|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14193 |
PRK14193 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-281 |
2.60e-175 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237637 [Multi-domain] Cd Length: 284 Bit Score: 484.90 E-value: 2.60e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 1 MTAQKLDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:PRK14193 1 MTAIILDGKATADEIKADLAERVAALKEKGITPGLGTVLVGDDPGSQAYVRGKHRDCAEVGITSIRRDLPADATQEELNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAE 158
Cdd:PRK14193 81 VIDELNADPACTGYIVQLPlpKHLDENAVLERIDPAKDADGLHPTNLGRLVLNEPAPLPCTPRGIVHLLRRYDVELAGAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 159 VVVVGRGLTVGRPLGLLLTRRSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRV-DGK 237
Cdd:PRK14193 161 VVVIGRGVTVGRPIGLLLTRRSENATVTLCHTGTRDLAAHTRRADIIVAAAGVAHLVTADMVKPGAAVLDVGVSRAgDGK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1906349552 238 IAGDLADDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQALE 281
Cdd:PRK14193 241 LVGDVHPDVWEVAGAVSPNPGGVGPMTRAFLLTNVVERAERRAG 284
|
|
| FolD |
COG0190 |
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase ... |
1-282 |
1.30e-164 |
|
5,10-methylene-tetrahydrofolate dehydrogenase/Methenyl tetrahydrofolate cyclohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 439960 [Multi-domain] Cd Length: 285 Bit Score: 457.94 E-value: 1.30e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 1 MTAQKLDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:COG0190 1 MMAQILDGKAVAAEIREELKERVAALKAKGITPGLAVVLVGDDPASQVYVRNKHKACEEVGIESELIRLPADTTQEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAE 158
Cdd:COG0190 81 LIDELNADPSVHGILVQLPlpKHIDEEAVLEAIDPEKDVDGFHPVNLGRLVLGEPGFVPCTPAGIMELLERYGIDLAGKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 159 VVVVGRGLTVGRPLGLLLTRRseNATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRV-DGK 237
Cdd:COG0190 161 AVVVGRSNIVGKPLALLLLRR--NATVTVCHSRTKDLAEHTRQADILVAAVGKPGLITADMVKPGAVVIDVGINRVeDGK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1906349552 238 IAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQALER 282
Cdd:COG0190 239 LVGDVDfESVAEKASAITPVPGGVGPMTIAMLLENTLKAAERQAGL 284
|
|
| PRK14190 |
PRK14190 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-282 |
2.23e-118 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184560 [Multi-domain] Cd Length: 284 Bit Score: 340.84 E-value: 2.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 1 MTAQKLDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:PRK14190 1 MMAVIIDGKEVAKEKREQLKEEVVKLKEQGIVPGLAVILVGDDPASHSYVRGKKKAAEKVGIYSELYEFPADITEEELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAE 158
Cdd:PRK14190 81 LIDRLNADPRINGILVQlpLPKHIDEKAVIERISPEKDVDGFHPINVGRMMLGQDTFLPCTPHGILELLKEYNIDISGKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 159 VVVVGRGLTVGRPLGLLLTRrsENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVD-GK 237
Cdd:PRK14190 161 VVVVGRSNIVGKPVGQLLLN--ENATVTYCHSKTKNLAELTKQADILIVAVGKPKLITADMVKEGAVVIDVGVNRLEnGK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1906349552 238 IAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQALER 282
Cdd:PRK14190 239 LCGDVDfDNVKEKASYITPVPGGVGPMTITMLMHNTVELAKRAGGR 284
|
|
| PRK14189 |
PRK14189 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
1-279 |
8.10e-107 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 184559 [Multi-domain] Cd Length: 285 Bit Score: 311.62 E-value: 8.10e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 1 MTAQKLDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:PRK14189 1 MTAQLIDGNALSKQLRAEAAQRAAALTARGHQPGLAVILVGDNPASQVYVRNKVKACEDNGFHSLKDRYPADLSEAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQQ--PTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAE 158
Cdd:PRK14189 81 RIDELNRDPKIHGILVQLplPKHIDSHKVIEAIAPEKDVDGFHVANAGALMTGQPLFRPCTPYGVMKMLESIGIPLRGAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 159 VVVVGRGLTVGRPLGLLLTRRseNATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVD-GK 237
Cdd:PRK14189 161 AVVIGRSNIVGKPMAMLLLQA--GATVTICHSKTRDLAAHTRQADIVVAAVGKRNVLTADMVKPGATVIDVGMNRDDaGK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1906349552 238 IAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQA 279
Cdd:PRK14189 239 LCGDVDfAGVKEVAGYITPVPGGVGPMTITMLLVNTIEAAERA 281
|
|
| PRK14186 |
PRK14186 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-275 |
7.07e-102 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237636 [Multi-domain] Cd Length: 297 Bit Score: 299.29 E-value: 7.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 2 TAQKLDGTATLKTIKAELADRVEK-LKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:PRK14186 1 MALILDGKALAAEIEQRLQAQIESnLPKAGRPPGLAVLRVGDDPASAVYVRNKEKACARVGIASFGKHLPADTSQAEVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAE 158
Cdd:PRK14186 81 LIAQLNQDERVDGILLQLPlpKHLDEVPLLHAIDPDKDADGLHPLNLGRLVKGEPGLRSCTPAGVMRLLRSQQIDIAGKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 159 VVVVGRGLTVGRPLGLLLtrRSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRV---- 234
Cdd:PRK14186 161 AVVVGRSILVGKPLALML--LAANATVTIAHSRTQDLASITREADILVAAAGRPNLIGAEMVKPGAVVVDVGIHRLpssd 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1906349552 235 -DGKIAGD-LADDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLS 275
Cdd:PRK14186 239 gKTRLCGDvDFEEVEPVAAAITPVPGGVGPMTVTMLLVNTVLS 281
|
|
| PRK10792 |
PRK10792 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-282 |
8.02e-97 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 236760 [Multi-domain] Cd Length: 285 Bit Score: 286.04 E-value: 8.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 1 MTAQKLDGTATLKTIKAELADRVEKLKAAGV-TPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVE 79
Cdd:PRK10792 1 MTAKIIDGKTIAQQVRSEVAQKVQARVAAGLrAPGLAVVLVGSDPASQVYVASKRKACEEVGFVSRSYDLPETTSEAELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 80 AEIGRLNADPACTGFLVQQ--PTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGA 157
Cdd:PRK10792 81 ALIDELNADPTIDGILVQLplPAHIDNVKVLERIHPDKDVDGFHPYNVGRLAQRIPLLRPCTPRGIMTLLERYGIDTYGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 158 EVVVVGRGLTVGRP--LGLLLTRrsenATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRV- 234
Cdd:PRK10792 161 NAVVVGASNIVGRPmsLELLLAG----CTVTVCHRFTKNLRHHVRNADLLVVAVGKPGFIPGEWIKPGAIVIDVGINRLe 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1906349552 235 DGKIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQALER 282
Cdd:PRK10792 237 DGKLVGDVEfETAAERASWITPVPGGVGPMTVATLLENTLQACEEYHDP 285
|
|
| PRK14167 |
PRK14167 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
3-279 |
6.63e-93 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184549 [Multi-domain] Cd Length: 297 Bit Score: 276.66 E-value: 6.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 3 AQKLDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEI 82
Cdd:PRK14167 2 TEIIDGNAVAAQIRDDLTDAIETLEDAGVTPGLATVLMSDDPASETYVSMKQRDCEEVGIEAIDVEIDPDAPAEELYDTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 83 GRLNADPACTGFLVQQPT--GLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVV 160
Cdd:PRK14167 82 DELNADEDVHGILVQMPVpdHVDDREVLRRIDPAKDVDGFHPENVGRLVAGDARFKPCTPHGIQKLLAAAGVDTEGADVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 161 VVGRGLTVGRPLGLLLTRRSE--NATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDG-- 236
Cdd:PRK14167 162 VVGRSDIVGKPMANLLIQKADggNATVTVCHSRTDDLAAKTRRADIVVAAAGVPELIDGSMLSEGATVIDVGINRVDAdt 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1906349552 237 ----KIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQA 279
Cdd:PRK14167 242 ekgyELVGDVEfESAKEKASAITPVPGGVGPMTRAMLLYNTVKAASLQ 289
|
|
| PRK14188 |
PRK14188 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
2-279 |
1.52e-92 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184558 [Multi-domain] Cd Length: 296 Bit Score: 275.68 E-value: 1.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 2 TAQKLDGTATLKTIKAELADRVEKLKAA-GVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:PRK14188 1 MATIIDGKAFAADVRATVAAEVARLKAAhGVTPGLAVVLVGEDPASQVYVRSKGKQTKEAGMASFEHKLPADTSQAELLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAE 158
Cdd:PRK14188 81 LIARLNADPAIHGILVQlpLPKHLDSEAVIQAIDPEKDVDGLHVVNAGRLATGETALVPCTPLGCMMLLRRVHGDLSGLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 159 VVVVGRGLTVGRPLGLLLTRrsENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDG-- 236
Cdd:PRK14188 161 AVVIGRSNLVGKPMAQLLLA--ANATVTIAHSRTRDLPAVCRRADILVAAVGRPEMVKGDWIKPGATVIDVGINRIPApe 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1906349552 237 ------KIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQA 279
Cdd:PRK14188 239 kgegktRLVGDVAfAEAAEVAGAITPVPGGVGPMTIACLLANTLTAACRA 288
|
|
| PRK14184 |
PRK14184 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-275 |
2.38e-92 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 237635 [Multi-domain] Cd Length: 286 Bit Score: 274.73 E-value: 2.38e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 6 LDGTATLKTIKAELADRVEKLKA-AGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGR 84
Cdd:PRK14184 4 LDGKATAATIREELKTEVAALTArHGRAPGLAVILVGEDPASQVYVRNKERACEDAGIVSEAFRLPADTTQEELEDLIAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 85 LNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVVVV 162
Cdd:PRK14184 84 LNARPDIDGILLQLPlpKGLDSQRCLELIDPAKDVDGFHPENMGRLALGLPGFRPCTPAGVMTLLERYGLSPAGKKAVVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 163 GRGLTVGRPLGLLLTRRSE--NATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDGKIAG 240
Cdd:PRK14184 164 GRSNIVGKPLALMLGAPGKfaNATVTVCHSRTPDLAEECREADFLFVAIGRPRFVTADMVKPGAVVVDVGINRTDDGLVG 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 1906349552 241 DLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLS 275
Cdd:PRK14184 244 DCDfEGLSDVASAITPVPGGVGPMTIAQLLVNTVQS 279
|
|
| PRK14191 |
PRK14191 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-283 |
3.74e-89 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172679 [Multi-domain] Cd Length: 285 Bit Score: 266.63 E-value: 3.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 4 QKLDGTATLKTIKAELADRVEKLKA-AGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEI 82
Cdd:PRK14191 2 VLLDGKALSYKIEKDLKNKIQILTAqTGKRPKLAVILVGKDPASQTYVNMKIKACERVGMDSDLHTLQENTTEAELLSLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 83 GRLNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVV 160
Cdd:PRK14191 82 KDLNTDQNIDGILVQLPlpRHIDTKMVLEAIDPNKDVDGFHPLNIGKLCSQLDGFVPATPMGVMRLLKHYHIEIKGKDVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 161 VVGRGLTVGRPLGLLLTrrSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRV-DGKIA 239
Cdd:PRK14191 162 IIGASNIVGKPLAMLML--NAGASVSVCHILTKDLSFYTQNADIVCVGVGKPDLIKASMVKKGAVVVDIGINRLnDGRLV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1906349552 240 GDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQALERL 283
Cdd:PRK14191 240 GDVDfENVAPKASFITPVPGGVGPMTIVSLLENTLIAAEKRQRKG 284
|
|
| PRK14176 |
PRK14176 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-280 |
1.15e-87 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184553 [Multi-domain] Cd Length: 287 Bit Score: 262.82 E-value: 1.15e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 6 LDGTATLKTIKAELADRVEKLKA-AGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGR 84
Cdd:PRK14176 11 IDGKALAKKIEAEVRSGVERLKSnRGITPGLATILVGDDPASKMYVRLKHKACERVGIRAEDQFLPADTTQEELLELIDS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 85 LNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVVVV 162
Cdd:PRK14176 91 LNKRKDVHGILLQLPlpKHLDPQEAMEAIDPAKDADGFHPYNMGKLMIGDEGLVPCTPHGVIRALEEYGVDIEGKNAVIV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 163 GRGLTVGRPLGLLLTRRseNATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDGKIAGDL 242
Cdd:PRK14176 171 GHSNVVGKPMAAMLLNR--NATVSVCHVFTDDLKKYTLDADILVVATGVKHLIKADMVKEGAVIFDVGITKEEDKVYGDV 248
|
250 260 270
....*....|....*....|....*....|....*....
gi 1906349552 243 A-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQAL 280
Cdd:PRK14176 249 DfENVIKKASLITPVPGGVGPLTIAMLMKHVLMCAEKSL 287
|
|
| PRK14174 |
PRK14174 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-279 |
3.55e-85 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172662 [Multi-domain] Cd Length: 295 Bit Score: 257.06 E-value: 3.55e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 6 LDGTATLKTIKAELADRVEKLKA-AGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGR 84
Cdd:PRK14174 4 IDGKKVSLDLKNELKTRVEAYRAkTGKVPGLTVIIVGEDPASQVYVRNKAKSCKEIGMNSTVIELPADTTEEHLLKKIED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 85 LNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLG--EDGPLPCTPVGCIELLRRHGVEINGAEVV 160
Cdd:PRK14174 84 LNNDPDVHGILVQQPlpKQIDEFAVTLAIDPAKDVDGFHPENLGRLVMGhlDKCFVSCTPYGILELLGRYNIETKGKHCV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 161 VVGRGLTVGRPLGLLLTR--RSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDG-- 236
Cdd:PRK14174 164 VVGRSNIVGKPMANLMLQklKESNCTVTICHSATKDIPSYTRQADILIAAIGKARFITADMVKPGAVVIDVGINRIEDps 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1906349552 237 -----KIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQA 279
Cdd:PRK14174 244 tksgyRLVGDVDyEGVSAKASAITPVPGGVGPMTIAMLLKNTLQSFERV 292
|
|
| PRK14183 |
PRK14183 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-278 |
8.91e-84 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184555 [Multi-domain] Cd Length: 281 Bit Score: 252.83 E-value: 8.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 4 QKLDGTATLKTIKAELADRVEKLK-AAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEI 82
Cdd:PRK14183 2 QILDGKALSDKIKENVKKEVDELKlVKNIVPGLAVILVGDDPASHTYVKMKAKACDRVGIYSITHEMPSTISQKEILETI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 83 GRLNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVV 160
Cdd:PRK14183 82 AMMNNNPNIDGILVQLPlpKHIDTTKILEAIDPKKDVDGFHPYNVGRLVTGLDGFVPCTPLGVMELLEEYEIDVKGKDVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 161 VVGRGLTVGRPLGLLLTRRseNATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRV-DGKIA 239
Cdd:PRK14183 162 VVGASNIVGKPMAALLLNA--NATVDICHIFTKDLKAHTKKADIVIVGVGKPNLITEDMVKEGAIVIDIGINRTeDGRLV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1906349552 240 GDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQ 278
Cdd:PRK14183 240 GDVDfENVAKKCSYITPVPGGVGPMTIAMLLSNTLKAAKN 279
|
|
| PLN02516 |
PLN02516 |
methylenetetrahydrofolate dehydrogenase (NADP+) |
2-282 |
1.13e-82 |
|
methylenetetrahydrofolate dehydrogenase (NADP+)
Pssm-ID: 178131 [Multi-domain] Cd Length: 299 Bit Score: 250.58 E-value: 1.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 2 TAQKLDGTATLKTIKAELADRVEKLKAA-GVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:PLN02516 8 VAQIIDGKAIAKAIRSEIAEEVAQLSEKhGKVPGLAVVIVGSRKDSQTYVNMKRKACAEVGIKSFDVDLPENISEAELIS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPL--PCTPVGCIELLRRHGVEING 156
Cdd:PLN02516 88 KVHELNANPDVHGILVQlpLPKHINEEKILNEISLEKDVDGFHPLNIGKLAMKGREPLflPCTPKGCLELLSRSGIPIKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 157 AEVVVVGRGLTVGRPLGLLLTRrsENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDG 236
Cdd:PLN02516 168 KKAVVVGRSNIVGLPVSLLLLK--ADATVTVVHSRTPDPESIVREADIVIAAAGQAMMIKGDWIKPGAAVIDVGTNAVSD 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1906349552 237 -------KIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQALER 282
Cdd:PLN02516 246 pskksgyRLVGDVDfAEVSKVAGWITPVPGGVGPMTVAMLLKNTVDGAKRVFAQ 299
|
|
| PRK14175 |
PRK14175 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-279 |
2.58e-82 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184552 [Multi-domain] Cd Length: 286 Bit Score: 249.45 E-value: 2.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 1 MTAQKLDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:PRK14175 1 MVAKILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAE 158
Cdd:PRK14175 81 ELNRLNNDDSVSGILVQvpLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 159 VVVVGRGLTVGRPLGLLLTRRseNATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVG-VSRVDGK 237
Cdd:PRK14175 161 AVVIGRSHIVGQPVSKLLLQK--NASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGnTPDENGK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1906349552 238 IAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQA 279
Cdd:PRK14175 239 LKGDVDyDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMR 281
|
|
| PRK14166 |
PRK14166 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-281 |
3.39e-82 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172654 [Multi-domain] Cd Length: 282 Bit Score: 248.79 E-value: 3.39e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 6 LDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGRL 85
Cdd:PRK14166 4 LDGKALSAKIKEELKEKNQFLKSKGIESCLAVILVGDNPASQTYVKSKAKACEECGIKSLVYHLNENTTQNELLALINTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 86 NADPACTGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLG-EDGPLPCTPVGCIELLRRHGVEINGAEVVVV 162
Cdd:PRK14166 84 NHDDSVHGILVQlpLPDHICKDLILESIISSKDVDGFHPINVGYLNLGlESGFLPCTPLGVMKLLKAYEIDLEGKDAVII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 163 GRGLTVGRPLGLLLTrrSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVD-GKIAGD 241
Cdd:PRK14166 164 GASNIVGRPMATMLL--NAGATVSVCHIKTKDLSLYTRQADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLEsGKIVGD 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1906349552 242 LA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQALE 281
Cdd:PRK14166 242 VDfEEVSKKSSYITPVPGGVGPMTIAMLLENTVKSAKNRLN 282
|
|
| PRK14173 |
PRK14173 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
1-277 |
5.93e-81 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 184551 [Multi-domain] Cd Length: 287 Bit Score: 245.89 E-value: 5.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 1 MTAQKLDGTATLKTIKAELADRVEKLKAagvTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:PRK14173 1 MAARELSGPPAAEAVYAELRARLAKLPF---VPHLRVVRLGEDPASVSYVRLKDRQAKALGLRSQVEVLPESTSQEELLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQQPT--GLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAE 158
Cdd:PRK14173 78 LIARLNADPEVDGILVQLPLppHIDFQRVLEAIDPLKDVDGFHPLNVGRLWMGGEALEPCTPAGVVRLLKHYGIPLAGKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 159 VVVVGRGLTVGRPLGLLLTRrsENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDGK- 237
Cdd:PRK14173 158 VVVVGRSNIVGKPLAALLLR--EDATVTLAHSKTQDLPAVTRRADVLVVAVGRPHLITPEMVRPGAVVVDVGINRVGGNg 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1906349552 238 ----IAGDLADDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAE 277
Cdd:PRK14173 236 grdiLTGDVHPEVAEVAGALTPVPGGVGPMTVAMLMANTVIAAL 279
|
|
| PRK14178 |
PRK14178 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
16-271 |
2.51e-80 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172666 [Multi-domain] Cd Length: 279 Bit Score: 243.98 E-value: 2.51e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 16 KAELADRVEKLKA----AGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGRLNADPAC 91
Cdd:PRK14178 6 KAVSEKRLELLKEeiieSGLYPRLATVIVGDDPASQMYVRMKHRACERVGIGSVGIELPGDATTRTVLERIRRLNEDPDI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 92 TGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVVVVGRGLTVG 169
Cdd:PRK14178 86 NGILVQLPlpKGVDTERVIAAILPEKDVDGFHPLNLGRLVSGLPGFAPCTPNGIMTLLHEYKISIAGKRAVVVGRSIDVG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 170 RPLGLLLTrrSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDGKIAGDLA-DDVWD 248
Cdd:PRK14178 166 RPMAALLL--NADATVTICHSKTENLKAELRQADILVSAAGKAGFITPDMVKPGATVIDVGINQVNGKLCGDVDfDAVKE 243
|
250 260
....*....|....*....|...
gi 1906349552 249 VAGWVSPNPGGVGPMTRAMLLSN 271
Cdd:PRK14178 244 IAGAITPVPGGVGPMTIATLMEN 266
|
|
| PLN02616 |
PLN02616 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
3-278 |
1.42e-79 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 215332 [Multi-domain] Cd Length: 364 Bit Score: 244.91 E-value: 1.42e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 3 AQKLDGTATLKTIKAELADRVEKLKAA-GVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAE 81
Cdd:PLN02616 73 AKVIDGKAVAKKIRDEITIEVSRMKESiGVVPGLAVILVGDRKDSATYVRNKKKACDSVGINSFEVRLPEDSTEQEVLKF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 82 IGRLNADPACTGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPL--PCTPVGCIELLRRHGVEINGA 157
Cdd:PLN02616 153 ISGFNNDPSVHGILVQlpLPSHMDEQNILNAVSIEKDVDGFHPLNIGRLAMRGREPLfvPCTPKGCIELLHRYNVEIKGK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 158 EVVVVGRGLTVGRPLGLLLTRrsENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDG- 236
Cdd:PLN02616 233 RAVVIGRSNIVGMPAALLLQR--EDATVSIVHSRTKNPEEITREADIIISAVGQPNMVRGSWIKPGAVVIDVGINPVEDa 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1906349552 237 ------KIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQ 278
Cdd:PLN02616 311 ssprgyRLVGDVCyEEACKVASAVTPVPGGVGPMTIAMLLSNTLTSAKR 359
|
|
| THF_DHG_CYH_C |
pfam02882 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain; |
121-280 |
2.38e-79 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain;
Pssm-ID: 427036 Cd Length: 160 Bit Score: 236.98 E-value: 2.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 121 HPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVVVVGRGLTVGRPLGLLLTRRseNATVTLCHTGTRDLAAHTR 200
Cdd:pfam02882 1 HPYNLGRLVLGKPCFVPCTPRGIMELLKRYGIDLAGKNVVVVGRSNIVGKPLALLLLNA--NATVTVCHSKTKDLAEITR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 201 NADIVVAAAGVPGIITKDMVKPGAALLDVGVSRV-DGKIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQ 278
Cdd:pfam02882 79 EADIVVVAVGKPELIKADWIKPGAVVIDVGINRVgNGKLVGDVDfENVKEKASAITPVPGGVGPMTVAMLLQNTVEAAKR 158
|
..
gi 1906349552 279 AL 280
Cdd:pfam02882 159 QL 160
|
|
| NAD_bind_m-THF_DH_Cyclohyd |
cd01080 |
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding ... |
113-277 |
1.71e-77 |
|
NADP binding domain of methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NADP binding domain of the Methylene-Tetrahydrofolate Dehydrogenase/cyclohydrolase (m-THF DH/cyclohydrolase) bifunctional enzyme. Tetrahydrofolate is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofucntional DH, as well as bifunctional m-THF m-THF DHm-THF DHDH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains the bifunctional DH/cyclohydrolase. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains.
Pssm-ID: 133448 Cd Length: 168 Bit Score: 232.83 E-value: 1.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 113 PEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVVVVGRGLTVGRPLGLLLTRRseNATVTLCHTGT 192
Cdd:cd01080 1 PEKDVDGLHPVNLGRLALGRPGFIPCTPAGILELLKRYGIDLAGKKVVVVGRSNIVGKPLAALLLNR--NATVTVCHSKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 193 RDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRV----DGKIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAM 267
Cdd:cd01080 79 KNLKEHTKQADIVIVAVGKPGLVKGDMVKPGAVVIDVGINRVpdksGGKLVGDVDfESAKEKASAITPVPGGVGPMTVAM 158
|
170
....*....|
gi 1906349552 268 LLSNIVLSAE 277
Cdd:cd01080 159 LMKNTVEAAK 168
|
|
| PRK14179 |
PRK14179 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; |
3-282 |
1.98e-77 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase;
Pssm-ID: 237634 [Multi-domain] Cd Length: 284 Bit Score: 236.57 E-value: 1.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 3 AQKLDGTATLKTIKAELADRVEKLKA-AGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAE 81
Cdd:PRK14179 2 TEIIDGKALAQKMQAELAEKVAKLKEeKGIVPGLVVILVGDNPASQVYVRNKERSALAAGFKSEVVRLPETISQEELLDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 82 IGRLNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEV 159
Cdd:PRK14179 82 IERYNQDPTWHGILVQLPlpKHINEEKILLAIDPKKDVDGFHPMNTGHLWSGRPVMIPCTPAGIMEMFREYNVELEGKHA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 160 VVVGRGLTVGRPLGLLLTRRseNATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSR-VDGKI 238
Cdd:PRK14179 162 VVIGRSNIVGKPMAQLLLDK--NATVTLTHSRTRNLAEVARKADILVVAIGRGHFVTKEFVKEGAVVIDVGMNRdENGKL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1906349552 239 AGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQALER 282
Cdd:PRK14179 240 IGDVDfDEVAEVASYITPVPGGVGPMTITMLMEQTYQAALRSLHK 284
|
|
| PRK14172 |
PRK14172 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
4-272 |
3.29e-77 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172660 [Multi-domain] Cd Length: 278 Bit Score: 235.83 E-value: 3.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 4 QKLDGTATLKTIKAELADRVEKLKAAG-VTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEI 82
Cdd:PRK14172 3 QIINGKEVALKIKEEIKNFVEERKENGlSIPKIASILVGNDGGSIYYMNNQEKVANSLGIDFKKIKLDESISEEDLINEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 83 GRLNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVV 160
Cdd:PRK14172 83 EELNKDNNVHGIMLQLPlpKHLDEKKITNKIDANKDIDCLTFISVGKFYKGEKCFLPCTPNSVITLIKSLNIDIEGKEVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 161 VVGRGLTVGRPLGLLLTrrSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDGKIAG 240
Cdd:PRK14172 163 VIGRSNIVGKPVAQLLL--NENATVTICHSKTKNLKEVCKKADILVVAIGRPKFIDEEYVKEGAIVIDVGTSSVNGKITG 240
|
250 260 270
....*....|....*....|....*....|...
gi 1906349552 241 DLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNI 272
Cdd:PRK14172 241 DVNfDKVIDKASYITPVPGGVGSLTTTLLIKNV 273
|
|
| PRK14192 |
PRK14192 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-280 |
9.36e-76 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184561 [Multi-domain] Cd Length: 283 Bit Score: 232.43 E-value: 9.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 1 MTAQKLDGTATLKTIKAELADRVEKLKA-AGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVE 79
Cdd:PRK14192 1 MMALVLDGKALAKQIEEELSVRVEALKAkTGRTPILATILVGDDPASATYVRMKGNACRRVGMDSLKVELPQETTTEQLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 80 AEIGRLNADPACTGFLVQQPT--GLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGA 157
Cdd:PRK14192 81 AKIEELNANPDVHGILLQHPVpaQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMRLLKAYNIELAGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 158 EVVVVGRGLTVGRPLGLLLTrrSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDGK 237
Cdd:PRK14192 161 HAVVVGRSAILGKPMAMMLL--NANATVTICHSRTQNLPELVKQADIIVGAVGKPELIKKDWIKQGAVVVDAGFHPRDGG 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1906349552 238 IAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQAL 280
Cdd:PRK14192 239 GVGDIElQGIEEIASAYTPVPGGVGPMTINTLIRQTVEAAEKAL 282
|
|
| PRK14168 |
PRK14168 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-280 |
8.77e-75 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 237633 [Multi-domain] Cd Length: 297 Bit Score: 230.53 E-value: 8.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 1 MTAQKLDGTATLKTIKAELADRVEKLKAA-GVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVE 79
Cdd:PRK14168 1 MSAKIIKGTEIREEILEEIRGEVAELKEKyGKVPGLVTILVGESPASLSYVTLKIKTAHRLGFHEIQDNQSVDITEEELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 80 AEIGRLNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGP--LPCTPVGCIELLRRHGVEIN 155
Cdd:PRK14168 81 ALIDKYNNDDSIHGILVQLPlpKHINEKKVLNAIDPDKDVDGFHPVNVGRLMIGGDEVkfLPCTPAGIQEMLVRSGVETS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 156 GAEVVVVGRGLTVGRPLGLLLTRRS--ENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSR 233
Cdd:PRK14168 161 GAEVVVVGRSNIVGKPIANMMTQKGpgANATVTIVHTRSKNLARHCQRADILIVAAGVPNLVKPEWIKPGATVIDVGVNR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1906349552 234 VDGKI-------AGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQAL 280
Cdd:PRK14168 241 VGTNEstgkailSGDVDfDAVKEIAGKITPVPGGVGPMTIAMLMRNTLKSAKFHL 295
|
|
| PRK14169 |
PRK14169 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-280 |
4.81e-73 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184550 [Multi-domain] Cd Length: 282 Bit Score: 225.59 E-value: 4.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 3 AQKLDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEI 82
Cdd:PRK14169 1 ATRLDGRAVSKKILADLKQTVAKLAQQDVTPTLAVVLVGSDPASEVYVRNKQRRAEDIGVRSLMFRLPEATTQADLLAKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 83 GRLNADPACTGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVV 160
Cdd:PRK14169 81 AELNHDPDVDAILVQlpLPAGLDEQAVIDAIDPDKDVDGFSPVSVGRLWANEPTVVASTPYGIMALLDAYDIDVAGKRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 161 VVGRGLTVGRPLGLLLTrrSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSR-VDGKIA 239
Cdd:PRK14169 161 IVGRSNIVGRPLAGLMV--NHDATVTIAHSKTRNLKQLTKEADILVVAVGVPHFIGADAVKPGAVVIDVGISRgADGKLL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1906349552 240 GDLADD-VWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQAL 280
Cdd:PRK14169 239 GDVDEAaVAPIASAITPVPGGVGPMTIASLMAQTVTLAKRRA 280
|
|
| PRK14177 |
PRK14177 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-278 |
3.06e-71 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172665 [Multi-domain] Cd Length: 284 Bit Score: 221.00 E-value: 3.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 6 LDGTATLKTIKAELADRVEKLKAAGV-TPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGR 84
Cdd:PRK14177 6 LDGKKLSEKIRNEIRETIEERKTKNKrIPKLATILVGNNPASETYVSMKVKACHKVGMGSEMIRLKEQTTTEELLGVIDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 85 LNADPACTGFLVQQPT--GLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVVVV 162
Cdd:PRK14177 86 LNLDPNVDGILLQHPVpsQIDERAAFDRIALEKDVDGVTTLSFGKLSMGVETYLPCTPYGMVLLLKEYGIDVTGKNAVVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 163 GRGLTVGRPLGLLLTRRseNATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSrvDGKIAGDL 242
Cdd:PRK14177 166 GRSPILGKPMAMLLTEM--NATVTLCHSKTQNLPSIVRQADIIVGAVGKPEFIKADWISEGAVLLDAGYN--PGNVGDIE 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 1906349552 243 ADDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQ 278
Cdd:PRK14177 242 ISKAKDKSSFYTPVPGGVGPMTIAVLLLQTLYSFKE 277
|
|
| PLN02897 |
PLN02897 |
tetrahydrofolate dehydrogenase/cyclohydrolase, putative |
2-279 |
9.48e-71 |
|
tetrahydrofolate dehydrogenase/cyclohydrolase, putative
Pssm-ID: 178485 [Multi-domain] Cd Length: 345 Bit Score: 221.76 E-value: 9.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 2 TAQKLDGTATLKTIKAELADRVEKLKAA-GVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:PLN02897 55 KTVVIDGNVIAEEIRTKIASEVRKMKKAvGKVPGLAVVLVGQQRDSQTYVRNKIKACEETGIKSLLAELPEDCTEGQILS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPL--PCTPVGCIELLRRHGVEING 156
Cdd:PLN02897 135 ALRKFNEDTSIHGILVQlpLPQHLDESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLfvSCTPKGCVELLIRSGVEIAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 157 AEVVVVGRGLTVGRPLGLLLTRrsENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDG 236
Cdd:PLN02897 215 KNAVVIGRSNIVGLPMSLLLQR--HDATVSTVHAFTKDPEQITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVED 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1906349552 237 -------KIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQA 279
Cdd:PLN02897 293 sscefgyRLVGDVCyEEALGVASAITPVPGGVGPMTITMLLCNTLDAAKRI 343
|
|
| PRK14182 |
PRK14182 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-273 |
3.53e-70 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172670 [Multi-domain] Cd Length: 282 Bit Score: 218.35 E-value: 3.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 6 LDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGRL 85
Cdd:PRK14182 4 IDGKQIAAKVKGEVATEVRALAARGVQTGLTVVRVGDDPASAIYVRGKRKDCEEVGITSVEHHLPATTTQAELLALIARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 86 NADPACTGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDG-PLPCTPVGCIELLRRHGVEINGAEVVVV 162
Cdd:PRK14182 84 NADPAVHGILVQlpLPKHVDERAVLDAISPAKDADGFHPFNVGALSIGIAGvPRPCTPAGVMRMLDEARVDPKGKRALVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 163 GRGLTVGRPLGLLLTRRseNATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRV-DGKIAGD 241
Cdd:PRK14182 164 GRSNIVGKPMAMMLLER--HATVTIAHSRTADLAGEVGRADILVAAIGKAELVKGAWVKEGAVVIDVGMNRLaDGKLVGD 241
|
250 260 270
....*....|....*....|....*....|...
gi 1906349552 242 LA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIV 273
Cdd:PRK14182 242 VEfAAAAARASAITPVPGGVGPMTRAMLLVNTV 274
|
|
| PRK14171 |
PRK14171 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-273 |
4.06e-70 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172659 [Multi-domain] Cd Length: 288 Bit Score: 218.29 E-value: 4.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 6 LDGTATLKTIKAELADRVEKLKA-AGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGR 84
Cdd:PRK14171 5 IDGKALANEILADLKLEIQELKSqTNASPKLAIVLVGDNPASIIYVKNKIKNAHKIGIDTLLVNLSTTIHTNDLISKINE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 85 LNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLG-EDGPLPCTPVGCIELLRRHGVEINGAEVVV 161
Cdd:PRK14171 85 LNLDNEISGIIVQLPlpSSIDKNKILSAVSPSKDIDGFHPLNVGYLHSGiSQGFIPCTALGCLAVIKKYEPNLTGKNVVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 162 VGRGLTVGRPLGLLLTRrsENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDG-KIAG 240
Cdd:PRK14171 165 IGRSNIVGKPLSALLLK--ENCSVTICHSKTHNLSSITSKADIVVAAIGSPLKLTAEYFNPESIVIDVGINRISGnKIIG 242
|
250 260 270
....*....|....*....|....*....|....
gi 1906349552 241 DLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIV 273
Cdd:PRK14171 243 DVDfENVKSKVKYITPVPGGIGPMTIAFLLKNTV 276
|
|
| PRK14181 |
PRK14181 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
17-271 |
2.64e-68 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172669 [Multi-domain] Cd Length: 287 Bit Score: 213.57 E-value: 2.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 17 AELADRV-----EKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGRLNADPAC 91
Cdd:PRK14181 6 APAAEHIlatikENISASSTAPGLAVVLIGNDPASEVYVGMKVKKATDLGMVSKAHRLPSDATLSDILKLIHRLNNDPNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 92 TGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGE-DGPLPCTPVGCIELLRRHGVEINGAEVVVVGRGLTV 168
Cdd:PRK14181 86 HGILVQlpLPKHLDAQAILQAISPDKDVDGLHPVNMGKLLLGEtDGFIPCTPAGIIELLKYYEIPLHGRHVAIVGRSNIV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 169 GRPLGLLLTRR--SENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDGK------IAG 240
Cdd:PRK14181 166 GKPLAALLMQKhpDTNATVTLLHSQSENLTEILKTADIIIAAIGVPLFIKEEMIAEKAVIVDVGTSRVPAAnpkgyiLVG 245
|
250 260 270
....*....|....*....|....*....|..
gi 1906349552 241 DLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSN 271
Cdd:PRK14181 246 DVDfNNVVPKCRAITPVPGGVGPMTVAMLMRN 277
|
|
| PRK14185 |
PRK14185 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
4-282 |
2.18e-67 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 184556 [Multi-domain] Cd Length: 293 Bit Score: 211.23 E-value: 2.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 4 QKLDGTATLKTIKAELADRVEKLKAAG-VTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEI 82
Cdd:PRK14185 2 QLIDGKAISAQIKQEIAAEVAEIVAKGgKRPHLAAILVGHDGGSETYVANKVKACEECGFKSSLIRYESDVTEEELLAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 83 GRLNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVV 160
Cdd:PRK14185 82 RELNQDDDVDGFIVQLPlpKHISEQKVIEAIDYRKDVDGFHPINVGRMSIGLPCFVSATPNGILELLKRYHIETSGKKCV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 161 VVGRGLTVGRPLGLLLTRRSE--NATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDG-- 236
Cdd:PRK14185 162 VLGRSNIVGKPMAQLMMQKAYpgDCTVTVCHSRSKNLKKECLEADIIIAALGQPEFVKADMVKEGAVVIDVGTTRVPDat 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1906349552 237 -----KIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQALER 282
Cdd:PRK14185 242 rksgfKLTGDVKfDEVAPKCSYITPVPGGVGPMTIVSLMKNTLLAGKKAIYK 293
|
|
| PRK14194 |
PRK14194 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
1-278 |
2.73e-67 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172682 [Multi-domain] Cd Length: 301 Bit Score: 211.24 E-value: 2.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 1 MTAQKLDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEA 80
Cdd:PRK14194 2 MSAKLIDGKAAAARVLAQVREDVRTLKAAGIEPALAVILVGNDPASQVYVRNKILRAEEAGIRSLEHRLPADTSQARLLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 81 EIGRLNADPACTGFLVQ--QPTGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAE 158
Cdd:PRK14194 82 LIAELNADPSVNGILLQlpLPAHIDEARVLQAINPLKDVDGFHSENVGGLSQGRDVLTPCTPSGCLRLLEDTCGDLTGKH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 159 VVVVGRGLTVGRPLGLLLTRrsENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVD--- 235
Cdd:PRK14194 162 AVVIGRSNIVGKPMAALLLQ--AHCSVTVVHSRSTDAKALCRQADIVVAAVGRPRLIDADWLKPGAVVIDVGINRIDddg 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1906349552 236 -GKIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQ 278
Cdd:PRK14194 240 rSRLVGDVDfDSALPVVSAITPVPGGVGPMTIAFLMKNTVTAARL 284
|
|
| PRK14180 |
PRK14180 |
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ... |
6-278 |
1.30e-66 |
|
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
Pssm-ID: 172668 [Multi-domain] Cd Length: 282 Bit Score: 209.12 E-value: 1.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 6 LDGTATLKTIKAELADRVEKLK-AAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGR 84
Cdd:PRK14180 4 IDGKSLSKDLKERLATQVQEYKhHTAITPKLVAIIVGNDPASKTYVASKEKACAQVGIDSQVITLPEHTTESELLELIDQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 85 LNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPL-PCTPVGCIELLRRHGVEINGAEVVV 161
Cdd:PRK14180 84 LNNDSSVHAILVQLPlpAHINKNNVIYSIKPEKDVDGFHPTNVGRLQLRDKKCLeSCTPKGIMTMLREYGIKTEGAYAVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 162 VGRGLTVGRPLGLLLTrrSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVDGKIAGD 241
Cdd:PRK14180 164 VGASNVVGKPVSQLLL--NAKATVTTCHRFTTDLKSHTTKADILIVAVGKPNFITADMVKEGAVVIDVGINHVDGKIVGD 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 1906349552 242 LA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQ 278
Cdd:PRK14180 242 VDfAAVKDKVAAITPVPGGVGPMTITELLYNTFQCAQE 279
|
|
| PRK14170 |
PRK14170 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
3-278 |
2.32e-66 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172658 [Multi-domain] Cd Length: 284 Bit Score: 208.39 E-value: 2.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 3 AQKLDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEI 82
Cdd:PRK14170 2 GEIIDGKKLAKEIQEKVTREVAELVKEGKKPGLAVVLVGDNQASRTYVRNKQKRTEEAGMKSVLIELPENVTEEKLLSVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 83 GRLNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGEDGPLPCTPVGCIELLRRHGVEINGAEVV 160
Cdd:PRK14170 82 EELNEDKTIHGILVQLPlpEHISEEKVIDTISYDKDVDGFHPVNVGNLFIGKDSFVPCTPAGIIELIKSTGTQIEGKRAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 161 VVGRGLTVGRPLGLLLTrrSENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSR-VDGKIA 239
Cdd:PRK14170 162 VIGRSNIVGKPVAQLLL--NENATVTIAHSRTKDLPQVAKEADILVVATGLAKFVKKDYIKPGAIVIDVGMDRdENNKLC 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1906349552 240 GDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAEQ 278
Cdd:PRK14170 240 GDVDfDDVVEEAGFITPVPGGVGPMTITMLLANTLKAAKR 279
|
|
| PRK14187 |
PRK14187 |
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase ... |
6-276 |
4.41e-61 |
|
bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD;
Pssm-ID: 172675 [Multi-domain] Cd Length: 294 Bit Score: 195.43 E-value: 4.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 6 LDGTATLKTIKAELADRVEKLKAA-GVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGR 84
Cdd:PRK14187 5 IDGKKIANDITEILATCIDDLKRQhNLFPCLIVILVGDDPASQLYVRNKQRKAEMLGLRSETILLPSTISESSLIEKINE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 85 LNADPACTGFLVQQP--TGLDEFALLSRVAPEKDVDGLHPHNLGKLVLGE--DGPLPCTPVGCIELLRRHGVEINGAEVV 160
Cdd:PRK14187 85 LNNDDSVHGILVQLPvpNHIDKNLIINTIDPEKDVDGFHNENVGRLFTGQkkNCLIPCTPKGCLYLIKTITRNLSGSDAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 161 VVGRGLTVGRPLGLLLTRrsENATVTLCHTGTRDLAAHTRNADIVVAAAGVPGIITKDMVKPGAALLDVGVSRVD----G 236
Cdd:PRK14187 165 VIGRSNIVGKPMACLLLG--ENCTVTTVHSATRDLADYCSKADILVAAVGIPNFVKYSWIKKGAIVIDVGINSIEeggvK 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1906349552 237 KIAGDLA-DDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSA 276
Cdd:PRK14187 243 KFVGDVDfAEVKKKASAITPVPGGVGPMTIAFLMVNTVIAA 283
|
|
| THF_DHG_CYH |
pfam00763 |
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain; |
6-118 |
4.61e-51 |
|
Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain;
Pssm-ID: 459930 [Multi-domain] Cd Length: 115 Bit Score: 163.34 E-value: 4.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 6 LDGTATLKTIKAELADRVEKLKAAGVTPGLGTVLVGDDPGSRWYVNAKHKDCAEIGIESIRVDLPGTSTQEEVEAEIGRL 85
Cdd:pfam00763 1 IDGKAIAKKIREELKEEVAALKAGGRKPGLAVILVGDDPASQVYVRNKKKACEEVGIESELIRLPEDTTEEELLALIDKL 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1906349552 86 NADPACTGFLVQQP--TGLDEFALLSRVAPEKDVD 118
Cdd:pfam00763 81 NADPSVHGILVQLPlpKHIDEEKVLEAIDPEKDVD 115
|
|
| NAD_bind_m-THF_DH_Cyclohyd_like |
cd05212 |
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and ... |
136-277 |
1.55e-22 |
|
NAD(P) binding domain of methylene-tetrahydrofolate dehydrogenase and methylene-tetrahydrofolate dehydrogenase/cyclohydrolase; NAD(P) binding domains of methylene-tetrahydrofolate dehydrogenase (m-THF DH) and m-THF DH/cyclohydrolase bifunctional enzymes (m-THF DH/cyclohydrolase). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. In addition, most DHs also have an associated cyclohydrolase activity which catalyzes its hydrolysis to N10-formyltetrahydrofolate. m-THF DH is typically found as part of a multifunctional protein in eukaryotes. NADP-dependent m-THF DH in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, mono-functional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express a monofunctional DH. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133451 Cd Length: 140 Bit Score: 90.64 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 136 LPCTPVGC-------IELLRRHGVEINGAEVVVVGRGLTVGRPLGLLLTRRseNATVTLCHTGTRDLAAHTRNADIVVAA 208
Cdd:cd05212 1 GPCTPLFVspvakavKELLNKEGVRLDGKKVLVVGRSGIVGAPLQCLLQRD--GATVYSCDWKTIQLQSKVHDADVVVVG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1906349552 209 AGVPGIITKDMVKPGAALLDVGVSRVDGkiagdlaDDVWDVAGWVSPNPGGVGPMTRAMLLSNIVLSAE 277
Cdd:cd05212 79 SPKPEKVPTEWIKPGATVINCSPTKLSG-------DDVKESASLYVPMTGGVGKLTVAMRMQNMVRSVR 140
|
|
| NAD_bind_m-THF_DH |
cd01079 |
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of ... |
113-273 |
6.50e-10 |
|
NAD binding domain of methylene-tetrahydrofolate dehydrogenase; The NAD-binding domain of methylene-tetrahydrofolate dehydrogenase (m-THF DH). M-THF is a versatile carrier of activated one-carbon units. The major one-carbon folate donors are N-5 methyltetrahydrofolate, N5,N10-m-THF, and N10-formayltetrahydrofolate. The oxidation of metabolic intermediate m-THF to m-THF requires the enzyme m-THF DH. M-THF DH is a component of an unusual monofunctional enzyme; in eukaryotes, m-THF DH is typically found as part of a multifunctional protein. NADP-dependent m-THF DHs in mammals, birds and yeast are components of a trifunctional enzyme with DH, cyclohydrolase, and synthetase activities. Certain eukaryotic cells also contain homodimeric bifunctional DH/cyclodrolase form. In bacteria, monofunctional DH, as well as bifunctional DH/cyclodrolase are found. In addition, yeast (S. cerevisiae) also express an monofunctional DH. This family contains only the monofunctional DHs from S. cerevisiae and certain bacteria. M-THF DH, like other amino acid DH-like NAD(P)-binding domains, is a member of the Rossmann fold superfamily which includes glutamate, leucine, and phenylalanine DHs, m-THF DH, methylene-tetrahydromethanopterin DH, m-THF DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133447 [Multi-domain] Cd Length: 197 Bit Score: 57.44 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 113 PEKDVDGLHPHNLGKLVLGE---DGP------LPCTP---VGCIELLRRH------GVEINGAEVVVVGRGLTVGRPLGL 174
Cdd:cd01079 1 PHKDVEGLSHKYIFNLYHNIrflDPEnrkksiLPCTPlaiVKILEFLGIYnkilpyGNRLYGKTITIINRSEVVGRPLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 175 LLTrrSENATV-------TLCHTGTRDLAAHTRN--------------ADIVVaaAGVPGIITK---DMVKPGAALLDVG 230
Cdd:cd01079 81 LLA--NDGARVysvdingIQVFTRGESIRHEKHHvtdeeamtldclsqSDVVI--TGVPSPNYKvptELLKDGAICINFA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1906349552 231 VSRVDGkiagdlaDDVWDVAGWVSPNpggVGPMTRAMLLSNIV 273
Cdd:cd01079 157 SIKNFE-------PSVKEKASIYVPS---IGKVTIAMLLRNLL 189
|
|
| COG5322 |
COG5322 |
Predicted amino acid dehydrogenase [General function prediction only]; |
147-230 |
2.84e-05 |
|
Predicted amino acid dehydrogenase [General function prediction only];
Pssm-ID: 444114 [Multi-domain] Cd Length: 362 Bit Score: 44.83 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 147 LRRHGVEINGAEVVVVG------------------RGLTVGRPLGLLLT-----RRSENATVTLchtgTRDLAAHTRNAD 203
Cdd:COG5322 142 AERMGIDLKKATVAVVGatgsigsvcarllarevkRLTLVARNLERLEElaeeiLRNPGGKVTI----TTDIDEALREAD 217
|
90 100
....*....|....*....|....*...
gi 1906349552 204 IVVAAAGVPG-IITKDMVKPGAALLDVG 230
Cdd:COG5322 218 IVVTVTSAVGaIIDPEDLKPGAVVCDVA 245
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
156-229 |
1.72e-04 |
|
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: 40.95 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 156 GAEVVVVGRGLTVGRPLGLLLtrrseNATVTLCHTGTRDLAAHTRNADIVVAAAGVPG-----IITKDMV---KPGAALL 227
Cdd:smart01002 43 GAEVTVLDVRPARLRQLESLL-----GARFTTLYSQAELLEEAVKEADLVIGAVLIPGakapkLVTREMVksmKPGSVIV 117
|
..
gi 1906349552 228 DV 229
Cdd:smart01002 118 DV 119
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
195-231 |
5.79e-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: 37.09 E-value: 5.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1906349552 195 LAAHTRNADIVVAAAGVPG-----IITKDMV---KPGAALLDVGV 231
Cdd:pfam01262 86 IAEAVKEADLVIGTALIPGakapkLVTREMVksmKPGSVIVDVAI 130
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
156-229 |
9.39e-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: 37.00 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906349552 156 GAEVVVVGRGLTVGRPLGLLLTRRsenatVTLCHTGTRDLAAHTRNADIVVAAAGVPG-----IITKDMV---KPGAALL 227
Cdd:cd05305 191 GAEVTVLDINLERLRYLDDIFGGR-----VTTLYSNPANLEEALKEADLVIGAVLIPGakapkLVTEEMVktmKPGSVIV 265
|
..
gi 1906349552 228 DV 229
Cdd:cd05305 266 DV 267
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
195-233 |
9.87e-03 |
|
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: 37.00 E-value: 9.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1906349552 195 LAAHTRNADIVVAAAGVPG-----IITKDMV---KPGAALLDVGVSR 233
Cdd:cd05304 243 LAKHIAEADIVITTALIPGrkapkLITKEMVesmKPGSVIVDLAAEQ 289
|
|
| |
