622
Cdd:COG0673 74 NHLHAELAIAALEAGKHVlcekpLALTL--EEARELVAAAEEAGVVLmVGFNRrFDPA--VRAARELID-SGAIGEIRSV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1952982102 623 YISYCGGLPAPEHSdnpLRYKFSWSPLGVLTNMM----QPATYLLDGKVVTVAG 672
Cdd:COG0673 149 RARFGHPRPAGPAD---WRFDPELAGGGALLDLGihdiDLARWLLGSEPESVSA 199
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
297-447 |
2.48e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 40.17 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 297 TTCLINGiyweQNTPRLLTRQDVQSLLvPGksSVagvegcpalphklvaICDISADTGGSIEfMTECTTIEHPFCMYDad 376
Cdd:pfam01262 98 GTALIPG----AKAPKLVTREMVKSMK-PG--SV---------------IVDVAIDQGGNVE-TSRPTTHGEPVYVVD-- 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952982102 377 qhiihdsvegsGILMCSIDNLPAQLPIEATEYFGDMLYPYVEEMilsdATQPLESQNF-SPVVRDAVITSNG 447
Cdd:pfam01262 153 -----------GVVHYGVANMPGAVPRTSSQALTNNTLPYLLLL----ADKGLKAALLeDEALRAGLNTHDG 209
|
|
| ThiF |
pfam00899 |
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
457-571 |
5.88e-03 |
|
ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.
Pssm-ID: 459987 [Multi-domain] Cd Length: 238 Bit Score: 39.55 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952982102 457 QKLRESRelaqslsmgtkkrVLVLGSGYVSEPVLEYLSR---------DN-RIDIT------------VG---SD-MKDQ 510
Cdd:pfam00899 16 EKLRNSR-------------VLIVGAGGLGSEAAKYLARagvgkitlvDFdTVELSnlnrqflfreadIGkpkAEvAAER 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952982102 511 IEQLGKKYNINPVSMDISKQEekLSSLVAKQDLVISLL-PYALHPLVAKACIRSKVDMITAS 571
Cdd:pfam00899 83 LREINPDVEVEAYTERLTPEN--AEELIKSFDIVVDATdNFAARYLVNDACVKLGKPLIEAG 142
|
|
| |
