|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
9-567 |
0e+00 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 1144.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 9 RSKTILSFLRPCRQLHSTPKSTGDVTVLSPVKGRRRLPTCWSSSLFPLAIAASATSFAYLNLSNPSISESSsALDSRdit 88
Cdd:PLN02805 1 RLRSLLRTSRPNRALPSFPKSTLDVTVTTPVKGRRRLPTSWSSSLLPLAIAASAGSLAYLNQSNPSLCDSS-DLDSR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 89 VGGKDSTEAVVKGEYKQVPKELISQLKTILEDNLTTDYDERYFHGKPQNSFHKAVNIPDVVVFPRSEEEVSKILKSCNEY 168
Cdd:PLN02805 77 VGGKGSTEFVVKGEHKLVPQELIDELKAILQDNMTLDYDERYFHGKPQNSFHKAVNIPDVVVFPRSEEEVSKIVKSCNKY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 169 KVPIVPYGGATSIEGHTLAPKGGVCIDMSLMKRVKALHVEDMDVIVEPGIGWLELNEYLEEYGLFFPLDPGPGASIGGMC 248
Cdd:PLN02805 157 KVPIVPYGGATSIEGHTLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPGPGATIGGMC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 249 ATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLIIGSEGTLGVITEITLRLQKIPQHSVVAVC 328
Cdd:PLN02805 237 ATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 329 NFPTVKDAADVAIATMMSGIQVSRVELLDEVQIRAINMANGKNLTEAPTLMFEFIGTEAYTREQTQIVQQIASKHNGSDF 408
Cdd:PLN02805 317 NFPTIKDAADVAIATMLSGIQVSRVELLDEVQIRAINMANGKNLPEAPTLMFEFIGTEAYAREQTLIVQKIASKHNGSDF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 409 MFAEEPEAKKELWKIRKEALWACYAMAPGHEAMITDVCVPLSHLAELISRSKKELDASSLLCTVIAHAGDGNFHTCIMFD 488
Cdd:PLN02805 397 VFAEEPEAKKELWKIRKEALWACFAMEPKYEAMITDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFD 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18415252 489 PSSEEQRREAERLNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKTLDPNDIMNPGKLIPPHVCF 567
Cdd:PLN02805 477 PSQEDQRREAERLNHFMVHTALSMEGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIPPHVCF 555
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
106-563 |
8.92e-174 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 499.81 E-value: 8.92e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 106 VPKELISQLKTILEDNLTTDYDERYFHGKPQNSFHKAVniPDVVVFPRSEEEVSKILKSCNEYKVPIVPYGGATSIEGHT 185
Cdd:COG0277 2 LTAALLAALRAILAGRVLTDPADRAAYARDGNSLYRGR--PDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 186 LAPKGGVCIDMSLMKRVKALHVEDMDVIVEPGIGWLELNEYLEEYGLFFPLDPG--PGASIGGMCATRCSGSLAVRYGTM 263
Cdd:COG0277 80 VPLDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSsqGTATIGGNIATNAGGPRSLKYGLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 264 RDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLIIGSEGTLGVITEITLRLQKIPQHSVVAVCNFPTVKDAADVAIAT 343
Cdd:COG0277 160 RDNVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 344 MMSGIQVSRVELLDEVQIRAINMANGKNLTE--APTLMFEFIGTEAYT-REQTQIVQQIASKHNGSDFMFAEEPEAKKEL 420
Cdd:COG0277 240 LAAGIAPAALELMDRAALALVEAAPPLGLPEdgGALLLVEFDGDDAEEvEAQLARLRAILEAGGATDVRVAADGAERERL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 421 WKIRKEALWACYAMAPGHeAMITDVCVPLSHLAELISRSKKELDASSLLCTVIAHAGDGNFHTCIMFDPSSEEQRREAER 500
Cdd:COG0277 320 WKARKAALPALGRLDGGA-KLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18415252 501 LNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKTLDPNDIMNPGKLIPP 563
Cdd:COG0277 399 AAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPP 461
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
149-559 |
4.99e-97 |
|
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity. [Energy metabolism, Other]
Pssm-ID: 273050 [Multi-domain] Cd Length: 413 Bit Score: 301.31 E-value: 4.99e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 149 VVFPRSEEEVSKILKSCNEYKVPIVPYGGATSIEGHTLAPKGGVCIDMSLMKRVKALHVEDMDVIVEPGIGWLELNEYLE 228
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQAVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 229 EYGLFFPLDPGP--GASIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLIIGSEGTL 306
Cdd:TIGR00387 81 EHNLFYPPDPSSqiSSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKTAKDVAGYDLTGLFVGSEGTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 307 GVITEITLRLQKIPQHSVVAVCNFPTVKDAADVAIATMMSGIQVSRVELLDEVQIRAINMANGKNL--TEAPTLMFEFIG 384
Cdd:TIGR00387 161 GIVTEATLKLLPKPENIVVALAFFDSIEKAMQAVYDIIAAGIIPAGMEFLDNLSIKAVEDISGIGLpkDAGAILLVEIDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 385 TEAYTREQTQIVQQIASKHNGSDFMFAEEPEAKKELWKIRKEALWACYAMAPghEAMITDVCVPLSHLAELISRSKKELD 464
Cdd:TIGR00387 241 VHEAVERDEEKIEQICRKNGAVDVQIAQDEEERALLWAGRRNAFKAASKLSP--LYLIEDGTVPRSKLPEALRGIADIAS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 465 ASSLLCTVIAHAGDGNFHTCIMFDPSSEEQRREAERLNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEALQTMKR 544
Cdd:TIGR00387 319 KYDFTIANFGHAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRA 398
|
410
....*....|....*
gi 18415252 545 IKKTLDPNDIMNPGK 559
Cdd:TIGR00387 399 IKKAFDPDNILNPGK 413
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
319-560 |
1.79e-83 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 260.32 E-value: 1.79e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 319 IPQHSVVAVCNFPTVKDAADVAIATMMSGIQVSRVELLDEVQIRAIN----MANGKNLTEAPTLMFEFIGT-EAYTREQT 393
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEatlgFPKGLPRDAAALLLVEFEGDdEETAEEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 394 QIVQQIASKHNGSDFMFAEEPEAKKELWKIRKEALWA-CYAMAPGHEAMITDVCVPLSHLAELISRSKKELDASSLLCTV 472
Cdd:pfam02913 81 EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPLrDALGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKYGLVVCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 473 IAHAGDGNFHTCIMFDPSSEEQRREAERLNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKTLDPN 552
Cdd:pfam02913 161 FGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPK 240
|
....*...
gi 18415252 553 DIMNPGKL 560
Cdd:pfam02913 241 GILNPGKV 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
9-567 |
0e+00 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 1144.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 9 RSKTILSFLRPCRQLHSTPKSTGDVTVLSPVKGRRRLPTCWSSSLFPLAIAASATSFAYLNLSNPSISESSsALDSRdit 88
Cdd:PLN02805 1 RLRSLLRTSRPNRALPSFPKSTLDVTVTTPVKGRRRLPTSWSSSLLPLAIAASAGSLAYLNQSNPSLCDSS-DLDSR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 89 VGGKDSTEAVVKGEYKQVPKELISQLKTILEDNLTTDYDERYFHGKPQNSFHKAVNIPDVVVFPRSEEEVSKILKSCNEY 168
Cdd:PLN02805 77 VGGKGSTEFVVKGEHKLVPQELIDELKAILQDNMTLDYDERYFHGKPQNSFHKAVNIPDVVVFPRSEEEVSKIVKSCNKY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 169 KVPIVPYGGATSIEGHTLAPKGGVCIDMSLMKRVKALHVEDMDVIVEPGIGWLELNEYLEEYGLFFPLDPGPGASIGGMC 248
Cdd:PLN02805 157 KVPIVPYGGATSIEGHTLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPGPGATIGGMC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 249 ATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLIIGSEGTLGVITEITLRLQKIPQHSVVAVC 328
Cdd:PLN02805 237 ATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 329 NFPTVKDAADVAIATMMSGIQVSRVELLDEVQIRAINMANGKNLTEAPTLMFEFIGTEAYTREQTQIVQQIASKHNGSDF 408
Cdd:PLN02805 317 NFPTIKDAADVAIATMLSGIQVSRVELLDEVQIRAINMANGKNLPEAPTLMFEFIGTEAYAREQTLIVQKIASKHNGSDF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 409 MFAEEPEAKKELWKIRKEALWACYAMAPGHEAMITDVCVPLSHLAELISRSKKELDASSLLCTVIAHAGDGNFHTCIMFD 488
Cdd:PLN02805 397 VFAEEPEAKKELWKIRKEALWACFAMEPKYEAMITDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFD 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18415252 489 PSSEEQRREAERLNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKTLDPNDIMNPGKLIPPHVCF 567
Cdd:PLN02805 477 PSQEDQRREAERLNHFMVHTALSMEGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIPPHVCF 555
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
106-563 |
8.92e-174 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 499.81 E-value: 8.92e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 106 VPKELISQLKTILEDNLTTDYDERYFHGKPQNSFHKAVniPDVVVFPRSEEEVSKILKSCNEYKVPIVPYGGATSIEGHT 185
Cdd:COG0277 2 LTAALLAALRAILAGRVLTDPADRAAYARDGNSLYRGR--PDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 186 LAPKGGVCIDMSLMKRVKALHVEDMDVIVEPGIGWLELNEYLEEYGLFFPLDPG--PGASIGGMCATRCSGSLAVRYGTM 263
Cdd:COG0277 80 VPLDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSsqGTATIGGNIATNAGGPRSLKYGLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 264 RDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLIIGSEGTLGVITEITLRLQKIPQHSVVAVCNFPTVKDAADVAIAT 343
Cdd:COG0277 160 RDNVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 344 MMSGIQVSRVELLDEVQIRAINMANGKNLTE--APTLMFEFIGTEAYT-REQTQIVQQIASKHNGSDFMFAEEPEAKKEL 420
Cdd:COG0277 240 LAAGIAPAALELMDRAALALVEAAPPLGLPEdgGALLLVEFDGDDAEEvEAQLARLRAILEAGGATDVRVAADGAERERL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 421 WKIRKEALWACYAMAPGHeAMITDVCVPLSHLAELISRSKKELDASSLLCTVIAHAGDGNFHTCIMFDPSSEEQRREAER 500
Cdd:COG0277 320 WKARKAALPALGRLDGGA-KLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18415252 501 LNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKTLDPNDIMNPGKLIPP 563
Cdd:COG0277 399 AAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPP 461
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
149-559 |
4.99e-97 |
|
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity. [Energy metabolism, Other]
Pssm-ID: 273050 [Multi-domain] Cd Length: 413 Bit Score: 301.31 E-value: 4.99e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 149 VVFPRSEEEVSKILKSCNEYKVPIVPYGGATSIEGHTLAPKGGVCIDMSLMKRVKALHVEDMDVIVEPGIGWLELNEYLE 228
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQAVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 229 EYGLFFPLDPGP--GASIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLIIGSEGTL 306
Cdd:TIGR00387 81 EHNLFYPPDPSSqiSSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKTAKDVAGYDLTGLFVGSEGTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 307 GVITEITLRLQKIPQHSVVAVCNFPTVKDAADVAIATMMSGIQVSRVELLDEVQIRAINMANGKNL--TEAPTLMFEFIG 384
Cdd:TIGR00387 161 GIVTEATLKLLPKPENIVVALAFFDSIEKAMQAVYDIIAAGIIPAGMEFLDNLSIKAVEDISGIGLpkDAGAILLVEIDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 385 TEAYTREQTQIVQQIASKHNGSDFMFAEEPEAKKELWKIRKEALWACYAMAPghEAMITDVCVPLSHLAELISRSKKELD 464
Cdd:TIGR00387 241 VHEAVERDEEKIEQICRKNGAVDVQIAQDEEERALLWAGRRNAFKAASKLSP--LYLIEDGTVPRSKLPEALRGIADIAS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 465 ASSLLCTVIAHAGDGNFHTCIMFDPSSEEQRREAERLNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEALQTMKR 544
Cdd:TIGR00387 319 KYDFTIANFGHAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRA 398
|
410
....*....|....*
gi 18415252 545 IKKTLDPNDIMNPGK 559
Cdd:TIGR00387 399 IKKAFDPDNILNPGK 413
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
319-560 |
1.79e-83 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 260.32 E-value: 1.79e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 319 IPQHSVVAVCNFPTVKDAADVAIATMMSGIQVSRVELLDEVQIRAIN----MANGKNLTEAPTLMFEFIGT-EAYTREQT 393
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEatlgFPKGLPRDAAALLLVEFEGDdEETAEEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 394 QIVQQIASKHNGSDFMFAEEPEAKKELWKIRKEALWA-CYAMAPGHEAMITDVCVPLSHLAELISRSKKELDASSLLCTV 472
Cdd:pfam02913 81 EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPLrDALGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKYGLVVCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 473 IAHAGDGNFHTCIMFDPSSEEQRREAERLNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKTLDPN 552
Cdd:pfam02913 161 FGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPK 240
|
....*...
gi 18415252 553 DIMNPGKL 560
Cdd:pfam02913 241 GILNPGKV 248
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
145-566 |
4.19e-51 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 183.05 E-value: 4.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 145 IPDVVVFPRSEEEVSKILKSCNEYKVPIVPYGGATSIEGHTLAPKGGVCIDMSLMKRVKALHVEDMDVIVEPGIGWLELN 224
Cdd:PRK11230 55 RPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKGVLLVMARFNRILDINPVGRRARVQPGVRNLAIS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 225 EYLEEYGLFFPLDPGP--GASIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAaGYDLTRLIIGS 302
Cdd:PRK11230 135 QAAAPHGLYYAPDPSSqiACSIGGNVAENAGGVHCLKYGLTVHNLLKVEILTLDGEALTLGSDALDSP-GFDLLALFTGS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 303 EGTLGVITEITLRLQKIPQHSVVAVCNFPTVKDAADVAIATMMSGIQVSRVELLDEVQIRAIN--MANGKNLTEAPTLMF 380
Cdd:PRK11230 214 EGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPGGLEMMDNLSIRAAEdfIHAGYPVDAEAILLC 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 381 EFIGTEAYTREQTQIVQQIASKHNGSDFMFAEEPEAKKELWKIRKEALWACYAMAPGHEAMitDVCVPLSHLAELIsRSK 460
Cdd:PRK11230 294 ELDGVESDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGRKNAFPAVGRISPDYYCM--DGTIPRRELPGVL-EGI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 461 KELDAS-SLLCTVIAHAGDGNFHTCIMFDPSSEEQRREAERLNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEAL 539
Cdd:PRK11230 371 ARLSQQyGLRVANVFHAGDGNMHPLILFDANEPGELERAEALGGKILELCVEVGGSITGEHGVGREKINQMCAQFNSDEI 450
|
410 420
....*....|....*....|....*...
gi 18415252 540 QTMKRIKKTLDPNDIMNPGKLIPP-HVC 566
Cdd:PRK11230 451 TLFHAVKAAFDPDGLLNPGKNIPTlHRC 478
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
146-282 |
1.27e-45 |
|
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: 157.36 E-value: 1.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 146 PDVVVFPRSEEEVSKILKSCNEYKVPIVPYGGATSIEGHTLaPKGGVCIDMSLMKRVKALHVEDMDVIVEPGIGWLELNE 225
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAV-QTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 18415252 226 YLEEYGLFFPLDPGPG--ASIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKT 282
Cdd:pfam01565 80 ALAAKGLLLGLDPGSGipGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRL 138
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
145-338 |
6.35e-13 |
|
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: 70.70 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 145 IPDVVVFPRSEEEVSKILKSCNEYKVPIVPYGGatsieGHTlaPKGGVCID-----MSLMKRVKALHVEDMDVIVEPGIG 219
Cdd:TIGR01678 14 SPEVYYQPTSVEEVREVLALAREQKKKVKVVGG-----GHS--PSDIACTDgflihLDKMNKVLQFDKEKKQITVEAGIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 220 WLELNEYLEEYGLFFP-LDPGPGASIGGMCATrCSGSLAVRYGTMRDNVISLKVVLPNGDvVKTASRARKSaagyDLTRL 298
Cdd:TIGR01678 87 LYQLHEQLDEHGYSMSnLGSISEVSVAGIIST-GTHGSSIKHGILATQVVALTIMTADGE-VLECSEERNA----DVFQA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18415252 299 IIGSEGTLGVITEITLRLqkIPQHSVVAVCNFPTVKDAAD 338
Cdd:TIGR01678 161 ARVSLGCLGIIVTVTIQV--VPQFHLQETSFVSTLKELLD 198
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
152-325 |
2.84e-12 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 69.11 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 152 PRSEEEVSKILKSCNEYKVPIVPYGGATSIEGHTLAPKGGVciDMSLMKRVKALHVEDMDVIVEPGIGWLELNEYLEEYG 231
Cdd:PLN02465 103 PESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAFSREGMV--NLALMDKVLEVDKEKKRVTVQAGARVQQVVEALRPHG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 232 LFFPldpgPGASI-----GGMCATRCSGSLAvRYGTMRDNVISLKVVLP-NGDVVKTASrarKSAAGYDLTRLIIGSegt 305
Cdd:PLN02465 181 LTLQ----NYASIreqqiGGFIQVGAHGTGA-RIPPIDEQVVSMKLVTPaKGTIELSKE---DDPELFRLARCGLGG--- 249
|
170 180
....*....|....*....|
gi 18415252 306 LGVITEITLRLqkIPQHSVV 325
Cdd:PLN02465 250 LGVVAEVTLQC--VPAHRLV 267
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
222-315 |
1.08e-11 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 66.40 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 222 ELNEYLEEYGLFFPLDP---GPGASIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRL 298
Cdd:PRK11282 69 ELEAALAEAGQMLPFEPphfGGGATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGEHLRFGGQVMKNVAGYDVSRL 148
|
90
....*....|....*..
gi 18415252 299 IIGSEGTLGVITEITLR 315
Cdd:PRK11282 149 MAGSLGTLGVLLEVSLK 165
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
149-324 |
8.47e-11 |
|
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: 64.50 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 149 VVFPRSEEEVSKILKSCNEYKVPIvpygGATSIEGHTLaPK--------GGVCIDMSLMKRVKALHVEDMDVIVEPGIGW 220
Cdd:TIGR01677 35 VAYPKTEAELVSVVAAATAAGRKM----KVVTRYSHSI-PKlacpdgsdGALLISTKRLNHVVAVDATAMTVTVESGMSL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 221 LELNEYLEEYGLFFPLDP-GPGASIGGMCATRCSGS-LAVRYGTMRDNVISLKVVLPnGDVVKTASRARKSAAGYDLTRL 298
Cdd:TIGR01677 110 RELIVEAEKAGLALPYAPyWWGLTVGGMMGTGAHGSsLWGKGSAVHDYVVGIRLVVP-ASAAEGFAKVRILSEGDTPNEF 188
|
170 180
....*....|....*....|....*...
gi 18415252 299 --IIGSEGTLGVITEITLRLQKIPQHSV 324
Cdd:TIGR01677 189 naAKVSLGVLGVISQVTLALQPMFKRSV 216
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
152-326 |
2.47e-08 |
|
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: 56.61 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 152 PRSEEEVSKILKSCNEYKVPIVPYGGATSIEGHTLAPKGGVciDMSLMKRVKALHVEDMDVIVEPGIGWLELNEYLEEYG 231
Cdd:TIGR01676 68 PEAIEELEGIVKQANEKKARIRPVGSGLSPNGIGLSRAGMV--NLALMDKVLEVDEEKKRVRVQAGIRVQQLVDAIKEYG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415252 232 L----FFPLDPgpgASIGGMCATRCSGSLAvRYGTMRDNVISLKVVLPNGDVVKTASraRKSAAGYDLTRLIIGSegtLG 307
Cdd:TIGR01676 146 ItlqnFASIRE---QQIGGIIQVGAHGTGA-KLPPIDEQVIAMKLVTPAKGTIEISK--DKDPELFFLARCGLGG---LG 216
|
170 180
....*....|....*....|..
gi 18415252 308 VITEITLRL---QKIPQHSVVA 326
Cdd:TIGR01676 217 VVAEVTLQCverQELVEHTFIS 238
|
|
| |
