|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
18-478 |
1.61e-171 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 491.98 E-value: 1.61e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 18 RREIVADLADLLPEGGLISDERGLKPFETDAFIAYRRMPLAVVLPETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGGAIP 97
Cdd:PRK11230 18 RTSLLMALREHLPGLEILHTDEELIPYECDGLSAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 98 QEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISDAVSADGFFYAPDPSSQLACTIGGNIGMNSGGAHCLKYGVTTN 177
Cdd:PRK11230 98 LEKGVLLVMARFNRILDINPVGRRARVQPGVRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 178 NLLGVKMVLFDGTVIELGGKALDAPGYDLLGLVCGSEGQLGIVTEATVRLIAKPEGARPVLFGFASSESAGSCVADIIGS 257
Cdd:PRK11230 178 NLLKVEILTLDGEALTLGSDALDSPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 258 GIIPVAIEFMDRPAIEICEAFAQAGYPLDVEALLIVEVEGSEAEMDATLAGIIEIARRHGVMTIRESQSALEAALIWKGR 337
Cdd:PRK11230 258 GIIPGGLEMMDNLSIRAAEDFIHAGYPVDAEAILLCELDGVESDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 338 KSAFGATGRIA-DYICMDGTVPLSQLSHVLRRTGEIVAGYGLRVANVFHAGDGNMHPLILYNINDPEEAARAEAAGNDIL 416
Cdd:PRK11230 338 KNAFPAVGRISpDYYCMDGTIPRRELPGVLEGIARLSQQYGLRVANVFHAGDGNMHPLILFDANEPGELERAEALGGKIL 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499271415 417 KLCVEAGGCLTGEHGVGIEKRDLMLHQYSRADLGQQMAARAAFDPQWLMNPSKVFPLEGRPA 478
Cdd:PRK11230 418 ELCVEVGGSITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPDGLLNPGKNIPTLHRCA 479
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
18-472 |
3.75e-170 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 487.09 E-value: 3.75e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 18 RREIVADLADLLPeGGLISDERGLKPFETDAFIAYRRMPLAVVLPETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGGAIP 97
Cdd:COG0277 3 TAALLAALRAILA-GRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 98 QEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISDAVSADGFFYAPDPSSQLACTIGGNIGMNSGGAHCLKYGVTTN 177
Cdd:COG0277 82 LDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 178 NLLGVKMVLFDGTVIELGGKAL-DAPGYDLLGLVCGSEGQLGIVTEATVRLIAKPEGARPVLFGFASSESAGSCVADIIG 256
Cdd:COG0277 162 NVLGLEVVLADGEVVRTGGRVPkNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 257 SGIIPVAIEFMDRPAIEICEAFAQAGYPLDVEALLIVEVEGS-EAEMDATLAGIIEIARRHGVMTIRESQSALEAALIWK 335
Cdd:COG0277 242 AGIAPAALELMDRAALALVEAAPPLGLPEDGGALLLVEFDGDdAEEVEAQLARLRAILEAGGATDVRVAADGAERERLWK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 336 GRKSAFGATGRIADY--ICMDGTVPLSQLSHVLRRTGEIVAGYGLRVANVFHAGDGNMHPLILYNINDPEEAARAEAAGN 413
Cdd:COG0277 322 ARKAALPALGRLDGGakLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAAAE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 499271415 414 DILKLCVEAGGCLTGEHGVGIEKRDLMLHQYSRADLGQQMAARAAFDPQWLMNPSKVFP 472
Cdd:COG0277 402 EIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
59-469 |
4.76e-153 |
|
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: 441.52 E-value: 4.76e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 59 VVLPETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGGAIPQEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISDAVS 138
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQAVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 139 ADGFFYAPDPSSQLACTIGGNIGMNSGGAHCLKYGVTTNNLLGVKMVLFDGTVIELGGK-ALDAPGYDLLGLVCGSEGQL 217
Cdd:TIGR00387 81 EHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKtAKDVAGYDLTGLFVGSEGTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 218 GIVTEATVRLIAKPEGARPVLFGFASSESAGSCVADIIGSGIIPVAIEFMDRPAIEICEAFAQAGYPLDVEALLIVEVEG 297
Cdd:TIGR00387 161 GIVTEATLKLLPKPENIVVALAFFDSIEKAMQAVYDIIAAGIIPAGMEFLDNLSIKAVEDISGIGLPKDAGAILLVEIDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 298 SEAEMDATLAGIIEIARRHGVMTIRESQSALEAALIWKGRKSAFGATGRIA-DYICMDGTVPLSQLSHVLRRTGEIVAGY 376
Cdd:TIGR00387 241 VHEAVERDEEKIEQICRKNGAVDVQIAQDEEERALLWAGRRNAFKAASKLSpLYLIEDGTVPRSKLPEALRGIADIASKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 377 GLRVANVFHAGDGNMHPLILYNINDPEEAARAEAAGNDILKLCVEAGGCLTGEHGVGIEKRDLMLHQYSRADLGQQMAAR 456
Cdd:TIGR00387 321 DFTIANFGHAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRAIK 400
|
410
....*....|...
gi 499271415 457 AAFDPQWLMNPSK 469
Cdd:TIGR00387 401 KAFDPDNILNPGK 413
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
230-470 |
3.80e-56 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 187.14 E-value: 3.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 230 KPEGARPVLFGFASSESAGSCVADIIGSGIIPVAIEFMDRPAIEICEAFA--QAGYPLDVEALLIVEVEGSEAEMD-ATL 306
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLgfPKGLPRDAAALLLVEFEGDDEETAeEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 307 AGIIEIARRHGVMTIRESQSALEAALIWKGRKSAFGATGRIAD----YICMDGTVPLSQLSHVLRRTGEIVAGYGLRVAN 382
Cdd:pfam02913 81 EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPLRDALGGagpaVFSEDVSVPRSRLADLVRDIKELLDKYGLVVCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 383 VFHAGDGNMHPLILYNINDPEEAARAEAAGNDILKLCVEAGGCLTGEHGVGIEKRDLMLHQYSRADLGQQMAARAAFDPQ 462
Cdd:pfam02913 161 FGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPK 240
|
....*...
gi 499271415 463 WLMNPSKV 470
Cdd:pfam02913 241 GILNPGKV 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
18-478 |
1.61e-171 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 491.98 E-value: 1.61e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 18 RREIVADLADLLPEGGLISDERGLKPFETDAFIAYRRMPLAVVLPETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGGAIP 97
Cdd:PRK11230 18 RTSLLMALREHLPGLEILHTDEELIPYECDGLSAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 98 QEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISDAVSADGFFYAPDPSSQLACTIGGNIGMNSGGAHCLKYGVTTN 177
Cdd:PRK11230 98 LEKGVLLVMARFNRILDINPVGRRARVQPGVRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 178 NLLGVKMVLFDGTVIELGGKALDAPGYDLLGLVCGSEGQLGIVTEATVRLIAKPEGARPVLFGFASSESAGSCVADIIGS 257
Cdd:PRK11230 178 NLLKVEILTLDGEALTLGSDALDSPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 258 GIIPVAIEFMDRPAIEICEAFAQAGYPLDVEALLIVEVEGSEAEMDATLAGIIEIARRHGVMTIRESQSALEAALIWKGR 337
Cdd:PRK11230 258 GIIPGGLEMMDNLSIRAAEDFIHAGYPVDAEAILLCELDGVESDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 338 KSAFGATGRIA-DYICMDGTVPLSQLSHVLRRTGEIVAGYGLRVANVFHAGDGNMHPLILYNINDPEEAARAEAAGNDIL 416
Cdd:PRK11230 338 KNAFPAVGRISpDYYCMDGTIPRRELPGVLEGIARLSQQYGLRVANVFHAGDGNMHPLILFDANEPGELERAEALGGKIL 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499271415 417 KLCVEAGGCLTGEHGVGIEKRDLMLHQYSRADLGQQMAARAAFDPQWLMNPSKVFPLEGRPA 478
Cdd:PRK11230 418 ELCVEVGGSITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPDGLLNPGKNIPTLHRCA 479
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
18-472 |
3.75e-170 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 487.09 E-value: 3.75e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 18 RREIVADLADLLPeGGLISDERGLKPFETDAFIAYRRMPLAVVLPETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGGAIP 97
Cdd:COG0277 3 TAALLAALRAILA-GRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 98 QEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISDAVSADGFFYAPDPSSQLACTIGGNIGMNSGGAHCLKYGVTTN 177
Cdd:COG0277 82 LDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 178 NLLGVKMVLFDGTVIELGGKAL-DAPGYDLLGLVCGSEGQLGIVTEATVRLIAKPEGARPVLFGFASSESAGSCVADIIG 256
Cdd:COG0277 162 NVLGLEVVLADGEVVRTGGRVPkNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 257 SGIIPVAIEFMDRPAIEICEAFAQAGYPLDVEALLIVEVEGS-EAEMDATLAGIIEIARRHGVMTIRESQSALEAALIWK 335
Cdd:COG0277 242 AGIAPAALELMDRAALALVEAAPPLGLPEDGGALLLVEFDGDdAEEVEAQLARLRAILEAGGATDVRVAADGAERERLWK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 336 GRKSAFGATGRIADY--ICMDGTVPLSQLSHVLRRTGEIVAGYGLRVANVFHAGDGNMHPLILYNINDPEEAARAEAAGN 413
Cdd:COG0277 322 ARKAALPALGRLDGGakLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAAAE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 499271415 414 DILKLCVEAGGCLTGEHGVGIEKRDLMLHQYSRADLGQQMAARAAFDPQWLMNPSKVFP 472
Cdd:COG0277 402 EIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
59-469 |
4.76e-153 |
|
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: 441.52 E-value: 4.76e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 59 VVLPETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGGAIPQEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISDAVS 138
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQAVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 139 ADGFFYAPDPSSQLACTIGGNIGMNSGGAHCLKYGVTTNNLLGVKMVLFDGTVIELGGK-ALDAPGYDLLGLVCGSEGQL 217
Cdd:TIGR00387 81 EHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKtAKDVAGYDLTGLFVGSEGTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 218 GIVTEATVRLIAKPEGARPVLFGFASSESAGSCVADIIGSGIIPVAIEFMDRPAIEICEAFAQAGYPLDVEALLIVEVEG 297
Cdd:TIGR00387 161 GIVTEATLKLLPKPENIVVALAFFDSIEKAMQAVYDIIAAGIIPAGMEFLDNLSIKAVEDISGIGLPKDAGAILLVEIDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 298 SEAEMDATLAGIIEIARRHGVMTIRESQSALEAALIWKGRKSAFGATGRIA-DYICMDGTVPLSQLSHVLRRTGEIVAGY 376
Cdd:TIGR00387 241 VHEAVERDEEKIEQICRKNGAVDVQIAQDEEERALLWAGRRNAFKAASKLSpLYLIEDGTVPRSKLPEALRGIADIASKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 377 GLRVANVFHAGDGNMHPLILYNINDPEEAARAEAAGNDILKLCVEAGGCLTGEHGVGIEKRDLMLHQYSRADLGQQMAAR 456
Cdd:TIGR00387 321 DFTIANFGHAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRAIK 400
|
410
....*....|...
gi 499271415 457 AAFDPQWLMNPSK 469
Cdd:TIGR00387 401 KAFDPDNILNPGK 413
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
230-470 |
3.80e-56 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 187.14 E-value: 3.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 230 KPEGARPVLFGFASSESAGSCVADIIGSGIIPVAIEFMDRPAIEICEAFA--QAGYPLDVEALLIVEVEGSEAEMD-ATL 306
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLgfPKGLPRDAAALLLVEFEGDDEETAeEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 307 AGIIEIARRHGVMTIRESQSALEAALIWKGRKSAFGATGRIAD----YICMDGTVPLSQLSHVLRRTGEIVAGYGLRVAN 382
Cdd:pfam02913 81 EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPLRDALGGagpaVFSEDVSVPRSRLADLVRDIKELLDKYGLVVCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 383 VFHAGDGNMHPLILYNINDPEEAARAEAAGNDILKLCVEAGGCLTGEHGVGIEKRDLMLHQYSRADLGQQMAARAAFDPQ 462
Cdd:pfam02913 161 FGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPK 240
|
....*...
gi 499271415 463 WLMNPSKV 470
Cdd:pfam02913 241 GILNPGKV 248
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
19-472 |
2.35e-52 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 185.60 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 19 REIVADLADLLPEG-GLISDERGLKPFETDAFIAYRRMPLAVVLPETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGGAIP 97
Cdd:PLN02805 96 QELIDELKAILQDNmTLDYDERYFHGKPQNSFHKAVNIPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 98 QEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISDAVSADGFFYAPDPSSqlACTIGGNIGMNSGGAHCLKYGVTTN 177
Cdd:PLN02805 176 PHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPGP--GATIGGMCATRCSGSLAVRYGTMRD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 178 NLLGVKMVLFDGTVIELGGKAL-DAPGYDLLGLVCGSEGQLGIVTEATVRLIAKPEGARPVLFGFASSESAGSCVADIIG 256
Cdd:PLN02805 254 NVISLKVVLPNGDVVKTASRARkSAAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIATML 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 257 SGIIPVAIEFMDR---PAIEICEafaqaGYPLDVEALLIVEVEGSEAEMDATLAGIIEIARRHG---VMTIRESQSALEa 330
Cdd:PLN02805 334 SGIQVSRVELLDEvqiRAINMAN-----GKNLPEAPTLMFEFIGTEAYAREQTLIVQKIASKHNgsdFVFAEEPEAKKE- 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 331 alIWKGRKSAFGATGRIA-DYICM--DGTVPLSQLSHVLRRTGEIVAGYGLRVANVFHAGDGNMHPLILYNINDPEEAAR 407
Cdd:PLN02805 408 --LWKIRKEALWACFAMEpKYEAMitDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFDPSQEDQRRE 485
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499271415 408 AEAAGNDILKLCVEAGGCLTGEHGVGIEKRDLMLHQYSRADLGQQMAARAAFDPQWLMNPSKVFP 472
Cdd:PLN02805 486 AERLNHFMVHTALSMEGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIP 550
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
56-195 |
1.19e-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: 155.82 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 56 PLAVVLPETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGGAIpQEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISD 135
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAV-QTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVR 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 136 AVSADGFFYAPDPSSQLACTIGGNIGMNSGGAHCLKYGVTTNNLLGVKMVLFDGTVIELG 195
Cdd:pfam01565 80 ALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRLG 139
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
62-226 |
3.39e-07 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 52.54 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 62 PETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGGAIPQEDaiVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISDAVSADG 141
Cdd:PLN02465 103 PESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAFSREG--MVNLALMDKVLEVDKEKKRVTVQAGARVQQVVEALRPHG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 142 FF---YAPDPSSQlactIGGNIGMnsgGAHclkyGVttnnllGVKMVLFDGTVIELggkALDAPGYDLLGLV-------- 210
Cdd:PLN02465 181 LTlqnYASIREQQ----IGGFIQV---GAH----GT------GARIPPIDEQVVSM---KLVTPAKGTIELSkeddpelf 240
|
170 180
....*....|....*....|
gi 499271415 211 ----CGSeGQLGIVTEATVR 226
Cdd:PLN02465 241 rlarCGL-GGLGVVAEVTLQ 259
|
|
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
60-227 |
3.30e-06 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 48.57 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 60 VLPETTEHVAAVLKYCSRYGIPIVPRGAGTSL--SGGAIPqedAIVVGLSKMSRTLDIDlfNRTATVQAGVTNLNISDAV 137
Cdd:PRK13905 35 VEPADIEDLQEFLKLLKENNIPVTVLGNGSNLlvRDGGIR---GVVIRLGKGLNEIEVE--GNRITAGAGAPLIKLARFA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 138 SADGF----FYAPDPSsqlacTIGGNIGMNsGGAhclkYGVTT-NNLLGVKMVLFDGTVIELGGKALDApGYDllglvcG 212
Cdd:PRK13905 110 AEAGLsgleFAAGIPG-----TVGGAVFMN-AGA----YGGETaDVLESVEVLDRDGEIKTLSNEELGF-GYR------H 172
|
170
....*....|....*..
gi 499271415 213 SEGQLG--IVTEATVRL 227
Cdd:PRK13905 173 SALQEEglIVLSATFQL 189
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
52-228 |
7.82e-06 |
|
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: 47.97 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 52 YRRMPLAVVLPETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGgaIPQEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNL 131
Cdd:TIGR01678 11 YSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSD--IACTDGFLIHLDKMNKVLQFDKEKKQITVEAGIRLY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 132 NISDAVSADGfFYAPDPSSQLACTIGGNIGMNSGGAHcLKYGVTTNNLLGVKMVLFDGTVIELgGKALDApgyDLLGLVC 211
Cdd:TIGR01678 89 QLHEQLDEHG-YSMSNLGSISEVSVAGIISTGTHGSS-IKHGILATQVVALTIMTADGEVLEC-SEERNA---DVFQAAR 162
|
170
....*....|....*..
gi 499271415 212 GSEGQLGIVTEATVRLI 228
Cdd:TIGR01678 163 VSLGCLGIIVTVTIQVV 179
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
62-232 |
9.73e-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: 41.59 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 62 PETTEHVAAVLKYCSRYGIPIVPRGAGTSLSGgaIPQEDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNISDAVSADG 141
Cdd:TIGR01676 68 PEAIEELEGIVKQANEKKARIRPVGSGLSPNG--IGLSRAGMVNLALMDKVLEVDEEKKRVRVQAGIRVQQLVDAIKEYG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 142 FF---YAPDPSSQlactIGG--NIGMNSGGAhclKYGVTTNNLLGVKMVLFDGTVIELgGKALDApgyDLLGLVCGSEGQ 216
Cdd:TIGR01676 146 ITlqnFASIREQQ----IGGiiQVGAHGTGA---KLPPIDEQVIAMKLVTPAKGTIEI-SKDKDP---ELFFLARCGLGG 214
|
170
....*....|....*.
gi 499271415 217 LGIVTEATVRLIAKPE 232
Cdd:TIGR01676 215 LGVVAEVTLQCVERQE 230
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
58-243 |
3.14e-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: 39.84 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 58 AVVLPETTEHVAAVLKYCSRYGIPI-VPRGAGTSLSGGAIPQ--EDAIVVGLSKMSRTLDIDLFNRTATVQAGVTNLNIS 134
Cdd:TIGR01677 34 NVAYPKTEAELVSVVAAATAAGRKMkVVTRYSHSIPKLACPDgsDGALLISTKRLNHVVAVDATAMTVTVESGMSLRELI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271415 135 DAVSADGFF--YAPdpsSQLACTIGGNIGMNSGGAHCL-KYGVTTNNLLGVKMVL----FDGTVIELGGKALDAPgyDLL 207
Cdd:TIGR01677 114 VEAEKAGLAlpYAP---YWWGLTVGGMMGTGAHGSSLWgKGSAVHDYVVGIRLVVpasaAEGFAKVRILSEGDTP--NEF 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 499271415 208 GLVCGSEGQLGIVTEATVRLiaKPEGARPVLFGFAS 243
Cdd:TIGR01677 189 NAAKVSLGVLGVISQVTLAL--QPMFKRSVTYTMRD 222
|
|
| |
