|
Name |
Accession |
Description |
Interval |
E-value |
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
1-379 |
0e+00 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 815.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 1 MIISASTDYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGL 80
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 81 TGMYARRGEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPV 160
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 161 PGARYRDMHSGMSGPNAAMRRVFQAMRHPSWALDVGLLGKPHDLGNISTYRGEPTKLEDYIGWLGANFDPSISWKDLEWI 240
Cdd:PRK11197 161 PGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 241 RDFWDGPMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLA 320
Cdd:PRK11197 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 491526336 321 LGADCTLLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSLVKIP 379
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQGN 379
|
|
| L_lactate_LldD |
NF033901 |
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ... |
1-377 |
0e+00 |
|
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. It occurs in E. coli, Salmonella, and as one of two L-lactate dehydrogenases in Pseudomonas aeruginosa. It is unrelated to the NAD-dependent enzyme.
Pssm-ID: 411463 Cd Length: 377 Bit Score: 780.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 1 MIISASTDYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGL 80
Cdd:NF033901 1 MIISASTDYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 81 TGMYARRGEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPV 160
Cdd:NF033901 81 TGMYARRGEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 161 PGARYRDMHSGMSGPNAAMRRVFQAMRHPSWALDVGLLGKPHDLGNISTYRGEPTKLEDYIGWLGANFDPSISWKDLEWI 240
Cdd:NF033901 161 PGARYRDAHSGMSGPNAALRRMLQAVTHPQWAWDVGLLGRPHDLGNISAYRGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 241 RDFWDGPMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLA 320
Cdd:NF033901 241 REFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 491526336 321 LGADCTLLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSLVK 377
Cdd:NF033901 321 LGADSVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRDSLVQ 377
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
3-376 |
3.20e-173 |
|
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: 486.56 E-value: 3.20e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 3 ISASTDYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTG 82
Cdd:COG1304 4 ILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 83 MYARRGEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPG 162
Cdd:COG1304 84 LAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 163 ARYRDMHSGMSGP-NAAMRRVFQAMRHPSWALdvgllgkphdlgnistyrgeptKLEDYIGWLGANFDPSISWKDLEWIR 241
Cdd:COG1304 164 RRERDLREGFSQPpRLTPRNLLEAATHPRWAL----------------------GLASLAAWLDTNFDPSLTWDDIAWLR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 242 DFWDGPMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLAL 321
Cdd:COG1304 222 ERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALAL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 491526336 322 GADCTLLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSLV 376
Cdd:COG1304 302 GADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
13-377 |
5.06e-161 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 455.45 E-value: 5.06e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 13 AKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTGMYARRGEVQA 92
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 93 AKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPGARYRDMHSGM 172
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 173 S-GPNAAMRRVFQAMRHPSWALDVGLLGKPHDLGnistyrgeptkledyiGWLGANFDPSISWKDLEWIRDFWDGPMVIK 251
Cdd:pfam01070 161 TlPPRLTPRNLLDLALHPRWALGVLRRGGAGGAA----------------AFVGSQFDPALTWDDLAWLRERWKGPLVVK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 252 GILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLALGADCTLLGRS 331
Cdd:pfam01070 225 GILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRP 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 491526336 332 FVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSLVK 377
Cdd:pfam01070 305 FLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
8-372 |
6.61e-152 |
|
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: 430.33 E-value: 6.61e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 8 DYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTGMYARR 87
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 88 GEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPGARyrd 167
Cdd:cd02809 82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 168 mhsgmsgpnaamrrvfqamrhpswaldvgllgkphdlgnistyrgeptkledyigwlganfdpsISWKDLEWIRDFWDGP 247
Cdd:cd02809 159 ----------------------------------------------------------------LTWDDLAWLRSQWKGP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 248 MVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLALGADCTL 327
Cdd:cd02809 175 LILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVL 254
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 491526336 328 LGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSR 372
Cdd:cd02809 255 IGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
1-379 |
0e+00 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 815.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 1 MIISASTDYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGL 80
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 81 TGMYARRGEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPV 160
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 161 PGARYRDMHSGMSGPNAAMRRVFQAMRHPSWALDVGLLGKPHDLGNISTYRGEPTKLEDYIGWLGANFDPSISWKDLEWI 240
Cdd:PRK11197 161 PGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 241 RDFWDGPMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLA 320
Cdd:PRK11197 241 RDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 491526336 321 LGADCTLLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSLVKIP 379
Cdd:PRK11197 321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQGN 379
|
|
| L_lactate_LldD |
NF033901 |
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ... |
1-377 |
0e+00 |
|
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. It occurs in E. coli, Salmonella, and as one of two L-lactate dehydrogenases in Pseudomonas aeruginosa. It is unrelated to the NAD-dependent enzyme.
Pssm-ID: 411463 Cd Length: 377 Bit Score: 780.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 1 MIISASTDYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGL 80
Cdd:NF033901 1 MIISASTDYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 81 TGMYARRGEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPV 160
Cdd:NF033901 81 TGMYARRGEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 161 PGARYRDMHSGMSGPNAAMRRVFQAMRHPSWALDVGLLGKPHDLGNISTYRGEPTKLEDYIGWLGANFDPSISWKDLEWI 240
Cdd:NF033901 161 PGARYRDAHSGMSGPNAALRRMLQAVTHPQWAWDVGLLGRPHDLGNISAYRGKPTGLEDYIGWLGNNFDPSISWKDLEWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 241 RDFWDGPMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLA 320
Cdd:NF033901 241 REFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 491526336 321 LGADCTLLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSLVK 377
Cdd:NF033901 321 LGADSVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRDSLVQ 377
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
3-376 |
3.20e-173 |
|
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: 486.56 E-value: 3.20e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 3 ISASTDYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTG 82
Cdd:COG1304 4 ILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 83 MYARRGEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPG 162
Cdd:COG1304 84 LAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 163 ARYRDMHSGMSGP-NAAMRRVFQAMRHPSWALdvgllgkphdlgnistyrgeptKLEDYIGWLGANFDPSISWKDLEWIR 241
Cdd:COG1304 164 RRERDLREGFSQPpRLTPRNLLEAATHPRWAL----------------------GLASLAAWLDTNFDPSLTWDDIAWLR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 242 DFWDGPMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLAL 321
Cdd:COG1304 222 ERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALAL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 491526336 322 GADCTLLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSLV 376
Cdd:COG1304 302 GADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
13-377 |
5.06e-161 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 455.45 E-value: 5.06e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 13 AKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTGMYARRGEVQA 92
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 93 AKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPGARYRDMHSGM 172
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 173 S-GPNAAMRRVFQAMRHPSWALDVGLLGKPHDLGnistyrgeptkledyiGWLGANFDPSISWKDLEWIRDFWDGPMVIK 251
Cdd:pfam01070 161 TlPPRLTPRNLLDLALHPRWALGVLRRGGAGGAA----------------AFVGSQFDPALTWDDLAWLRERWKGPLVVK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 252 GILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLALGADCTLLGRS 331
Cdd:pfam01070 225 GILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRP 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 491526336 332 FVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSLVK 377
Cdd:pfam01070 305 FLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
8-372 |
6.61e-152 |
|
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: 430.33 E-value: 6.61e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 8 DYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTGMYARR 87
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 88 GEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPGARyrd 167
Cdd:cd02809 82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 168 mhsgmsgpnaamrrvfqamrhpswaldvgllgkphdlgnistyrgeptkledyigwlganfdpsISWKDLEWIRDFWDGP 247
Cdd:cd02809 159 ----------------------------------------------------------------LTWDDLAWLRSQWKGP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 248 MVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLALGADCTL 327
Cdd:cd02809 175 LILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVL 254
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 491526336 328 LGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSR 372
Cdd:cd02809 255 IGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
8-375 |
2.22e-104 |
|
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: 312.68 E-value: 2.22e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 8 DYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTGMYARR 87
Cdd:cd03332 23 RLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFHPD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 88 GEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAI-ERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPGARYR 166
Cdd:cd03332 103 AELATARAAAELGVPYILSTASSSSIEDVAAAAgDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRPR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 167 DMHSG-------------MSGPnaamrrVFQAMrhpswaldvglLGKPHDLGNISTYRGEPTKLEdyigWLGANFDPSIS 233
Cdd:cd03332 183 DLDLGylpflrgigianyFSDP------VFRKK-----------LAEPVGEDPEAPPPMEAAVAR----FVSVFSGPSLT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 234 WKDLEWIRDFWDGPMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGL 313
Cdd:cd03332 242 WEDLAFLREWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491526336 314 DVVRMLALGADCTLLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSL 375
Cdd:cd03332 322 DIMKALALGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
8-372 |
6.83e-97 |
|
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: 292.89 E-value: 6.83e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 8 DYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTGMYARR 87
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 88 GEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKdRGFMKNVLERAKAAGVTTLVFTVDMPVPGARYRD 167
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRERD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 168 MHSGMSGP-NAAMRRVFQAMRHPSWALDVGLLGKPHdLGNISTyrGEPTKLEDYIGWLGANFDPSISWKDLEWIRDFWDG 246
Cdd:cd04736 161 LRNGFAIPfRYTPRVLLDGILHPRWLLRFLRNGMPQ-LANFAS--DDAIDVEVQAALMSRQMDASFNWQDLRWLRDLWPH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 247 PMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLkiFVDSGIRTGLDVVRMLALGADCT 326
Cdd:cd04736 238 KLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYKPV--LIDSGIRRGSDIVKALALGANAV 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 491526336 327 LLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSR 372
Cdd:cd04736 316 LLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
8-375 |
1.83e-88 |
|
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: 270.85 E-value: 1.83e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 8 DYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTGMYARR 87
Cdd:cd04737 10 DLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLAHAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 88 GEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIER-PMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPGARYR 166
Cdd:cd04737 90 GEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGgPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGGNREA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 167 DMhsgmsgpnaAMRRVFqamrhpswaldvgllgkPHDLGNISTYrGEPTKLEDYIGWLGANFDPSISWKDLEWIRDFWDG 246
Cdd:cd04737 170 DI---------RNKFQF-----------------PFGMPNLNHF-SEGTGKGKGISEIYAAAKQKLSPADIEFIAKISGL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 247 PMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLALGADCT 326
Cdd:cd04737 223 PVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAV 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 491526336 327 LLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSL 375
Cdd:cd04737 303 AVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKRTFL 351
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
8-370 |
3.61e-88 |
|
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: 269.85 E-value: 3.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 8 DYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTGMYARR 87
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 88 GEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIE--RPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPGARY 165
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPpdQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 166 RDMHSGMSGpnaamrrvfqamrhpswALDVGLLGKPHDLGNISTYRGeptkledyigwLGANFDPSISWKDLEWIRDFWD 245
Cdd:cd02922 162 RDERLKAEE-----------------AVSDGPAGKKTKAKGGGAGRA-----------MSGFIDPTLTWDDIKWLRKHTK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 246 GPMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSI---ADAVKGDLKIFVDSGIRTGLDVVRMLALG 322
Cdd:cd02922 214 LPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIrkhCPEVFDKIEVYVDGGVRRGTDVLKALCLG 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 491526336 323 ADCTLLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADL 370
Cdd:cd02922 294 AKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLGVTSLDQL 341
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
1-376 |
2.91e-76 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 240.02 E-value: 2.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 1 MIISASTDYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGL 80
Cdd:PLN02493 1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 81 TGMYARRGEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPV 160
Cdd:PLN02493 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 161 PGARYRDMHSGMSGPNAAMRRVFQAmrhpswaLDVGLLGKPHDLGNIStyrgeptkledyigWLGANFDPSISWKDLEWI 240
Cdd:PLN02493 161 LGRRESDIKNRFTLPPNLTLKNFEG-------LDLGKMDEANDSGLAS--------------YVAGQIDRTLSWKDVQWL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 241 RDFWDGPMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLA 320
Cdd:PLN02493 220 QTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALA 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 491526336 321 LGADCTLLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSRDSLV 376
Cdd:PLN02493 300 LGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHIT 355
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
8-372 |
2.00e-74 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 235.12 E-value: 2.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 8 DYRAAAKAKLPPFLFHYIDGGSYDERTLKRNTDDLGDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTGMYARR 87
Cdd:PLN02535 10 EFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLAHPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 88 GEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIERPMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPGARYRD 167
Cdd:PLN02535 90 GEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGRREAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 168 MHSGMSGPNaamRRVFQAMRHPSWALDVGllgkphdlGNISTYRGEptkledyigwlgaNFDPSISWKDLEWIRDFWDGP 247
Cdd:PLN02535 170 IKNKMISPQ---LKNFEGLLSTEVVSDKG--------SGLEAFASE-------------TFDASLSWKDIEWLRSITNLP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 248 MVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLALGADCTL 327
Cdd:PLN02535 226 ILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 491526336 328 LGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLTGAKSIADLSR 372
Cdd:PLN02535 306 VGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITR 350
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
43-375 |
2.81e-62 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 203.80 E-value: 2.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 43 GDVALRQRVLRDMTDLSLETEIFGEKLAMPIALAPVGLTGMYARRGEVQAAKAAEKKGIPFTMSTVSVCPIEEVAPAIER 122
Cdd:PLN02979 42 GFCDFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 123 PMWFQLYVLKDRGFMKNVLERAKAAGVTTLVFTVDMPVPGARYRDMHSGMSGPNAAMRRVFQAmrhpswaLDVGLLGKPH 202
Cdd:PLN02979 122 IRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEG-------LDLGKMDEAN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 203 DLGNISTYRGEptkledyigwlganFDPSISWKDLEWIRDFWDGPMVIKGILDEEDAKDAVRFGADGIVVSNHGGRQLDG 282
Cdd:PLN02979 195 DSGLASYVAGQ--------------IDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 283 VLSSAKALPSIADAVKGDLKIFVDSGIRTGLDVVRMLALGADCTLLGRSFVYALAAQGGAGVENLLDLYDKEMRVAMTLT 362
Cdd:PLN02979 261 VPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALS 340
|
330
....*....|...
gi 491526336 363 GAKSIADLSRDSL 375
Cdd:PLN02979 341 GCRSLKEISRNHI 353
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
219-372 |
4.73e-15 |
|
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: 75.23 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 219 DYIGWLGAnfdpsiswkdLEWIRDFWDGPMVIK----GIlDEEDAKDAVRFGADGIVVSNHGG---------RQLDGV-- 283
Cdd:cd02811 162 DFRGWLER----------IEELVKALSVPVIVKevgfGI-SRETAKRLADAGVKAIDVAGAGGtswarvenyRAKDSDqr 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 284 ---------LSSAKALPSIADAVKgDLKIFVDSGIRTGLDVVRMLALGADCTLLGRSFVYAlAAQGGAGVENLLDLYDKE 354
Cdd:cd02811 231 laeyfadwgIPTAASLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKA-ALEGEEAVIETIEQIIEE 308
|
170
....*....|....*...
gi 491526336 355 MRVAMTLTGAKSIADLSR 372
Cdd:cd02811 309 LRTAMFLTGAKNLAELKQ 326
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
234-330 |
2.27e-08 |
|
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: 53.74 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 234 WKDLEWIRDFW-DGPMVIKGI-LDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAKALPSIADAVKGDLKIFVDSGIRT 311
Cdd:cd04722 102 LELIRELREAVpDVKVVVKLSpTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGIND 181
|
90
....*....|....*....
gi 491526336 312 GLDVVRMLALGADCTLLGR 330
Cdd:cd04722 182 PEDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
297-377 |
1.40e-05 |
|
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: 46.77 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 297 VKGDLKIFVDSGIRTGLDVVRMLALGADCTLLGRSFVYAL-----------------AAQ------------GGAGVENL 347
Cdd:cd02808 282 LRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALgciqarkchtntcpvgvATQdpelrrrldvegKAERVANY 361
|
90 100 110
....*....|....*....|....*....|
gi 491526336 348 LDLYDKEMRVAMTLTGAKSIADLSRDSLVK 377
Cdd:cd02808 362 LKSLAEELRELAAALGKRSLELLGRSDLLA 391
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
223-324 |
3.14e-04 |
|
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: 41.70 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 223 WLGANFDPSIswkdLEWIRDFwdGPMVIKGILDEEDAKDAVRFGADGIVVSN-----HGGRQLDGVLSSakaLPSIADAV 297
Cdd:cd04730 85 SFSFGPPAEV----VERLKAA--GIKVIPTVTSVEEARKAEAAGADALVAQGaeaggHRGTFDIGTFAL---VPEVRDAV 155
|
90 100
....*....|....*....|....*..
gi 491526336 298 kgDLKIFVDSGIRTGLDVVRMLALGAD 324
Cdd:cd04730 156 --DIPVIAAGGIADGRGIAAALALGAD 180
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
237-329 |
4.74e-04 |
|
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 41.57 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 237 LEWIRDFWDGPMVIK--GILDEED----AKDAVRFGADGIVVSNH-------------GGRQLDGVLSSAKALP------ 291
Cdd:cd02810 154 LKAVKAAVDIPLLVKlsPYFDLEDivelAKAAERAGADGLTAINTisgrvvdlktvgpGPKRGTGGLSGAPIRPlalrwv 233
|
90 100 110
....*....|....*....|....*....|....*....
gi 491526336 292 -SIADAVKGDLKIFVDSGIRTGLDVVRMLALGADCTLLG 329
Cdd:cd02810 234 aRLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVA 272
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
244-336 |
4.93e-04 |
|
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: 41.93 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 244 WDGPMVIK---GILDEEDAKDAVRFGADGIVVSNHGGRQLDGVLSSAK--ALP---SIADAVKG--------DLKIFVDS 307
Cdd:pfam01645 201 PKAPISVKlvsGHGVGTIAAGVAKAGADIILIDGYDGGTGASPKTSIKhaGLPwelALAEAHQTlkenglrdRVSLIADG 280
|
90 100
....*....|....*....|....*....
gi 491526336 308 GIRTGLDVVRMLALGADCTLLGRSFVYAL 336
Cdd:pfam01645 281 GLRTGADVAKAAALGADAVYIGTAALIAL 309
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
302-336 |
1.13e-03 |
|
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439839 Cd Length: 728 Bit Score: 41.00 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|....*
gi 491526336 302 KIFVDSGIRTGLDVVRMLALGADCTLLGRSFVYAL 336
Cdd:COG0069 442 RLIADGKLKTGRDVAIAAALGADEFGFARAFMVAL 476
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
237-332 |
8.33e-03 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 37.88 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 237 LEWIRD-FWDGPMVIKGILDEEDAKDAVRFGADGIVV-----SNHGGRQLDGV-LSSAKALPSIADAVKG-DLKIFVDSG 308
Cdd:cd00381 126 IKFIKKkYPNVDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTRIVTGVgVPQATAVADVAAAARDyGVPVIADGG 205
|
90 100
....*....|....*....|....
gi 491526336 309 IRTGLDVVRMLALGADCTLLGRSF 332
Cdd:cd00381 206 IRTSGDIVKALAAGADAVMLGSLL 229
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
249-332 |
8.48e-03 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 38.03 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491526336 249 VIKG-ILDEEDAKDAVRFGADGI-------------VVSNHGGRQLDGVLSSAK-----ALPSIADAvkgdlkifvdsGI 309
Cdd:PTZ00314 285 IIAGnVVTADQAKNLIDAGADGLrigmgsgsicitqEVCAVGRPQASAVYHVARyarerGVPCIADG-----------GI 353
|
90 100
....*....|....*....|...
gi 491526336 310 RTGLDVVRMLALGADCTLLGRSF 332
Cdd:PTZ00314 354 KNSGDICKALALGADCVMLGSLL 376
|
|
| |
