|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
8-478 |
4.47e-161 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 463.98 E-value: 4.47e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 8 ASQDFLDACAAAIGtQNVLTDAHDTAPYLADWRRRYQGAAFAVLCPANAQEVAAVVKFAHAHRVALVPQGGNTGLAGGAT 87
Cdd:COG0277 2 LTAALLAALRAILA-GRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 88 PDASGkhAVLSLRRLNRVREIDAHNNTITVEAGVILAEVQARAKDAGRLFPLSLAAEGSCTIGGNLSTNAGGTGVLRYGN 167
Cdd:COG0277 81 PLDGG--VVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 168 TRELCLGLEVVTPQGEIWDGLRGLRKDNTGYDLRDLFIGAEGTLGVITAAVMKLHPLPAARVTALAALGSAHAALDFLAL 247
Cdd:COG0277 159 TRDNVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 248 AQRyAGPLLTGFELMSDFCMRLVgRHFPQLRYPfaEHHAQVVLLELsDNESEAHARALFERLMEdALEQGLVEDAVVAEN 327
Cdd:COG0277 239 LLA-AGIAPAALELMDRAALALV-EAAPPLGLP--EDGGALLLVEF-DGDDAEEVEAQLARLRA-ILEAGGATDVRVAAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 328 LAQSQAFWNIREHIPLAQAQE--GLNIKHDIGVPISRIGHFIEETDAEIARAvpGARMVTFGHLGDGNLHYNVQAPEGGD 405
Cdd:COG0277 313 GAERERLWKARKAALPALGRLdgGAKLLEDVAVPPSRLPELLRELGALAAKY--GLRATAFGHAGDGNLHVRILFDPADP 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2102983508 406 pkRFLAENEKtLNRIVYDSVNRHRGTISAEHGLGQLKVEENIHYKSEVELALMRAIKTALDPLNLMNPGKVLG 478
Cdd:COG0277 391 --EEVERARA-AAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
50-475 |
1.15e-79 |
|
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: 253.54 E-value: 1.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 50 VLCPANAQEVAAVVKFAHAHRVALVPQGGNTGLAGGATPDASGkhAVLSLRRLNRVREIDAHNNTITVEAGVILAEVQAR 129
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGG--LVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 130 AKDAGRLFPLSLAAEGSCTIGGNLSTNAGGTGVLRYGNTRELCLGLEVVTPQGEIWDGLRGLRKDNTGYDLRDLFIGAEG 209
Cdd:TIGR00387 79 VEEHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKTAKDVAGYDLTGLFVGSEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 210 TLGVITAAVMKLHPLPAARVTALAALGSAHAAL----DFLAlaqryAGPLLTGFELMSDFCMRlVGRHFPQLRYPFAEhh 285
Cdd:TIGR00387 159 TLGIVTEATLKLLPKPENIVVALAFFDSIEKAMqavyDIIA-----AGIIPAGMEFLDNLSIK-AVEDISGIGLPKDA-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 286 AQVVLLELSDNESEAHaraLFERLMEDALEQGLVEDAVVAENLAQSQAFWNIREH-IPLAQAQEGLNIKHDIGVPISRIG 364
Cdd:TIGR00387 231 GAILLVEIDGVHEAVE---RDEEKIEQICRKNGAVDVQIAQDEEERALLWAGRRNaFKAASKLSPLYLIEDGTVPRSKLP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 365 HFIEETdAEIARAVPGARmVTFGHLGDGNLHYNVQAPEggDPKRFLAENEKTLNRIVYDSVnRHRGTISAEHGLGQLKVE 444
Cdd:TIGR00387 308 EALRGI-ADIASKYDFTI-ANFGHAGDGNLHPTILTDP--EDKGEMERVEEAGGEIFELAI-ELGGTISGEHGIGVVKAE 382
|
410 420 430
....*....|....*....|....*....|.
gi 2102983508 445 ENIHYKSEVELALMRAIKTALDPLNLMNPGK 475
Cdd:TIGR00387 383 FMPYKFNEKELETMRAIKKAFDPDNILNPGK 413
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
50-477 |
2.12e-46 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 169.42 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 50 VLCPANAQEVAAVVKFAHAHRVALVPQGGNTGLAGGATPDASGKHAVLSLrrLNRVREIDAHNNTITVEAGVILAEVQAR 129
Cdd:PLN02805 137 VVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGGVCIDMSL--MKSVKALHVEDMDVVVEPGIGWLELNEY 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 130 AKDAGRLFPLSLAAegSCTIGGNLSTNAGGTGVLRYGNTRELCLGLEVVTPQGEIWDGLRGLRKDNTGYDLRDLFIGAEG 209
Cdd:PLN02805 215 LEPYGLFFPLDPGP--GATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 210 TLGVITAAVMKLHPLPAARVTALAALGSAHAALDfLALAQRYAGPLLTGFELMSDFCMRLV----GRHFPQlrypfaehh 285
Cdd:PLN02805 293 TLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAAD-VAIATMLSGIQVSRVELLDEVQIRAInmanGKNLPE--------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 286 AQVVLLELSDNESEAHARALferLMEDALEQGLVEDAVVAENLAQSQAFWNIREH---IPLAQAQEGLNIKHDIGVPISR 362
Cdd:PLN02805 363 APTLMFEFIGTEAYAREQTL---IVQKIASKHNGSDFVFAEEPEAKKELWKIRKEalwACFAMEPKYEAMITDVCVPLSH 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 363 IGHFIEETDAEIaRAVPGARMVtFGHLGDGNLHYNVQAPEGGDPKRFLAENektLNRIVYDSVNRHRGTISAEHGLGQLK 442
Cdd:PLN02805 440 LAELISRSKKEL-DASPLVCTV-IAHAGDGNFHTIILFDPSQEDQRREAER---LNHFMVHTALSMEGTCTGEHGVGTGK 514
|
410 420 430
....*....|....*....|....*....|....*...
gi 2102983508 443 ---VEENIHYKSeveLALMRAIKTALDPLNLMNPGKVL 477
Cdd:PLN02805 515 mkyLEKELGIEA---LQTMKRIKKALDPNNIMNPGKLI 549
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
224-476 |
1.71e-45 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 159.02 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 224 LPAARVTALAALGSAHAALDFLALAQRyAGPLLTGFELMSDFCMRLVGRHFPQLRyPFAEHHAQVVLLEL-SDNESEAHA 302
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIAR-AGIIPAALELMDNDALDLVEATLGFPK-GLPRDAAALLLVEFeGDDEETAEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 303 RAlfeRLMEDALEQGLVEDAVVAENLAQSQAFWNIREHIP----LAQAQEGLNIKHDIGVPISRIGHFIEETDAEIARAv 378
Cdd:pfam02913 79 EL---EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALplrdALGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKY- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 379 pGARMVTFGHLGDGNLHYNVQAPEGgdpkrfLAENEKTLNRIVY---DSVNRHRGTISAEHGLGQLKVEENIHYKSEVEL 455
Cdd:pfam02913 155 -GLVVCLFGHAGDGNLHLYILFDFR------DPEQEERAEKLFDeimDLALELGGSISGEHGVGRDKKPYLEREFGEEGL 227
|
250 260
....*....|....*....|.
gi 2102983508 456 ALMRAIKTALDPLNLMNPGKV 476
Cdd:pfam02913 228 ALMRRIKAAFDPKGILNPGKV 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
8-478 |
4.47e-161 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 463.98 E-value: 4.47e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 8 ASQDFLDACAAAIGtQNVLTDAHDTAPYLADWRRRYQGAAFAVLCPANAQEVAAVVKFAHAHRVALVPQGGNTGLAGGAT 87
Cdd:COG0277 2 LTAALLAALRAILA-GRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 88 PDASGkhAVLSLRRLNRVREIDAHNNTITVEAGVILAEVQARAKDAGRLFPLSLAAEGSCTIGGNLSTNAGGTGVLRYGN 167
Cdd:COG0277 81 PLDGG--VVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 168 TRELCLGLEVVTPQGEIWDGLRGLRKDNTGYDLRDLFIGAEGTLGVITAAVMKLHPLPAARVTALAALGSAHAALDFLAL 247
Cdd:COG0277 159 TRDNVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 248 AQRyAGPLLTGFELMSDFCMRLVgRHFPQLRYPfaEHHAQVVLLELsDNESEAHARALFERLMEdALEQGLVEDAVVAEN 327
Cdd:COG0277 239 LLA-AGIAPAALELMDRAALALV-EAAPPLGLP--EDGGALLLVEF-DGDDAEEVEAQLARLRA-ILEAGGATDVRVAAD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 328 LAQSQAFWNIREHIPLAQAQE--GLNIKHDIGVPISRIGHFIEETDAEIARAvpGARMVTFGHLGDGNLHYNVQAPEGGD 405
Cdd:COG0277 313 GAERERLWKARKAALPALGRLdgGAKLLEDVAVPPSRLPELLRELGALAAKY--GLRATAFGHAGDGNLHVRILFDPADP 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2102983508 406 pkRFLAENEKtLNRIVYDSVNRHRGTISAEHGLGQLKVEENIHYKSEVELALMRAIKTALDPLNLMNPGKVLG 478
Cdd:COG0277 391 --EEVERARA-AAEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
50-475 |
1.15e-79 |
|
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: 253.54 E-value: 1.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 50 VLCPANAQEVAAVVKFAHAHRVALVPQGGNTGLAGGATPDASGkhAVLSLRRLNRVREIDAHNNTITVEAGVILAEVQAR 129
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGG--LVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 130 AKDAGRLFPLSLAAEGSCTIGGNLSTNAGGTGVLRYGNTRELCLGLEVVTPQGEIWDGLRGLRKDNTGYDLRDLFIGAEG 209
Cdd:TIGR00387 79 VEEHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKTAKDVAGYDLTGLFVGSEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 210 TLGVITAAVMKLHPLPAARVTALAALGSAHAAL----DFLAlaqryAGPLLTGFELMSDFCMRlVGRHFPQLRYPFAEhh 285
Cdd:TIGR00387 159 TLGIVTEATLKLLPKPENIVVALAFFDSIEKAMqavyDIIA-----AGIIPAGMEFLDNLSIK-AVEDISGIGLPKDA-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 286 AQVVLLELSDNESEAHaraLFERLMEDALEQGLVEDAVVAENLAQSQAFWNIREH-IPLAQAQEGLNIKHDIGVPISRIG 364
Cdd:TIGR00387 231 GAILLVEIDGVHEAVE---RDEEKIEQICRKNGAVDVQIAQDEEERALLWAGRRNaFKAASKLSPLYLIEDGTVPRSKLP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 365 HFIEETdAEIARAVPGARmVTFGHLGDGNLHYNVQAPEggDPKRFLAENEKTLNRIVYDSVnRHRGTISAEHGLGQLKVE 444
Cdd:TIGR00387 308 EALRGI-ADIASKYDFTI-ANFGHAGDGNLHPTILTDP--EDKGEMERVEEAGGEIFELAI-ELGGTISGEHGIGVVKAE 382
|
410 420 430
....*....|....*....|....*....|.
gi 2102983508 445 ENIHYKSEVELALMRAIKTALDPLNLMNPGK 475
Cdd:TIGR00387 383 FMPYKFNEKELETMRAIKKAFDPDNILNPGK 413
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
50-477 |
2.12e-46 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 169.42 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 50 VLCPANAQEVAAVVKFAHAHRVALVPQGGNTGLAGGATPDASGKHAVLSLrrLNRVREIDAHNNTITVEAGVILAEVQAR 129
Cdd:PLN02805 137 VVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGGVCIDMSL--MKSVKALHVEDMDVVVEPGIGWLELNEY 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 130 AKDAGRLFPLSLAAegSCTIGGNLSTNAGGTGVLRYGNTRELCLGLEVVTPQGEIWDGLRGLRKDNTGYDLRDLFIGAEG 209
Cdd:PLN02805 215 LEPYGLFFPLDPGP--GATIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 210 TLGVITAAVMKLHPLPAARVTALAALGSAHAALDfLALAQRYAGPLLTGFELMSDFCMRLV----GRHFPQlrypfaehh 285
Cdd:PLN02805 293 TLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAAD-VAIATMLSGIQVSRVELLDEVQIRAInmanGKNLPE--------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 286 AQVVLLELSDNESEAHARALferLMEDALEQGLVEDAVVAENLAQSQAFWNIREH---IPLAQAQEGLNIKHDIGVPISR 362
Cdd:PLN02805 363 APTLMFEFIGTEAYAREQTL---IVQKIASKHNGSDFVFAEEPEAKKELWKIRKEalwACFAMEPKYEAMITDVCVPLSH 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 363 IGHFIEETDAEIaRAVPGARMVtFGHLGDGNLHYNVQAPEGGDPKRFLAENektLNRIVYDSVNRHRGTISAEHGLGQLK 442
Cdd:PLN02805 440 LAELISRSKKEL-DASPLVCTV-IAHAGDGNFHTIILFDPSQEDQRREAER---LNHFMVHTALSMEGTCTGEHGVGTGK 514
|
410 420 430
....*....|....*....|....*....|....*...
gi 2102983508 443 ---VEENIHYKSeveLALMRAIKTALDPLNLMNPGKVL 477
Cdd:PLN02805 515 mkyLEKELGIEA---LQTMKRIKKALDPNNIMNPGKLI 549
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
224-476 |
1.71e-45 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 159.02 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 224 LPAARVTALAALGSAHAALDFLALAQRyAGPLLTGFELMSDFCMRLVGRHFPQLRyPFAEHHAQVVLLEL-SDNESEAHA 302
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIAR-AGIIPAALELMDNDALDLVEATLGFPK-GLPRDAAALLLVEFeGDDEETAEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 303 RAlfeRLMEDALEQGLVEDAVVAENLAQSQAFWNIREHIP----LAQAQEGLNIKHDIGVPISRIGHFIEETDAEIARAv 378
Cdd:pfam02913 79 EL---EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALplrdALGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKY- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 379 pGARMVTFGHLGDGNLHYNVQAPEGgdpkrfLAENEKTLNRIVY---DSVNRHRGTISAEHGLGQLKVEENIHYKSEVEL 455
Cdd:pfam02913 155 -GLVVCLFGHAGDGNLHLYILFDFR------DPEQEERAEKLFDeimDLALELGGSISGEHGVGRDKKPYLEREFGEEGL 227
|
250 260
....*....|....*....|.
gi 2102983508 456 ALMRAIKTALDPLNLMNPGKV 476
Cdd:pfam02913 228 ALMRRIKAAFDPKGILNPGKV 248
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
7-475 |
1.91e-43 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 159.94 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 7 HASQDFLDACAAAIGTQNVLTDAHDTAPYLADWRRRYQGAAFAVLCPANAQEVAAVVKFAHAHRVALVPQGGNTGLAGGA 86
Cdd:PRK11230 16 VDRTSLLMALREHLPGLEILHTDEELIPYECDGLSAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 87 TPDASGkhAVLSLRRLNRVREIDAHNNTITVEAGVI-LAEVQARAKdAGRLFPLSLAAEGSCTIGGNLSTNAGGTGVLRY 165
Cdd:PRK11230 96 LPLEKG--VLLVMARFNRILDINPVGRRARVQPGVRnLAISQAAAP-HGLYYAPDPSSQIACSIGGNVAENAGGVHCLKY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 166 GNTRELCLGLEVVTPQGE-IWDGLRGLrkDNTGYDLRDLFIGAEGTLGVITAAVMKLHPLPAARVTALAALGSAHAA--- 241
Cdd:PRK11230 173 GLTVHNLLKVEILTLDGEaLTLGSDAL--DSPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAgla 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 242 -LDFLAlaqryAGPLLTGFELMSDFCMRlVGRHFPQLRYPFaehHAQVVLL-ELSDNESEAHARAlfERLmEDALEQGLV 319
Cdd:PRK11230 251 vGDIIA-----AGIIPGGLEMMDNLSIR-AAEDFIHAGYPV---DAEAILLcELDGVESDVQEDC--ERV-NDILLKAGA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 320 EDAVVAENLAQSQAFWNIREH-IPLAQAQEGLNIKHDIGVP---ISRIGHFIEETDAEIaravpGARMVTFGHLGDGNLH 395
Cdd:PRK11230 319 TDVRLAQDEAERVRFWAGRKNaFPAVGRISPDYYCMDGTIPrreLPGVLEGIARLSQQY-----GLRVANVFHAGDGNMH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 396 ----YNVQAPegGDPKRFLAENEKTLNRIVydSVNrhrGTISAEHGLGQLKVEENIHYKSEVELALMRAIKTALDPLNLM 471
Cdd:PRK11230 394 plilFDANEP--GELERAEALGGKILELCV--EVG---GSITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPDGLL 466
|
....
gi 2102983508 472 NPGK 475
Cdd:PRK11230 467 NPGK 470
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
49-184 |
4.12e-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: 146.19 E-value: 4.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 49 AVLCPANAQEVAAVVKFAHAHRVALVPQGGNTGLAGGATPDASGkhaVLSLRRLNRVREIDAHNNTITVEAGVILAEVQA 128
Cdd:pfam01565 3 AVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGI---VLDLSRLNGILEIDPEDGTATVEAGVTLGDLVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2102983508 129 RAKDAGRLFPLSLAAEGSCTIGGNLSTNAGGTGVLRYGNTRELCLGLEVVTPQGEI 184
Cdd:pfam01565 80 ALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEV 135
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
21-224 |
2.64e-14 |
|
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: 75.28 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 21 GTQNVLTDAHDTAPYLADWRrryqgaAFAVLCPANAQEVAAVVKFAHAHRVAL-VPQGGNTGLAGGATPDASGKHAVLSL 99
Cdd:TIGR01677 12 GANCTVSNAYGAFPDRSTCR------AANVAYPKTEAELVSVVAAATAAGRKMkVVTRYSHSIPKLACPDGSDGALLIST 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 100 RRLNRVREIDAHNNTITVEAGVILAEVQARAKDAGRLFPLSLAAEGsCTIGGNLSTNAGGTGVL-RYGNTRELCLGLEVV 178
Cdd:TIGR01677 86 KRLNHVVAVDATAMTVTVESGMSLRELIVEAEKAGLALPYAPYWWG-LTVGGMMGTGAHGSSLWgKGSAVHDYVVGIRLV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2102983508 179 TP--QGEIWDGLRGLRKDNTGYDLRDLFIgAEGTLGVITAAVMKLHPL 224
Cdd:TIGR01677 165 VPasAAEGFAKVRILSEGDTPNEFNAAKV-SLGVLGVISQVTLALQPM 211
|
|
| PRK11183 |
PRK11183 |
D-lactate dehydrogenase; Provisional |
9-164 |
3.18e-11 |
|
D-lactate dehydrogenase; Provisional
Pssm-ID: 236872 [Multi-domain] Cd Length: 564 Bit Score: 65.25 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 9 SQDFLDACAAAIGTQNVLTDAHDTAPYLADWRRRyQGAAFAVLCPANAQEVAAVVKFAHAHRVALVPQGGNTGLAGGATP 88
Cdd:PRK11183 2 NKALINELTRIVGSSHVLTDPAKTERYRKGFRSG-QGDALAVVFPGTLLELWRVLQACVAADKIIIMQAANTGLTGGSTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 89 DASGKH---AVLSLRRLNRVREIDAHNNTITVeAGVILAEVQARAKDAGRLfPLSLAaeGSCTIG----GNLSTNAGGTG 161
Cdd:PRK11183 81 NGNDYDrdiVIISTLRLDKIQLLNNGKQVLAL-PGTTLYQLEKALKPLGRE-PHSVI--GSSCIGasviGGICNNSGGAL 156
|
...
gi 2102983508 162 VLR 164
Cdd:PRK11183 157 VQR 159
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
53-224 |
8.18e-09 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 57.94 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 53 PANAQEVAAVVKFAHAHRVALVPQGgnTGLA-GGATPDASGkhaVLSLRRLNRVREIDAHNNTITVEAGVILAEVQarak 131
Cdd:PLN02465 103 PESLEELEDIVKEAHEKGRRIRPVG--SGLSpNGLAFSREG---MVNLALMDKVLEVDKEKKRVTVQAGARVQQVV---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 132 DAGRLFPLSLAAEGSC---TIGGNLSTNAGGTGVlRYGNTRELCLGLEVVTP-QGEIwdglrGLRKDNTGydlrDLFIGA 207
Cdd:PLN02465 174 EALRPHGLTLQNYASIreqQIGGFIQVGAHGTGA-RIPPIDEQVVSMKLVTPaKGTI-----ELSKEDDP----ELFRLA 243
|
170 180
....*....|....*....|...
gi 2102983508 208 E---GTLGVITAAVMKL---HPL 224
Cdd:PLN02465 244 RcglGGLGVVAEVTLQCvpaHRL 266
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
57-246 |
2.13e-08 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 56.00 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 57 QEVAAVVKFAHAHRVALVPQGGNTGLAGGATPDASgkhaVLSLRRLNRVREIDAHNNTITVEAGVILAEVQARAKDAGRL 136
Cdd:PRK11282 5 AALLERVRQAAADGTPLRIRGGGSKDFYGRALAGE----VLDTRAHRGIVSYDPTELVITARAGTPLAELEAALAEAGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 137 fplsLAAE-----GSCTIGGNLStnAGGTGVLR--YGNTRELCLGLEVVTPQGEIwdglrgLR------KDNTGYDLRDL 203
Cdd:PRK11282 81 ----LPFEpphfgGGATLGGMVA--AGLSGPRRpwAGAVRDFVLGTRLINGRGEH------LRfggqvmKNVAGYDVSRL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2102983508 204 FIGAEGTLGVITAAVMKLHPLPAARVTaLAALGSAHAALDFLA 246
Cdd:PRK11282 149 MAGSLGTLGVLLEVSLKVLPRPRAELT-LRLEMDAAEALRKLN 190
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
38-223 |
1.42e-07 |
|
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: 53.75 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 38 DWRRRYQGAAFAVLCPANAQEVAAVVKFAHAHRVALVPQGGntglagGATPD--ASGKHAVLSLRRLNRVREIDAHNNTI 115
Cdd:TIGR01678 6 NWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGG------GHSPSdiACTDGFLIHLDKMNKVLQFDKEKKQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 116 TVEAGVILAEVQARAKDAGRLFPlSLAAEGSCTIGGNLSTNAGGTGvLRYGNTRELCLGLEVVTPQGEIWDGLRGLRKdn 195
Cdd:TIGR01678 80 TVEAGIRLYQLHEQLDEHGYSMS-NLGSISEVSVAGIISTGTHGSS-IKHGILATQVVALTIMTADGEVLECSEERNA-- 155
|
170 180 190
....*....|....*....|....*....|.
gi 2102983508 196 tgydlrDLFIGAE---GTLGVITAAVMKLHP 223
Cdd:TIGR01678 156 ------DVFQAARvslGCLGIIVTVTIQVVP 180
|
|
| PLN02441 |
PLN02441 |
cytokinin dehydrogenase |
38-225 |
7.58e-05 |
|
cytokinin dehydrogenase
Pssm-ID: 215242 [Multi-domain] Cd Length: 525 Bit Score: 45.29 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 38 DWRRRYQGAAFAVLCPANAQEVAAVVKFAHAH----RVAlvPQGGNTGLAGGATpdASGKhAVLSLRRLNRVREIDAHnn 113
Cdd:PLN02441 56 DFGNLVHSLPAAVLYPSSVEDIASLVRAAYGSssplTVA--ARGHGHSLNGQAQ--APGG-VVVDMRSLRGGVRGPPV-- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 114 tITVEAGVILAEVQA--------RAKDAGRLFPLS------LaaegscTIGGNLStNAGGTG-VLRYG----NTRELclg 174
Cdd:PLN02441 129 -IVVSGDGPYVDVSGgelwidvlKATLKHGLAPRSwtdylyL------TVGGTLS-NAGISGqAFRHGpqisNVLEL--- 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2102983508 175 lEVVTPQGEIwdgLRGLRKDNTgydlrDLFIGAEGTL---GVITAAVMKLHPLP 225
Cdd:PLN02441 198 -DVVTGKGEV---VTCSPTQNS-----DLFFAVLGGLgqfGIITRARIALEPAP 242
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
36-180 |
8.37e-04 |
|
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: 41.97 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 36 LADWRRRYQGAAFAVLCPANAQEVAAVVKFAHAHRVALVPQGGntglagGATPDASG--KHAVLSLRRLNRVREIDAHNN 113
Cdd:TIGR01676 51 VSNWSGTHEVLTRTFHQPEAIEELEGIVKQANEKKARIRPVGS------GLSPNGIGlsRAGMVNLALMDKVLEVDEEKK 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2102983508 114 TITVEAGVILAEVQARAKDAGrLFPLSLAAEGSCTIGGNLSTNAGGTGVlRYGNTRELCLGLEVVTP 180
Cdd:TIGR01676 125 RVRVQAGIRVQQLVDAIKEYG-ITLQNFASIREQQIGGIIQVGAHGTGA-KLPPIDEQVIAMKLVTP 189
|
|
| murB |
PRK13906 |
UDP-N-acetylmuramate dehydrogenase; |
45-161 |
9.94e-03 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 184386 [Multi-domain] Cd Length: 307 Bit Score: 37.88 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102983508 45 GAAFAVLCPANAQEVAAVVKFAHAHR--VALVPQGGNTGLAGGATpdasgKHAVLSLRRLNRvreIDAHNNTITVEAGVI 122
Cdd:PRK13906 35 GNADFYITPTKNEEVQAVVKYAYQNEipVTYLGNGSNIIIREGGI-----RGIVISLLSLDH---IEVSDDAIIAGSGAA 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 2102983508 123 LAEVQARAKDAGrLFPLSLAAEGSCTIGGNLSTNAGGTG 161
Cdd:PRK13906 107 IIDVSRVARDYA-LTGLEFACGIPGSIGGAVYMNAGAYG 144
|
|
| |
