|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
110-578 |
1.21e-143 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 423.54 E-value: 1.21e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 110 VVEDLKQVLgnkPENYSDAKSDLDAHSdTYFNTHHPspeQRPRIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSLEGH 189
Cdd:COG0277 6 LLAALRAIL---AGRVLTDPADRAAYA-RDGNSLYR---GRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 190 FLPTriGDTITVDLSKfMNNVVKFDKLDLDITVQAGLPWEDLNDYLSDHGLMFGCDPG--PGAQIGGCIANSCSGTNAYR 267
Cdd:COG0277 79 AVPL--DGGVVLDLSR-MNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSsqGTATIGGNIATNAGGPRSLK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 268 YGTMKENIINMTIVLPDGTIVKTKKRPRKSSAGYNLNGLFVGSEGTLGIVTEATVKCHVKPKAETVAVVSFDTIKDAAAC 347
Cdd:COG0277 156 YGLTRDNVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 348 ASNLTQSGIHLNAMELLDENMMKLINASESTdRCDWVEKPTMFFKIGGRSPNIVNALVDEVKAVAQLNHCNSFQFAKDDD 427
Cdd:COG0277 236 VRALLAAGIAPAALELMDRAALALVEAAPPL-GLPEDGGALLLVEFDGDDAEEVEAQLARLRAILEAGGATDVRVAADGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 428 EKLELWEARKVALWSVLDADkskdkSAKIWTTDVAVPVSQFDKVIHETKKDMQASKLINAIVGHAGDGNFHAFIVY--RT 505
Cdd:COG0277 315 ERERLWKARKAALPALGRLD-----GGAKLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFdpAD 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320027 506 PEEHETCSQLVDRMVKRALNAEGTCTGEHGVGIGKREYLLEELGEAPVDLMRKIKLAIDPKRIMNPDKIFKTD 578
Cdd:COG0277 390 PEEVERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
49-574 |
1.85e-127 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 385.52 E-value: 1.85e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 49 IASSATLFGYLFAKNLysretkeDLIEKLEMVKKIDPVNST---LKLSSLDSPDYLhdpvkidkvVEDLKQVLGNkpeny 125
Cdd:PLN02805 50 IAASAGSLAYLNQSNP-------SLCDSSDLDSRVGGKGSTefvVKGEHKLVPQEL---------IDELKAILQD----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 126 sDAKSDLDahsDTYFnthHPSPEQR-------PRIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSLEGHFLPTRIGdt 198
Cdd:PLN02805 109 -NMTLDYD---ERYF---HGKPQNSfhkavniPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGG-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 199 ITVDLSkFMNNVVKFDKLDLDITVQAGLPWEDLNDYLSDHGLMFGCDPGPGAQIGGCIANSCSGTNAYRYGTMKENIINM 278
Cdd:PLN02805 180 VCIDMS-LMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPGPGATIGGMCATRCSGSLAVRYGTMRDNVISL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 279 TIVLPDGTIVKTKKRPRKSSAGYNLNGLFVGSEGTLGIVTEATVKCHVKPKAETVAVVSFDTIKDAAACASNLTQSGIHL 358
Cdd:PLN02805 259 KVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATMLSGIQV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 359 NAMELLDENMMKLINASESTdrcDWVEKPTMFFK-IGGRSPNIVNALVdeVKAVAQLNHCNSFQFAKDDDEKLELWEARK 437
Cdd:PLN02805 339 SRVELLDEVQIRAINMANGK---NLPEAPTLMFEfIGTEAYAREQTLI--VQKIASKHNGSDFVFAEEPEAKKELWKIRK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 438 VALWSVLDADKSKDksAKIwtTDVAVPVSQFDKVIHETKKDMQASKLINAIVGHAGDGNFHAFIVYR-TPEEHETCSQLV 516
Cdd:PLN02805 414 EALWACFAMEPKYE--AMI--TDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFDpSQEDQRREAERL 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 6320027 517 DR-MVKRALNAEGTCTGEHGVGIGKREYLLEELGEAPVDLMRKIKLAIDPKRIMNPDKI 574
Cdd:PLN02805 490 NHfMVHTALSMEGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKL 548
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
327-574 |
1.47e-63 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 209.09 E-value: 1.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 327 KPKAETVAVVSFDTIKDAAACASNLTQSGIHLNAMELLDENMMKLINA-SESTDRCDWVEKPTMFFKIGGRSPNIVNALV 405
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEAtLGFPKGLPRDAAALLLVEFEGDDEETAEEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 406 DEVKAVAQLNHCNSFQFAKDDDEKLELWEARKVALWSVLDADKSKdksAKIWTTDVAVPVSQFDKVIHETKKDMQASKLI 485
Cdd:pfam02913 81 EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPLRDALGGAG---PAVFSEDVSVPRSRLADLVRDIKELLDKYGLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 486 NAIVGHAGDGNFHAFIVY--RTPEEHETCSQLVDRMVKRALNAEGTCTGEHGVGIGKREYLLEELGEAPVDLMRKIKLAI 563
Cdd:pfam02913 158 VCLFGHAGDGNLHLYILFdfRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAF 237
|
250
....*....|.
gi 6320027 564 DPKRIMNPDKI 574
Cdd:pfam02913 238 DPKGILNPGKV 248
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
157-324 |
8.11e-12 |
|
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
Pssm-ID: 273751 [Multi-domain] Cd Length: 438 Bit Score: 67.62 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 157 PHTTEEVSKILKICHDNNMPVVPFSGGTSleghflPTRIG--DTITVDLSKfMNNVVKFDKLDLDITVQAGLPWEDLNDY 234
Cdd:TIGR01678 21 PTSVEEVREVLALAREQKKKVKVVGGGHS------PSDIActDGFLIHLDK-MNKVLQFDKEKKQITVEAGIRLYQLHEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 235 LSDHGLMFgcdPGPGA----QIGGCIANSCSGTNAYrYGTMKENIINMTIVLPDGTIVKTKKRPRKSsagynlngLFVG- 309
Cdd:TIGR01678 94 LDEHGYSM---SNLGSisevSVAGIISTGTHGSSIK-HGILATQVVALTIMTADGEVLECSEERNAD--------VFQAa 161
|
170
....*....|....*..
gi 6320027 310 --SEGTLGIVTEATVKC 324
Cdd:TIGR01678 162 rvSLGCLGIIVTVTIQV 178
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
110-578 |
1.21e-143 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 423.54 E-value: 1.21e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 110 VVEDLKQVLgnkPENYSDAKSDLDAHSdTYFNTHHPspeQRPRIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSLEGH 189
Cdd:COG0277 6 LLAALRAIL---AGRVLTDPADRAAYA-RDGNSLYR---GRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 190 FLPTriGDTITVDLSKfMNNVVKFDKLDLDITVQAGLPWEDLNDYLSDHGLMFGCDPG--PGAQIGGCIANSCSGTNAYR 267
Cdd:COG0277 79 AVPL--DGGVVLDLSR-MNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSsqGTATIGGNIATNAGGPRSLK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 268 YGTMKENIINMTIVLPDGTIVKTKKRPRKSSAGYNLNGLFVGSEGTLGIVTEATVKCHVKPKAETVAVVSFDTIKDAAAC 347
Cdd:COG0277 156 YGLTRDNVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 348 ASNLTQSGIHLNAMELLDENMMKLINASESTdRCDWVEKPTMFFKIGGRSPNIVNALVDEVKAVAQLNHCNSFQFAKDDD 427
Cdd:COG0277 236 VRALLAAGIAPAALELMDRAALALVEAAPPL-GLPEDGGALLLVEFDGDDAEEVEAQLARLRAILEAGGATDVRVAADGA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 428 EKLELWEARKVALWSVLDADkskdkSAKIWTTDVAVPVSQFDKVIHETKKDMQASKLINAIVGHAGDGNFHAFIVY--RT 505
Cdd:COG0277 315 ERERLWKARKAALPALGRLD-----GGAKLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFdpAD 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6320027 506 PEEHETCSQLVDRMVKRALNAEGTCTGEHGVGIGKREYLLEELGEAPVDLMRKIKLAIDPKRIMNPDKIFKTD 578
Cdd:COG0277 390 PEEVERARAAAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
49-574 |
1.85e-127 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 385.52 E-value: 1.85e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 49 IASSATLFGYLFAKNLysretkeDLIEKLEMVKKIDPVNST---LKLSSLDSPDYLhdpvkidkvVEDLKQVLGNkpeny 125
Cdd:PLN02805 50 IAASAGSLAYLNQSNP-------SLCDSSDLDSRVGGKGSTefvVKGEHKLVPQEL---------IDELKAILQD----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 126 sDAKSDLDahsDTYFnthHPSPEQR-------PRIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSLEGHFLPTRIGdt 198
Cdd:PLN02805 109 -NMTLDYD---ERYF---HGKPQNSfhkavniPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGG-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 199 ITVDLSkFMNNVVKFDKLDLDITVQAGLPWEDLNDYLSDHGLMFGCDPGPGAQIGGCIANSCSGTNAYRYGTMKENIINM 278
Cdd:PLN02805 180 VCIDMS-LMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPGPGATIGGMCATRCSGSLAVRYGTMRDNVISL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 279 TIVLPDGTIVKTKKRPRKSSAGYNLNGLFVGSEGTLGIVTEATVKCHVKPKAETVAVVSFDTIKDAAACASNLTQSGIHL 358
Cdd:PLN02805 259 KVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATMLSGIQV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 359 NAMELLDENMMKLINASESTdrcDWVEKPTMFFK-IGGRSPNIVNALVdeVKAVAQLNHCNSFQFAKDDDEKLELWEARK 437
Cdd:PLN02805 339 SRVELLDEVQIRAINMANGK---NLPEAPTLMFEfIGTEAYAREQTLI--VQKIASKHNGSDFVFAEEPEAKKELWKIRK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 438 VALWSVLDADKSKDksAKIwtTDVAVPVSQFDKVIHETKKDMQASKLINAIVGHAGDGNFHAFIVYR-TPEEHETCSQLV 516
Cdd:PLN02805 414 EALWACFAMEPKYE--AMI--TDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFDpSQEDQRREAERL 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 6320027 517 DR-MVKRALNAEGTCTGEHGVGIGKREYLLEELGEAPVDLMRKIKLAIDPKRIMNPDKI 574
Cdd:PLN02805 490 NHfMVHTALSMEGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKL 548
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
327-574 |
1.47e-63 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 209.09 E-value: 1.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 327 KPKAETVAVVSFDTIKDAAACASNLTQSGIHLNAMELLDENMMKLINA-SESTDRCDWVEKPTMFFKIGGRSPNIVNALV 405
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEAtLGFPKGLPRDAAALLLVEFEGDDEETAEEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 406 DEVKAVAQLNHCNSFQFAKDDDEKLELWEARKVALWSVLDADKSKdksAKIWTTDVAVPVSQFDKVIHETKKDMQASKLI 485
Cdd:pfam02913 81 EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPLRDALGGAG---PAVFSEDVSVPRSRLADLVRDIKELLDKYGLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 486 NAIVGHAGDGNFHAFIVY--RTPEEHETCSQLVDRMVKRALNAEGTCTGEHGVGIGKREYLLEELGEAPVDLMRKIKLAI 563
Cdd:pfam02913 158 VCLFGHAGDGNLHLYILFdfRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAF 237
|
250
....*....|.
gi 6320027 564 DPKRIMNPDKI 574
Cdd:pfam02913 238 DPKGILNPGKV 248
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
150-573 |
1.12e-42 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 159.94 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 150 RPRIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSLEGHFLPTRIGdtITVDLSKFmNNVVKFDKLDLDITVQAGLPWE 229
Cdd:PRK11230 55 RPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKG--VLLVMARF-NRILDINPVGRRARVQPGVRNL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 230 DLNDYLSDHGLMFGCDPGP--GAQIGGCIANSCSGTNAYRYGTMKENIINMTIVLPDGTIVkTKKRPRKSSAGYNLNGLF 307
Cdd:PRK11230 132 AISQAAAPHGLYYAPDPSSqiACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEAL-TLGSDALDSPGFDLLALF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 308 VGSEGTLGIVTEATVKCHVKPKAETVAVVSFDTIKDAAACASNLTQSGIHLNAMELLDeNMMklINASESTDRCDW-VEK 386
Cdd:PRK11230 211 TGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMD-NLS--IRAAEDFIHAGYpVDA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 387 PTMFFKIGGRSPNIVNALVDEVKAVAQLNHCNSFQFAKDDDEKLELWEARKVALWSVldadksKDKSAKIWTTDVAVPVS 466
Cdd:PRK11230 288 EAILLCELDGVESDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGRKNAFPAV------GRISPDYYCMDGTIPRR 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 467 QFDKVIHETKKDMQASKLINAIVGHAGDGNFHAFIVY--RTPEEHETCSQLVDRMVKRALNAEGTCTGEHGVGIGKREYL 544
Cdd:PRK11230 362 ELPGVLEGIARLSQQYGLRVANVFHAGDGNMHPLILFdaNEPGELERAEALGGKILELCVEVGGSITGEHGVGREKINQM 441
|
410 420
....*....|....*....|....*....
gi 6320027 545 LEELGEAPVDLMRKIKLAIDPKRIMNPDK 573
Cdd:PRK11230 442 CAQFNSDEITLFHAVKAAFDPDGLLNPGK 470
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
151-290 |
9.89e-42 |
|
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
Pssm-ID: 426326 [Multi-domain] Cd Length: 139 Bit Score: 146.96 E-value: 9.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 151 PRIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSLEGHFLPTrigDTITVDLSKfMNNVVKFDKLDLDITVQAGLPWED 230
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQT---GGIVLDLSR-LNGILEIDPEDGTATVEAGVTLGD 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6320027 231 LNDYLSDHGLMFGCDPGPG--AQIGGCIANSCSGTNAYRYGTMKENIINMTIVLPDGTIVKT 290
Cdd:pfam01565 77 LVRALAAKGLLLGLDPGSGipGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRL 138
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
157-324 |
8.11e-12 |
|
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
Pssm-ID: 273751 [Multi-domain] Cd Length: 438 Bit Score: 67.62 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 157 PHTTEEVSKILKICHDNNMPVVPFSGGTSleghflPTRIG--DTITVDLSKfMNNVVKFDKLDLDITVQAGLPWEDLNDY 234
Cdd:TIGR01678 21 PTSVEEVREVLALAREQKKKVKVVGGGHS------PSDIActDGFLIHLDK-MNKVLQFDKEKKQITVEAGIRLYQLHEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 235 LSDHGLMFgcdPGPGA----QIGGCIANSCSGTNAYrYGTMKENIINMTIVLPDGTIVKTKKRPRKSsagynlngLFVG- 309
Cdd:TIGR01678 94 LDEHGYSM---SNLGSisevSVAGIISTGTHGSSIK-HGILATQVVALTIMTADGEVLECSEERNAD--------VFQAa 161
|
170
....*....|....*..
gi 6320027 310 --SEGTLGIVTEATVKC 324
Cdd:TIGR01678 162 rvSLGCLGIIVTVTIQV 178
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
125-324 |
1.44e-11 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 67.18 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 125 YSDAKSDLDAHSDT-----YFNTHHPSPeqrpRIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSLEGHFLpTRIGdti 199
Cdd:PLN02465 70 NAKHKKAAPLPEDLhtvsnWSGTHEVQT----RRYHQPESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAF-SREG--- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 200 TVDLSkFMNNVVKFDKLDLDITVQAGLPWEDLNDYLSDHGLMFgcdPGPGA----QIGGCIANSCSGTNAyRYGTMKENI 275
Cdd:PLN02465 142 MVNLA-LMDKVLEVDKEKKRVTVQAGARVQQVVEALRPHGLTL---QNYASireqQIGGFIQVGAHGTGA-RIPPIDEQV 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6320027 276 INMTIVLP-DGTIVKTK-KRPrkssagynlnGLF----VGSeGTLGIVTEATVKC 324
Cdd:PLN02465 217 VSMKLVTPaKGTIELSKeDDP----------ELFrlarCGL-GGLGVVAEVTLQC 260
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
210-332 |
8.31e-11 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 63.70 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 210 VVKFDKLDLDITVQAGLPWEDLNDYLSDHGLMFGCDP---GPGAQIGGCIANSCSGTNAYRYGTMKENIINMTIVLPDGT 286
Cdd:PRK11282 49 IVSYDPTELVITARAGTPLAELEAALAEAGQMLPFEPphfGGGATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGE 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 6320027 287 IVKTKKRPRKSSAGYNLNGLFVGSEGTLGIVTEATVKCHVKPKAET 332
Cdd:PRK11282 129 HLRFGGQVMKNVAGYDVSRLMAGSLGTLGVLLEVSLKVLPRPRAEL 174
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
122-324 |
6.56e-10 |
|
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase (EC 1.3.2.3). This enzyme catalyzes the final step in ascorbic acid biosynthesis in higher plants. This protein is homologous to ascorbic acid biosynthesis enzymes of other species: L-gulono-gamma-lactone oxidase in rat and L-galactono-gamma-lactone oxidase in yeast. All three covalently bind the cofactor FAD.
Pssm-ID: 130737 [Multi-domain] Cd Length: 541 Bit Score: 61.62 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 122 PENYSDAKSDL--------DAHSDTYFNTHHpspEQRPRIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSLEGHFLpT 193
Cdd:TIGR01676 28 PENAKHKKAQIfryaplpdDLHTVSNWSGTH---EVLTRTFHQPEAIEELEGIVKQANEKKARIRPVGSGLSPNGIGL-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 194 RIGdtiTVDLSkFMNNVVKFDKLDLDITVQAGLPWEDLNDYLSDHGLMFGCDPG-PGAQIGGCIANSCSGTNAyRYGTMK 272
Cdd:TIGR01676 104 RAG---MVNLA-LMDKVLEVDEEKKRVRVQAGIRVQQLVDAIKEYGITLQNFASiREQQIGGIIQVGAHGTGA-KLPPID 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6320027 273 ENIINMTIVLP-DGTI-VKTKKRPRkssagynlngLFVGSE---GTLGIVTEATVKC 324
Cdd:TIGR01676 179 EQVIAMKLVTPaKGTIeISKDKDPE----------LFFLARcglGGLGVVAEVTLQC 225
|
|
| MurB |
COG0812 |
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ... |
152-288 |
3.41e-05 |
|
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylenolpyruvoylglucosamine reductase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440574 [Multi-domain] Cd Length: 279 Bit Score: 45.78 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 152 RIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSL---EGHFlptrigDTITVDLSKFMNnvVKFDKLDLdITVQAGLPW 228
Cdd:COG0812 16 DLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLlvrDDGF------DGLVIRLGRLKG--IEVDDGVL-VTAGAGENW 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320027 229 EDLNDYLSDHGLmfgcdPG-------PGaQIGGCIANscsgtNAYRYGT-MKENIINMTIVLPDGTIV 288
Cdd:COG0812 87 HDLVRFALEAGL-----SGleflagiPG-TVGGAPVM-----NAGAYGGeIKDVLESVEVLDRTGEVR 143
|
|
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
152-287 |
4.79e-04 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 42.41 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 152 RIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSL-------EGhflptrigdtITVDLSKFMNNVvkfDKLDLDITVQA 224
Cdd:PRK13905 32 DYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLlvrdggiRG----------VVIRLGKGLNEI---EVEGNRITAGA 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320027 225 GLPWEDLNDYLSDH---GLMFGCdpG-PGAqIGGCIAnscsgTNAYRYGT-MKENIINMTIVLPDGTI 287
Cdd:PRK13905 99 GAPLIKLARFAAEAglsGLEFAA--GiPGT-VGGAVF-----MNAGAYGGeTADVLESVEVLDRDGEI 158
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
154-321 |
2.35e-03 |
|
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.
Pssm-ID: 273750 [Multi-domain] Cd Length: 557 Bit Score: 40.61 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 154 ILFPHTTEEVSKILKICHDNNMPVVPFSGGTslegHFLP----TRIGDTITVDLSKFMNNVVKFDKLDLDITVQAGLPWE 229
Cdd:TIGR01677 35 VAYPKTEAELVSVVAAATAAGRKMKVVTRYS----HSIPklacPDGSDGALLISTKRLNHVVAVDATAMTVTVESGMSLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320027 230 DLNDYLSDHGLMFGCDP-GPGAQIGGCIANSCSGTNAY-RYGTMKENIINMTIVLPDGTIVKTKK--RPRKSSAGYNLNG 305
Cdd:TIGR01677 111 ELIVEAEKAGLALPYAPyWWGLTVGGMMGTGAHGSSLWgKGSAVHDYVVGIRLVVPASAAEGFAKvrILSEGDTPNEFNA 190
|
170
....*....|....*.
gi 6320027 306 LFVgSEGTLGIVTEAT 321
Cdd:TIGR01677 191 AKV-SLGVLGVISQVT 205
|
|
| |
