|
Name |
Accession |
Description |
Interval |
E-value |
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
12-435 |
2.78e-180 |
|
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.
Pssm-ID: 239448 [Multi-domain] Cd Length: 383 Bit Score: 507.98 E-value: 2.78e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 12 RQDALYRPGALGIAPTVPTRAEELEARALATMSRRAGAYIAGGAGGGATMRSNREAFDRWRVVPRMLHATTTRDLSTTLL 91
Cdd:cd03332 1 YQREIYLAGLLGRRPDLPVDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 92 GTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPMEETAQAMAGTPFWYQLYWSTDEELVDSMIGRA 171
Cdd:cd03332 81 GRTLAAPLLLAPIGVQELFHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 172 ETAGAQALVVTLDTTMLGWRTQDLDLGSLPFARGQGIAQYTSDPRFMELVRERLAAGARAAqslgidprrplqaaraakg 251
Cdd:cd03332 161 EKAGYRVLVVTLDTWSLGWRPRDLDLGYLPFLRGIGIANYFSDPVFRKKLAEPVGEDPEAP------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 252 gvatllsmsrehpggvrdnlrsPEPRAAVETFLDIYSNPALSWEHIATLRERTRLPVVLKGILHEDDARRAFDCGVDAVV 331
Cdd:cd03332 222 ----------------------PPMEAAVARFVSVFSGPSLTWEDLAFLREWTDLPIVLKGILHPDDARRAVEAGVDGVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 332 VSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVRSGADLFVALALGADACLLGRPHVYGLALDGEAGVSAVIDNV 411
Cdd:cd03332 280 VSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGRPYAYGLALGGEDGVEHVLRNL 359
|
410 420
....*....|....*....|....
gi 1119705313 412 LAELDLTMGLVGAATVDDITRELL 435
Cdd:cd03332 360 LAELDLTMGLAGIRSIAELTRDAL 383
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
60-436 |
1.05e-129 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 378.03 E-value: 1.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 60 TMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPM 139
Cdd:pfam01070 22 TLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALARAAAAAGIPFVLSTVSSTSL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 140 EETAQAmAGTPFWYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDLDLG-SLPFargqgiaqytsdprfm 218
Cdd:pfam01070 102 EEVAAA-AGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGfTLPP---------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 219 elvrerlaagaraaqslGIDPRRPLQAARaakggvatllsmsreHPGGVRDNLRSPEPRAAvETFLDIYSNPALSWEHIA 298
Cdd:pfam01070 165 -----------------RLTPRNLLDLAL---------------HPRWALGVLRRGGAGGA-AAFVGSQFDPALTWDDLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 299 TLRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVRSGADLFVA 378
Cdd:pfam01070 212 WLRERWKGPLVVKGILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKA 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119705313 379 LALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITRELLV 436
Cdd:pfam01070 292 LALGADAVLLGRPFLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
60-436 |
1.84e-126 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 370.23 E-value: 1.84e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 60 TMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPM 139
Cdd:COG1304 35 TLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGLAHPDGELALARAAAAAGIPMGLSTQSTTSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 140 EETAQAmAGTPFWYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDLDLG-SLPF-ARGQGIAQYTSDPRF 217
Cdd:COG1304 115 EEVAAA-APAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLGRRERDLREGfSQPPrLTPRNLLEAATHPRW 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 218 MElvrerlaagaraaqslgidprrplqaaraakggvatllsmsrehpggvrdnlrspePRAAVETFLDIYSNPALSWEHI 297
Cdd:COG1304 194 AL--------------------------------------------------------GLASLAAWLDTNFDPSLTWDDI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 298 ATLRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVRSGADLFV 377
Cdd:COG1304 218 AWLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAK 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119705313 378 ALALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITRELLV 436
Cdd:COG1304 298 ALALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
60-438 |
8.72e-63 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 207.57 E-value: 8.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 60 TMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPM 139
Cdd:PRK11197 34 TLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGMYARRGEVQAARAADAKGIPFTLSTVSVCPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 140 EETAQAMAGtPFWYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDLDLG-SLPFARGQGIAQYTSDPRFm 218
Cdd:PRK11197 114 EEVAPAIKR-PMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPGARYRDAHSGmSGPNAAMRRYLQAVTHPQW- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 219 elvrerlaagaraAQSLGIdprrplqaaraakggvatllsMSREHP-GGVRDNLRSPepraaveTFLDIYS-------NP 290
Cdd:PRK11197 192 -------------AWDVGL---------------------NGRPHDlGNISAYLGKP-------TGLEDYIgwlgnnfDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 291 ALSWEHIATLRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVR 370
Cdd:PRK11197 231 SISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIR 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119705313 371 SGADLFVALALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITRELLVEG 438
Cdd:PRK11197 311 NGLDVVRMIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQG 378
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
12-435 |
2.78e-180 |
|
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.
Pssm-ID: 239448 [Multi-domain] Cd Length: 383 Bit Score: 507.98 E-value: 2.78e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 12 RQDALYRPGALGIAPTVPTRAEELEARALATMSRRAGAYIAGGAGGGATMRSNREAFDRWRVVPRMLHATTTRDLSTTLL 91
Cdd:cd03332 1 YQREIYLAGLLGRRPDLPVDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 92 GTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPMEETAQAMAGTPFWYQLYWSTDEELVDSMIGRA 171
Cdd:cd03332 81 GRTLAAPLLLAPIGVQELFHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 172 ETAGAQALVVTLDTTMLGWRTQDLDLGSLPFARGQGIAQYTSDPRFMELVRERLAAGARAAqslgidprrplqaaraakg 251
Cdd:cd03332 161 EKAGYRVLVVTLDTWSLGWRPRDLDLGYLPFLRGIGIANYFSDPVFRKKLAEPVGEDPEAP------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 252 gvatllsmsrehpggvrdnlrsPEPRAAVETFLDIYSNPALSWEHIATLRERTRLPVVLKGILHEDDARRAFDCGVDAVV 331
Cdd:cd03332 222 ----------------------PPMEAAVARFVSVFSGPSLTWEDLAFLREWTDLPIVLKGILHPDDARRAVEAGVDGVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 332 VSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVRSGADLFVALALGADACLLGRPHVYGLALDGEAGVSAVIDNV 411
Cdd:cd03332 280 VSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGRPYAYGLALGGEDGVEHVLRNL 359
|
410 420
....*....|....*....|....
gi 1119705313 412 LAELDLTMGLVGAATVDDITRELL 435
Cdd:cd03332 360 LAELDLTMGLAGIRSIAELTRDAL 383
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
60-436 |
1.05e-129 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 378.03 E-value: 1.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 60 TMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPM 139
Cdd:pfam01070 22 TLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALARAAAAAGIPFVLSTVSSTSL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 140 EETAQAmAGTPFWYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDLDLG-SLPFargqgiaqytsdprfm 218
Cdd:pfam01070 102 EEVAAA-AGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGfTLPP---------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 219 elvrerlaagaraaqslGIDPRRPLQAARaakggvatllsmsreHPGGVRDNLRSPEPRAAvETFLDIYSNPALSWEHIA 298
Cdd:pfam01070 165 -----------------RLTPRNLLDLAL---------------HPRWALGVLRRGGAGGA-AAFVGSQFDPALTWDDLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 299 TLRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVRSGADLFVA 378
Cdd:pfam01070 212 WLRERWKGPLVVKGILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKA 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119705313 379 LALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITRELLV 436
Cdd:pfam01070 292 LALGADAVLLGRPFLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
60-436 |
1.84e-126 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 370.23 E-value: 1.84e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 60 TMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPM 139
Cdd:COG1304 35 TLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGLAHPDGELALARAAAAAGIPMGLSTQSTTSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 140 EETAQAmAGTPFWYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDLDLG-SLPF-ARGQGIAQYTSDPRF 217
Cdd:COG1304 115 EEVAAA-APAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLGRRERDLREGfSQPPrLTPRNLLEAATHPRW 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 218 MElvrerlaagaraaqslgidprrplqaaraakggvatllsmsrehpggvrdnlrspePRAAVETFLDIYSNPALSWEHI 297
Cdd:COG1304 194 AL--------------------------------------------------------GLASLAAWLDTNFDPSLTWDDI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 298 ATLRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVRSGADLFV 377
Cdd:COG1304 218 AWLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAK 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119705313 378 ALALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITRELLV 436
Cdd:COG1304 298 ALALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
60-432 |
1.67e-102 |
|
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.
Pssm-ID: 239203 [Multi-domain] Cd Length: 299 Bit Score: 307.07 E-value: 1.67e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 60 TMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPM 139
Cdd:cd02809 28 TLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPDGELATARAAAAAGIPFTLSTVSTTSL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 140 EETAQAmAGTPFWYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRtqdldlgslpfargqgiaqytsdprfme 219
Cdd:cd02809 108 EEVAAA-APGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR---------------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 220 lvrerlaagaraaqslgidprrplqaaraakggvatllsmsrehpggvrdnlrspepraavetfldiysnpaLSWEHIAT 299
Cdd:cd02809 159 ------------------------------------------------------------------------LTWDDLAW 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 300 LRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVRSGADLFVAL 379
Cdd:cd02809 167 LRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKAL 246
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1119705313 380 ALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITR 432
Cdd:cd02809 247 ALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
60-435 |
4.66e-69 |
|
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).
Pssm-ID: 240088 [Multi-domain] Cd Length: 351 Bit Score: 223.09 E-value: 4.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 60 TMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPM 139
Cdd:cd04737 36 TLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLAHATGEVATARGMAEVGSLFSISTYSNTSL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 140 EETAQAMAGTPFWYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDLdlgslpfargqgiaqytsdprfme 219
Cdd:cd04737 116 EEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGGNREADI------------------------ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 220 lvrerlaagaraaqslgidprrplqaaraakggvatllSMSREHPGGVRDNLRSPEPRAAVETFLDIY--SNPALSWEHI 297
Cdd:cd04737 172 --------------------------------------RNKFQFPFGMPNLNHFSEGTGKGKGISEIYaaAKQKLSPADI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 298 ATLRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVRSGADLFV 377
Cdd:cd04737 214 EFIAKISGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFK 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1119705313 378 ALALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITRELL 435
Cdd:cd04737 294 ALASGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKRTFL 351
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
60-430 |
2.45e-68 |
|
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.
Pssm-ID: 239238 [Multi-domain] Cd Length: 344 Bit Score: 220.93 E-value: 2.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 60 TMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPM 139
Cdd:cd02922 28 TLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPDGELNLARAAGKHGILQMISTNASCSL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 140 EE-TAQAMAGTPFWYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDldlgslpfargqgiaqytsdprfm 218
Cdd:cd02922 108 EEiVDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRERD------------------------ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 219 elvrERLAAGaraaqslgidprrplqaaraakggvatllSMSREHPGGVRDNLRSPEPRAAVETFLDiysnPALSWEHIA 298
Cdd:cd02922 164 ----ERLKAE-----------------------------EAVSDGPAGKKTKAKGGGAGRAMSGFID----PTLTWDDIK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 299 TLRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVRE---AVGPEPTLLMDSGVRSGADL 375
Cdd:cd02922 207 WLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIRKhcpEVFDKIEVYVDGGVRRGTDV 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1119705313 376 FVALALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDI 430
Cdd:cd02922 287 LKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLGVTSLDQL 341
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
60-438 |
8.72e-63 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 207.57 E-value: 8.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 60 TMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPM 139
Cdd:PRK11197 34 TLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGMYARRGEVQAARAADAKGIPFTLSTVSVCPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 140 EETAQAMAGtPFWYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDLDLG-SLPFARGQGIAQYTSDPRFm 218
Cdd:PRK11197 114 EEVAPAIKR-PMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPGARYRDAHSGmSGPNAAMRRYLQAVTHPQW- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 219 elvrerlaagaraAQSLGIdprrplqaaraakggvatllsMSREHP-GGVRDNLRSPepraaveTFLDIYS-------NP 290
Cdd:PRK11197 192 -------------AWDVGL---------------------NGRPHDlGNISAYLGKP-------TGLEDYIgwlgnnfDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 291 ALSWEHIATLRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVR 370
Cdd:PRK11197 231 SISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIR 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119705313 371 SGADLFVALALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITRELLVEG 438
Cdd:PRK11197 311 NGLDVVRMIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQG 378
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
61-432 |
2.71e-58 |
|
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).
Pssm-ID: 240087 Cd Length: 361 Bit Score: 195.05 E-value: 2.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 61 MRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPME 140
Cdd:cd04736 29 LRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPNGDLALARAAAKAGIPFVLSTASNMSIE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 141 ETAQAmAGTPFWYQLYwSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDLDLG-SLPFA-RGQGIAQYTSDPRF- 217
Cdd:cd04736 109 DVARQ-ADGDLWFQLY-VVHRELAELLVKRALAAGYTTLVLTTDVAVNGYRERDLRNGfAIPFRyTPRVLLDGILHPRWl 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 218 MELVRerlaagaraaqslGIDPRRPLQAARAAKGGVATLLSMSREhpggvrdnlrspepraavetfldiySNPALSWEHI 297
Cdd:cd04736 187 LRFLR-------------NGMPQLANFASDDAIDVEVQAALMSRQ-------------------------MDASFNWQDL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 298 ATLRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVgPEPtLLMDSGVRSGADLFV 377
Cdd:cd04736 229 RWLRDLWPHKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAAT-YKP-VLIDSGIRRGSDIVK 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1119705313 378 ALALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITR 432
Cdd:cd04736 307 ALALGANAVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
60-432 |
3.98e-58 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 194.67 E-value: 3.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 60 TMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPM 139
Cdd:PLN02535 36 TLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLAHPEGEIATARAAAACNTIMVLSFMASCTV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 140 EETAQAMAGTPFwYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDldlgslpfargqgiaqytsdprfme 219
Cdd:PLN02535 116 EEVASSCNAVRF-LQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGRREAD------------------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 220 lVRERLaagaraaqslgIDPRRplqaaRAAKGGVATLLSmsrehpggvrdnlrsPEPRAAVETFLDIYSNPALSWEHIAT 299
Cdd:PLN02535 170 -IKNKM-----------ISPQL-----KNFEGLLSTEVV---------------SDKGSGLEAFASETFDASLSWKDIEW 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 300 LRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVRSGADLFVAL 379
Cdd:PLN02535 218 LRSITNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKAL 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1119705313 380 ALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITR 432
Cdd:PLN02535 298 ALGAQAVLVGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITR 350
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
30-436 |
4.03e-48 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 168.76 E-value: 4.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 30 TRAEELEARALATMSRRAGAYIAGGAGGGATMRSNREAFDRWRVVPRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGL 109
Cdd:PLN02493 4 TNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 110 VTDDADLLIAQGAHASGVPYVFSCQGCSPMEETAQAMAGTPFwYQLYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLG 189
Cdd:PLN02493 84 AHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRF-FQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 190 WRTQDLDlgslpfargqgiAQYTSDPRFMELVRERLAAGaraaqslgidprrplQAARAAKGGVATLLSMSREHpggvrd 269
Cdd:PLN02493 163 RRESDIK------------NRFTLPPNLTLKNFEGLDLG---------------KMDEANDSGLASYVAGQIDR------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 270 nlrspepraavetfldiysnpALSWEHIATLRERTRLPVVLKGILHEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDA 349
Cdd:PLN02493 210 ---------------------TLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 350 LVRVREAVGPEPTLLMDSGVRSGADLFVALALGADACLLGRPHVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDD 429
Cdd:PLN02493 269 LEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKE 348
|
....*..
gi 1119705313 430 ITRELLV 436
Cdd:PLN02493 349 ISRNHIT 355
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
75-432 |
3.48e-42 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 152.95 E-value: 3.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 75 PRMLHATTTRDLSTTLLGTELTAPLLLAPVGAAGLVTDDADLLIAQGAHASGVPYVFSCQGCSPMEETAQAMAGTPFwYQ 154
Cdd:PLN02979 48 PRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRF-FQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 155 LYWSTDEELVDSMIGRAETAGAQALVVTLDTTMLGWRTQDLDlgslpfargqgiAQYTSDPRFMELVRERLAAGaraaqs 234
Cdd:PLN02979 127 LYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIK------------NRFTLPPNLTLKNFEGLDLG------ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 235 lgidprrplQAARAAKGGVATLLSMSREHpggvrdnlrspepraavetfldiysnpALSWEHIATLRERTRLPVVLKGIL 314
Cdd:PLN02979 189 ---------KMDEANDSGLASYVAGQIDR---------------------------TLSWKDVQWLQTITKLPILVKGVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 315 HEDDARRAFDCGVDAVVVSNHGGRQVDRSIAALDALVRVREAVGPEPTLLMDSGVRSGADLFVALALGADACLLGRPHVY 394
Cdd:PLN02979 233 TGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVF 312
|
330 340 350
....*....|....*....|....*....|....*...
gi 1119705313 395 GLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDDITR 432
Cdd:PLN02979 313 SLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISR 350
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
294-432 |
2.99e-13 |
|
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.
Pssm-ID: 239205 [Multi-domain] Cd Length: 326 Bit Score: 70.22 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 294 WEHIATLRERTRLPVVLK----GILHEDdARRAFDCGVDAVVVSNHGG---------RQVDRSIAALD-----------A 349
Cdd:cd02811 167 LERIEELVKALSVPVIVKevgfGISRET-AKRLADAGVKAIDVAGAGGtswarvenyRAKDSDQRLAEyfadwgiptaaS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 350 LVRVREAVgPEPTLLMDSGVRSGADLFVALALGADACLLGRPhVYGLALDGEAGVSAVIDNVLAELDLTMGLVGAATVDD 429
Cdd:cd02811 246 LLEVRSAL-PDLPLIASGGIRNGLDIAKALALGADLVGMAGP-FLKAALEGEEAVIETIEQIIEELRTAMFLTGAKNLAE 323
|
...
gi 1119705313 430 ITR 432
Cdd:cd02811 324 LKQ 326
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
244-391 |
4.65e-08 |
|
Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.
Pssm-ID: 396287 [Multi-domain] Cd Length: 367 Bit Score: 54.65 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 244 QAARAAKGG------VATLLSMSREHPGGVrdNLRSPEPraavetFLDIYSNPALSwEHIATLRERT-RLPVVLK---GI 313
Cdd:pfam01645 143 QGAKPGEGGhlpgekVSPEIARIRGSPPGV--GLISPPP------HHDIYSIEDLA-QLIYDLKEINpKAPISVKlvsGH 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 314 LHEDDARRAFDCGVDAVVVSNHGG-----RQVDRSIAALD---ALVRVREAV-----GPEPTLLMDSGVRSGADLFVALA 380
Cdd:pfam01645 214 GVGTIAAGVAKAGADIILIDGYDGgtgasPKTSIKHAGLPwelALAEAHQTLkenglRDRVSLIADGGLRTGADVAKAAA 293
|
170
....*....|.
gi 1119705313 381 LGADACLLGRP 391
Cdd:pfam01645 294 LGADAVYIGTA 304
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
278-390 |
3.56e-07 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 50.66 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 278 AAVETFLDIYSNPALSWEHIATLRERTR-LPVVLKGILHEDDARRAF-DCGVDAVVVSNHGGRQVDRSIAALDALVRVRE 355
Cdd:cd04722 86 DGVEIHGAVGYLAREDLELIRELREAVPdVKVVVKLSPTGELAAAAAeEAGVDEVGLGNGGGGGGGRDAVPIADLLLILA 165
|
90 100 110
....*....|....*....|....*....|....*
gi 1119705313 356 AVGPEPTLLMDSGVRSGADLFVALALGADACLLGR 390
Cdd:cd04722 166 KRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
285-390 |
9.80e-06 |
|
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.
Pssm-ID: 239202 [Multi-domain] Cd Length: 392 Bit Score: 47.54 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119705313 285 DIYSNPALSwEHIATLRERT-RLPVVLK--GILHEDDARRAFDCG-VDAVVVSNHGG-----RQVDR---SIAALDALVR 352
Cdd:cd02808 194 DIYSIEDLA-QLIEDLREATgGKPIGVKlvAGHGEGDIAAGVAAAgADFITIDGAEGgtgaaPLTFIdhvGLPTELGLAR 272
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1119705313 353 VREA-----VGPEPTLLMDSGVRSGADLFVALALGADACLLGR 390
Cdd:cd02808 273 AHQAlvkngLRDRVSLIASGGLRTGADVAKALALGADAVGIGT 315
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
317-389 |
3.67e-03 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 38.62 E-value: 3.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119705313 317 DDARRAFDCGVDAVVVSN-----HGGRQvdrsIAALDALVR-VREAVGPepTLLMDSGVRSGADLFVALALGADACLLG 389
Cdd:cd04730 113 EEARKAEAAGADALVAQGaeaggHRGTF----DIGTFALVPeVRDAVDI--PVIAAGGIADGRGIAAALALGADGVQMG 185
|
|
| |
