|
Name |
Accession |
Description |
Interval |
E-value |
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
44-456 |
0e+00 |
|
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: 578.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 44 IVRPHTAEEVQQIVKLCASYKVPIVPRGSGTNLCAGTCPTQGGLVILFTRMNQLLEIDEENLTATVQPGLITQELIHQVE 123
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQAVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 124 EKGLFYPPDPSSMKISTLGGNINENSGGLRGLKYGVTRDYVLGLEVVLPNGDIIKTGGKLAKDVAGYDMTRLFVGSEGTL 203
Cdd:TIGR00387 81 EHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKTAKDVAGYDLTGLFVGSEGTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 204 GIVTEAVLKLLPLPETKQTMLCLYESLEEAATSVSAIIAERIIPATLEFMDQPTLEVVEDFANIGLPTDVQAVLLIEQDG 283
Cdd:TIGR00387 161 GIVTEATLKLLPKPENIVVALAFFDSIEKAMQAVYDIIAAGIIPAGMEFLDNLSIKAVEDISGIGLPKDAGAILLVEIDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 284 NPEAVSRDIQKIAEVCEQHGATSVKIAHSEEEASALLTARRSALSALARLSPTTILEDATVPRSEIANMVRAIEDIARKY 363
Cdd:TIGR00387 241 VHEAVERDEEKIEQICRKNGAVDVQIAQDEEERALLWAGRRNAFKAASKLSPLYLIEDGTVPRSKLPEALRGIADIASKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 364 KVNICTFGHAGDGNLHPTCATDARNEEEMKRVEAAFQAIFEKAVALGGTITGEHGVGLMKAPYLELKVKKEGIAAMKAIK 443
Cdd:TIGR00387 321 DFTIANFGHAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRAIK 400
|
410
....*....|...
gi 518573741 444 QALDPAHIMNPDK 456
Cdd:TIGR00387 401 KAFDPDNILNPGK 413
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
1-459 |
0e+00 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 576.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 1 MLDSEFSNQLKEIVgAPNVQDSKADRLAYSYDATPNFQQMPDAIVRPHTAEEVQQIVKLCASYKVPIVPRGSGTNLCAGT 80
Cdd:COG0277 1 MLTAALLAALRAIL-AGRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 81 CPTQGGLVILFTRMNQLLEIDEENLTATVQPGLITQELIHQVEEKGLFYPPDPSSMKISTLGGNINENSGGLRGLKYGVT 160
Cdd:COG0277 80 VPLDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 161 RDYVLGLEVVLPNGDIIKTGGKLAKDVAGYDMTRLFVGSEGTLGIVTEAVLKLLPLPETKQTMLCLYESLEEAATSVSAI 240
Cdd:COG0277 160 RDNVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 241 IAERIIPATLEFMDQPTLEVVEDFANIGLPTDVQAVLLIEQDGN-PEAVSRDIQKIAEVCEQHGATSVKIAHSEEEASAL 319
Cdd:COG0277 240 LAAGIAPAALELMDRAALALVEAAPPLGLPEDGGALLLVEFDGDdAEEVEAQLARLRAILEAGGATDVRVAADGAERERL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 320 LTARRSALSALARLSPT-TILEDATVPRSEIANMVRAIEDIARKYKVNICTFGHAGDGNLHPTCATDARNEEEMKRVEAA 398
Cdd:COG0277 320 WKARKAALPALGRLDGGaKLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573741 399 FQAIFEKAVALGGTITGEHGVGLMKAPYLELKVKKEGIAAMKAIKQALDPAHIMNPDKVFG 459
Cdd:COG0277 400 AEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
9-456 |
3.22e-111 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 337.52 E-value: 3.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 9 QLKEIVGAPNVQDSKADRLAYSYDATPNFQQMPDAIVRPHTAEEVQQIVKLCASYKVPIVPRGSGTNLCAGTCPTQGGLV 88
Cdd:PRK11230 24 ALREHLPGLEILHTDEELIPYECDGLSAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKGVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 89 ILFTRMNQLLEIDEENLTATVQPGLITQELIHQVEEKGLFYPPDPSSMKISTLGGNINENSGGLRGLKYGVTRDYVLGLE 168
Cdd:PRK11230 104 LVMARFNRILDINPVGRRARVQPGVRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 169 VVLPNGDIIKTGGKlAKDVAGYDMTRLFVGSEGTLGIVTEAVLKLLPLPETKQTMLCLYESLEEAATSVSAIIAERIIPA 248
Cdd:PRK11230 184 ILTLDGEALTLGSD-ALDSPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 249 TLEFMDQPTLEVVEDFANIGLPTDVQAVLLIEQDGNPEAVSRDIQKIAEVCEQHGATSVKIAHSEEEASALLTARRSALS 328
Cdd:PRK11230 263 GLEMMDNLSIRAAEDFIHAGYPVDAEAILLCELDGVESDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGRKNAFP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 329 ALARLSPTTILEDATVPRSEIANMVRAIEDIARKYKVNICTFGHAGDGNLHPTCATDARNEEEMKRVEAAFQAIFEKAVA 408
Cdd:PRK11230 343 AVGRISPDYYCMDGTIPRRELPGVLEGIARLSQQYGLRVANVFHAGDGNMHPLILFDANEPGELERAEALGGKILELCVE 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 518573741 409 LGGTITGEHGVGLMKAPYLELKVKKEGIAAMKAIKQALDPAHIMNPDK 456
Cdd:PRK11230 423 VGGSITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPDGLLNPGK 470
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
216-457 |
5.59e-86 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 263.79 E-value: 5.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 216 LPETKQTMLCLYESLEEAATSVSAIIAERIIPATLEFMDQPTLEVVEDFANI--GLPTDVQAVLLIEQDGNPEAVS-RDI 292
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFpkGLPRDAAALLLVEFEGDDEETAeEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 293 QKIAEVCEQHGATSVKIAHSEEEASALLTARRSAL---SALARLSPTTILEDATVPRSEIANMVRAIEDIARKYKVNICT 369
Cdd:pfam02913 81 EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALplrDALGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKYGLVVCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 370 FGHAGDGNLHPTCATDARNEEEMKRVEAAFQAIFEKAVALGGTITGEHGVGLMKAPYLELKVKKEGIAAMKAIKQALDPA 449
Cdd:pfam02913 161 FGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPK 240
|
....*...
gi 518573741 450 HIMNPDKV 457
Cdd:pfam02913 241 GILNPGKV 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glcD |
TIGR00387 |
glycolate oxidase, subunit GlcD; This protein, the glycolate oxidase GlcD subunit, is similar ... |
44-456 |
0e+00 |
|
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: 578.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 44 IVRPHTAEEVQQIVKLCASYKVPIVPRGSGTNLCAGTCPTQGGLVILFTRMNQLLEIDEENLTATVQPGLITQELIHQVE 123
Cdd:TIGR00387 1 VVFPKNTEQVARILKLCHEHRIPIVPRGAGTGLSGGALPEEGGLVLVFKHMNKILEIDVVNLTAVVQPGVRNLELEQAVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 124 EKGLFYPPDPSSMKISTLGGNINENSGGLRGLKYGVTRDYVLGLEVVLPNGDIIKTGGKLAKDVAGYDMTRLFVGSEGTL 203
Cdd:TIGR00387 81 EHNLFYPPDPSSQISSTIGGNIAENAGGMRGLKYGTTVDYVLGLEVVTADGEILRIGGKTAKDVAGYDLTGLFVGSEGTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 204 GIVTEAVLKLLPLPETKQTMLCLYESLEEAATSVSAIIAERIIPATLEFMDQPTLEVVEDFANIGLPTDVQAVLLIEQDG 283
Cdd:TIGR00387 161 GIVTEATLKLLPKPENIVVALAFFDSIEKAMQAVYDIIAAGIIPAGMEFLDNLSIKAVEDISGIGLPKDAGAILLVEIDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 284 NPEAVSRDIQKIAEVCEQHGATSVKIAHSEEEASALLTARRSALSALARLSPTTILEDATVPRSEIANMVRAIEDIARKY 363
Cdd:TIGR00387 241 VHEAVERDEEKIEQICRKNGAVDVQIAQDEEERALLWAGRRNAFKAASKLSPLYLIEDGTVPRSKLPEALRGIADIASKY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 364 KVNICTFGHAGDGNLHPTCATDARNEEEMKRVEAAFQAIFEKAVALGGTITGEHGVGLMKAPYLELKVKKEGIAAMKAIK 443
Cdd:TIGR00387 321 DFTIANFGHAGDGNLHPTILTDPEDKGEMERVEEAGGEIFELAIELGGTISGEHGIGVVKAEFMPYKFNEKELETMRAIK 400
|
410
....*....|...
gi 518573741 444 QALDPAHIMNPDK 456
Cdd:TIGR00387 401 KAFDPDNILNPGK 413
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
1-459 |
0e+00 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 576.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 1 MLDSEFSNQLKEIVgAPNVQDSKADRLAYSYDATPNFQQMPDAIVRPHTAEEVQQIVKLCASYKVPIVPRGSGTNLCAGT 80
Cdd:COG0277 1 MLTAALLAALRAIL-AGRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 81 CPTQGGLVILFTRMNQLLEIDEENLTATVQPGLITQELIHQVEEKGLFYPPDPSSMKISTLGGNINENSGGLRGLKYGVT 160
Cdd:COG0277 80 VPLDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 161 RDYVLGLEVVLPNGDIIKTGGKLAKDVAGYDMTRLFVGSEGTLGIVTEAVLKLLPLPETKQTMLCLYESLEEAATSVSAI 240
Cdd:COG0277 160 RDNVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 241 IAERIIPATLEFMDQPTLEVVEDFANIGLPTDVQAVLLIEQDGN-PEAVSRDIQKIAEVCEQHGATSVKIAHSEEEASAL 319
Cdd:COG0277 240 LAAGIAPAALELMDRAALALVEAAPPLGLPEDGGALLLVEFDGDdAEEVEAQLARLRAILEAGGATDVRVAADGAERERL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 320 LTARRSALSALARLSPT-TILEDATVPRSEIANMVRAIEDIARKYKVNICTFGHAGDGNLHPTCATDARNEEEMKRVEAA 398
Cdd:COG0277 320 WKARKAALPALGRLDGGaKLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERARAA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573741 399 FQAIFEKAVALGGTITGEHGVGLMKAPYLELKVKKEGIAAMKAIKQALDPAHIMNPDKVFG 459
Cdd:COG0277 400 AEEIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILP 460
|
|
| PRK11230 |
PRK11230 |
glycolate oxidase subunit GlcD; Provisional |
9-456 |
3.22e-111 |
|
glycolate oxidase subunit GlcD; Provisional
Pssm-ID: 183043 [Multi-domain] Cd Length: 499 Bit Score: 337.52 E-value: 3.22e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 9 QLKEIVGAPNVQDSKADRLAYSYDATPNFQQMPDAIVRPHTAEEVQQIVKLCASYKVPIVPRGSGTNLCAGTCPTQGGLV 88
Cdd:PRK11230 24 ALREHLPGLEILHTDEELIPYECDGLSAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKGVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 89 ILFTRMNQLLEIDEENLTATVQPGLITQELIHQVEEKGLFYPPDPSSMKISTLGGNINENSGGLRGLKYGVTRDYVLGLE 168
Cdd:PRK11230 104 LVMARFNRILDINPVGRRARVQPGVRNLAISQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 169 VVLPNGDIIKTGGKlAKDVAGYDMTRLFVGSEGTLGIVTEAVLKLLPLPETKQTMLCLYESLEEAATSVSAIIAERIIPA 248
Cdd:PRK11230 184 ILTLDGEALTLGSD-ALDSPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 249 TLEFMDQPTLEVVEDFANIGLPTDVQAVLLIEQDGNPEAVSRDIQKIAEVCEQHGATSVKIAHSEEEASALLTARRSALS 328
Cdd:PRK11230 263 GLEMMDNLSIRAAEDFIHAGYPVDAEAILLCELDGVESDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGRKNAFP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 329 ALARLSPTTILEDATVPRSEIANMVRAIEDIARKYKVNICTFGHAGDGNLHPTCATDARNEEEMKRVEAAFQAIFEKAVA 408
Cdd:PRK11230 343 AVGRISPDYYCMDGTIPRRELPGVLEGIARLSQQYGLRVANVFHAGDGNMHPLILFDANEPGELERAEALGGKILELCVE 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 518573741 409 LGGTITGEHGVGLMKAPYLELKVKKEGIAAMKAIKQALDPAHIMNPDK 456
Cdd:PRK11230 423 VGGSITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPDGLLNPGK 470
|
|
| FAD-oxidase_C |
pfam02913 |
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold. |
216-457 |
5.59e-86 |
|
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
Pssm-ID: 397178 Cd Length: 248 Bit Score: 263.79 E-value: 5.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 216 LPETKQTMLCLYESLEEAATSVSAIIAERIIPATLEFMDQPTLEVVEDFANI--GLPTDVQAVLLIEQDGNPEAVS-RDI 292
Cdd:pfam02913 1 LPEVRAVALVGFPSFEAAVKAVREIARAGIIPAALELMDNDALDLVEATLGFpkGLPRDAAALLLVEFEGDDEETAeEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 293 QKIAEVCEQHGATSVKIAHSEEEASALLTARRSAL---SALARLSPTTILEDATVPRSEIANMVRAIEDIARKYKVNICT 369
Cdd:pfam02913 81 EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALplrDALGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKYGLVVCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 370 FGHAGDGNLHPTCATDARNEEEMKRVEAAFQAIFEKAVALGGTITGEHGVGLMKAPYLELKVKKEGIAAMKAIKQALDPA 449
Cdd:pfam02913 161 FGHAGDGNLHLYILFDFRDPEQEERAEKLFDEIMDLALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFDPK 240
|
....*...
gi 518573741 450 HIMNPDKV 457
Cdd:pfam02913 241 GILNPGKV 248
|
|
| PLN02805 |
PLN02805 |
D-lactate dehydrogenase [cytochrome] |
5-457 |
1.36e-83 |
|
D-lactate dehydrogenase [cytochrome]
Pssm-ID: 178402 [Multi-domain] Cd Length: 555 Bit Score: 268.03 E-value: 1.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 5 EFSNQLKEIVGapnvQDSKADRLAYSYDATP--NFQQ---MPDAIVRPHTAEEVQQIVKLCASYKVPIVPRGSGTNLCAG 79
Cdd:PLN02805 97 ELIDELKAILQ----DNMTLDYDERYFHGKPqnSFHKavnIPDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGH 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 80 TCPTQGGLVILFTRMNQLLEIDEENLTATVQPGLITQELIHQVEEKGLFYPPDPSSMkiSTLGGNINENSGGLRGLKYGV 159
Cdd:PLN02805 173 TLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEYLEPYGLFFPLDPGPG--ATIGGMCATRCSGSLAVRYGT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 160 TRDYVLGLEVVLPNGDIIKTGGKLAKDVAGYDMTRLFVGSEGTLGIVTEAVLKLLPLPETKQTMLCLYESLEEAATSVSA 239
Cdd:PLN02805 251 MRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEGTLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADVAIA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 240 IIAERIIPATLEFMDQPTLEVVEDFANIGLPTdvQAVLLIEQDGNpEAVSRD----IQKIAevcEQHGATSVKIAHSEEE 315
Cdd:PLN02805 331 TMLSGIQVSRVELLDEVQIRAINMANGKNLPE--APTLMFEFIGT-EAYAREqtliVQKIA---SKHNGSDFVFAEEPEA 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 316 ASALLTARRSALSALARLSPT--TILEDATVPRSEIANMVRAIEDIARKYKVNICTFGHAGDGNLHPTCATDARNEEEMK 393
Cdd:PLN02805 405 KKELWKIRKEALWACFAMEPKyeAMITDVCVPLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILFDPSQEDQRR 484
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518573741 394 RVEAAFQAIFEKAVALGGTITGEHGVGLMKAPYLELKVKKEGIAAMKAIKQALDPAHIMNPDKV 457
Cdd:PLN02805 485 EAERLNHFMVHTALSMEGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKALDPNNIMNPGKL 548
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
41-180 |
9.41e-51 |
|
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: 168.92 E-value: 9.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 41 PDAIVRPHTAEEVQQIVKLCASYKVPIVPRGSGTNLCAGTCPTqGGLVILFTRMNQLLEIDEENLTATVQPGLITQELIH 120
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQT-GGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVR 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 121 QVEEKGLFYPPDPSSMKISTLGGNINENSGGLRGLKYGVTRDYVLGLEVVLPNGDIIKTG 180
Cdd:pfam01565 80 ALAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRLG 139
|
|
| glcE |
PRK11282 |
glycolate oxidase FAD binding subunit; Provisional |
50-233 |
2.55e-15 |
|
glycolate oxidase FAD binding subunit; Provisional
Pssm-ID: 236893 [Multi-domain] Cd Length: 352 Bit Score: 77.18 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 50 AEEVQQivklCASYKVPIVPRGSGT-----NLCAGTcptqgglvILFTRMNQ-LLEIDEENLTATVQPGLITQELIHQVE 123
Cdd:PRK11282 8 LERVRQ----AAADGTPLRIRGGGSkdfygRALAGE--------VLDTRAHRgIVSYDPTELVITARAGTPLAELEAALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 124 EKG--L-FYPPDPSSMkiSTLGGNINENSGGLRGLKYGVTRDYVLGLEVVLPNGDIIKTGGKLAKDVAGYDMTRLFVGSE 200
Cdd:PRK11282 76 EAGqmLpFEPPHFGGG--ATLGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGEHLRFGGQVMKNVAGYDVSRLMAGSL 153
|
170 180 190
....*....|....*....|....*....|...
gi 518573741 201 GTLGIVTEAVLKLLPLPETKQTmLCLYESLEEA 233
Cdd:PRK11282 154 GTLGVLLEVSLKVLPRPRAELT-LRLEMDAAEA 185
|
|
| FAD_lactone_ox |
TIGR01678 |
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ... |
37-222 |
5.10e-11 |
|
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: 64.53 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 37 FQQMPDAIVRPHTAEEVQQIVKLCASYKVPIVPRGSG---TNLCAgtcpTQGGLVILfTRMNQLLEIDEENLTATVQPGL 113
Cdd:TIGR01678 11 YSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGhspSDIAC----TDGFLIHL-DKMNKVLQFDKEKKQITVEAGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 114 ITQELIHQVEEKGLFYpPDPSSMKISTLGGNINENSGGlRGLKYGVTRDYVLGLEVVLPNGDIIKTGGKLAKDVagYDMT 193
Cdd:TIGR01678 86 RLYQLHEQLDEHGYSM-SNLGSISEVSVAGIISTGTHG-SSIKHGILATQVVALTIMTADGEVLECSEERNADV--FQAA 161
|
170 180
....*....|....*....|....*....
gi 518573741 194 RLFVGSegtLGIVTEAVLKLLPLPETKQT 222
Cdd:TIGR01678 162 RVSLGC---LGIIVTVTIQVVPQFHLQET 187
|
|
| GLDHase |
TIGR01676 |
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ... |
46-212 |
1.80e-09 |
|
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: 59.69 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 46 RPHTAEEVQQIVKLCASYKVPIVPRGSGTNlCAGTCPTQGGLVILfTRMNQLLEIDEENLTATVQPGLITQELIHQVEEK 125
Cdd:TIGR01676 67 QPEAIEELEGIVKQANEKKARIRPVGSGLS-PNGIGLSRAGMVNL-ALMDKVLEVDEEKKRVRVQAGIRVQQLVDAIKEY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 126 GLFYpPDPSSMKISTLGGNINENSGGlRGLKYGVTRDYVLGLEVVLPNGDIIKTGGKlaKDVAGYDMTRLFVGSegtLGI 205
Cdd:TIGR01676 145 GITL-QNFASIREQQIGGIIQVGAHG-TGAKLPPIDEQVIAMKLVTPAKGTIEISKD--KDPELFFLARCGLGG---LGV 217
|
....*..
gi 518573741 206 VTEAVLK 212
Cdd:TIGR01676 218 VAEVTLQ 224
|
|
| pln_FAD_oxido |
TIGR01677 |
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ... |
30-216 |
2.07e-09 |
|
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: 59.49 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 30 SYDATPNFQQMPDA-IVRPHTAEEVQQIVKLCASY--KVPIVPRGSGTnLCAGTCP--TQGGLVILFTRMNQLLEIDEEN 104
Cdd:TIGR01677 20 AYGAFPDRSTCRAAnVAYPKTEAELVSVVAAATAAgrKMKVVTRYSHS-IPKLACPdgSDGALLISTKRLNHVVAVDATA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 105 LTATVQPGLITQELIHQVEEKGLFYPPDPSSMKIsTLGGNINENSGG--LRGlKYGVTRDYVLGLEVVLPnGDIIKTGGK 182
Cdd:TIGR01677 99 MTVTVESGMSLRELIVEAEKAGLALPYAPYWWGL-TVGGMMGTGAHGssLWG-KGSAVHDYVVGIRLVVP-ASAAEGFAK 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 518573741 183 LAKDVAGYDMTRLFVG--SEGTLGIVTEAVLKLLPL 216
Cdd:TIGR01677 176 VRILSEGDTPNEFNAAkvSLGVLGVISQVTLALQPM 211
|
|
| PLN02465 |
PLN02465 |
L-galactono-1,4-lactone dehydrogenase |
45-215 |
8.03e-09 |
|
L-galactono-1,4-lactone dehydrogenase
Pssm-ID: 215258 [Multi-domain] Cd Length: 573 Bit Score: 57.94 E-value: 8.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 45 VRPHTAEEVQQIVKLCASYKVPIVPRGSG--TNlcaGTCPTQGGLVILfTRMNQLLEIDEENLTATVQPGLITQELIHQV 122
Cdd:PLN02465 101 HQPESLEELEDIVKEAHEKGRRIRPVGSGlsPN---GLAFSREGMVNL-ALMDKVLEVDKEKKRVTVQAGARVQQVVEAL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 123 EEKGLFYpPDPSSMKISTLGGNINENSGGlRGLKYGVTRDYVLGLEVVLP-NGDIIKTGgklAKDVAGYDMTRLFVGSeg 201
Cdd:PLN02465 177 RPHGLTL-QNYASIREQQIGGFIQVGAHG-TGARIPPIDEQVVSMKLVTPaKGTIELSK---EDDPELFRLARCGLGG-- 249
|
170
....*....|....
gi 518573741 202 tLGIVTEAVLKLLP 215
Cdd:PLN02465 250 -LGVVAEVTLQCVP 262
|
|
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
42-215 |
1.94e-03 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 40.09 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 42 DAIVRPHTAEEVQQIVKLCASYKVPIVPRGSGTNLCA--GTCPtqgGLVILFTRMNQLLEIDEENLTAtvQPGLITQELI 119
Cdd:PRK13905 32 DYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVrdGGIR---GVVIRLGKGLNEIEVEGNRITA--GAGAPLIKLA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573741 120 HQVEEKGL----FY---PpdpssmkiSTLGGNINENSGGlrglkYGV-TRDYVLGLEVVLPNGDIIKTGgklAKDVA-GY 190
Cdd:PRK13905 107 RFAAEAGLsgleFAagiP--------GTVGGAVFMNAGA-----YGGeTADVLESVEVLDRDGEIKTLS---NEELGfGY 170
|
170 180
....*....|....*....|....*
gi 518573741 191 DMTRLFVGSEgtlgIVTEAVLKLLP 215
Cdd:PRK13905 171 RHSALQEEGL----IVLSATFQLEP 191
|
|
| |
