|
Name |
Accession |
Description |
Interval |
E-value |
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
8-385 |
0e+00 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 689.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 8 AASVLDYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAG 87
Cdd:PRK11197 3 ISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 88 MNARRGEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPG 167
Cdd:PRK11197 83 MYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 168 SRYRDYHSGLAGAAGtvgAIRRLGQAMRHPRWAWDVGLLGRPHQLGNIAPVLGKNTGLEDFFAWMRTNFDPGVTWRDLDF 247
Cdd:PRK11197 163 ARYRDAHSGMSGPNA---AMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 248 IRDIWDGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRML 327
Cdd:PRK11197 240 IRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMI 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 502804773 328 ALGAKGVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHILVD 385
Cdd:PRK11197 320 ALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQ 377
|
|
| L_lactate_LldD |
NF033901 |
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ... |
13-384 |
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: 572.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 13 DYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMNARR 92
Cdd:NF033901 8 DYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGLTGMYARR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 93 GEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSRYRD 172
Cdd:NF033901 88 GEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPTPGARYRD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 173 YHSGLAGAAGtvgAIRRLGQAMRHPRWAWDVGLLGRPHQLGNIAPVLGKNTGLEDFFAWMRTNFDPGVTWRDLDFIRDIW 252
Cdd:NF033901 168 AHSGMSGPNA---ALRRMLQAVTHPQWAWDVGLLGRPHDLGNISAYRGKPTGLEDYIGWLGNNFDPSISWKDLEWIREFW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 253 DGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRMLALGAK 332
Cdd:NF033901 245 DGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIALGAD 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 502804773 333 GVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHILV 384
Cdd:NF033901 325 SVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRDSLV 376
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
7-384 |
2.13e-162 |
|
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: 459.60 E-value: 2.13e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 7 KAASVLDYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLA 86
Cdd:COG1304 3 RILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 87 GMNARRGEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVP 166
Cdd:COG1304 83 GLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 167 GSRYRDYHSGLAGAAGtvGAIRRLGQAMRHPRWAWdvgllgrphqlgniapvlgkntGLEDFFAWMRTNFDPGVTWRDLD 246
Cdd:COG1304 163 GRRERDLREGFSQPPR--LTPRNLLEAATHPRWAL----------------------GLASLAAWLDTNFDPSLTWDDIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 247 FIRDIWDGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRM 326
Cdd:COG1304 219 WLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKA 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 502804773 327 LALGAKGVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHILV 384
Cdd:COG1304 299 LALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
18-384 |
4.93e-151 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 430.41 E-value: 4.93e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 18 ARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMNARRGEVQA 97
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 98 ARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSRYRDYHSGL 177
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 178 AGAAGTvgAIRRLGQAMRHPRWAWDVGLLGRPHQLGniapvlgkntgledffAWMRTNFDPGVTWRDLDFIRDIWDGPLI 257
Cdd:pfam01070 161 TLPPRL--TPRNLLDLALHPRWALGVLRRGGAGGAA----------------AFVGSQFDPALTWDDLAWLRERWKGPLV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 258 IKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRMLALGAKGVLLG 337
Cdd:pfam01070 223 VKGILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLG 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 502804773 338 RAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHILV 384
Cdd:pfam01070 303 RPFLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
13-380 |
8.11e-141 |
|
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: 402.60 E-value: 8.11e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 13 DYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMNARR 92
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 93 GEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSRyrd 172
Cdd:cd02809 82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 173 yhsglagaagtvgairrlgqamrhprwawdvgllgrphqlgniapvlgkntgledffawmrtnfdpgVTWRDLDFIRDIW 252
Cdd:cd02809 159 -------------------------------------------------------------------LTWDDLAWLRSQW 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 253 DGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRMLALGAK 332
Cdd:cd02809 172 KGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGAD 251
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 502804773 333 GVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGR 380
Cdd:cd02809 252 AVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
8-385 |
0e+00 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 689.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 8 AASVLDYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAG 87
Cdd:PRK11197 3 ISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 88 MNARRGEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPG 167
Cdd:PRK11197 83 MYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 168 SRYRDYHSGLAGAAGtvgAIRRLGQAMRHPRWAWDVGLLGRPHQLGNIAPVLGKNTGLEDFFAWMRTNFDPGVTWRDLDF 247
Cdd:PRK11197 163 ARYRDAHSGMSGPNA---AMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 248 IRDIWDGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRML 327
Cdd:PRK11197 240 IRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMI 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 502804773 328 ALGAKGVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHILVD 385
Cdd:PRK11197 320 ALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQ 377
|
|
| L_lactate_LldD |
NF033901 |
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ... |
13-384 |
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: 572.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 13 DYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMNARR 92
Cdd:NF033901 8 DYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGLTGMYARR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 93 GEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSRYRD 172
Cdd:NF033901 88 GEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPTPGARYRD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 173 YHSGLAGAAGtvgAIRRLGQAMRHPRWAWDVGLLGRPHQLGNIAPVLGKNTGLEDFFAWMRTNFDPGVTWRDLDFIRDIW 252
Cdd:NF033901 168 AHSGMSGPNA---ALRRMLQAVTHPQWAWDVGLLGRPHDLGNISAYRGKPTGLEDYIGWLGNNFDPSISWKDLEWIREFW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 253 DGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRMLALGAK 332
Cdd:NF033901 245 DGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIALGAD 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 502804773 333 GVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHILV 384
Cdd:NF033901 325 SVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRDSLV 376
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
7-384 |
2.13e-162 |
|
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: 459.60 E-value: 2.13e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 7 KAASVLDYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLA 86
Cdd:COG1304 3 RILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 87 GMNARRGEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVP 166
Cdd:COG1304 83 GLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 167 GSRYRDYHSGLAGAAGtvGAIRRLGQAMRHPRWAWdvgllgrphqlgniapvlgkntGLEDFFAWMRTNFDPGVTWRDLD 246
Cdd:COG1304 163 GRRERDLREGFSQPPR--LTPRNLLEAATHPRWAL----------------------GLASLAAWLDTNFDPSLTWDDIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 247 FIRDIWDGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRM 326
Cdd:COG1304 219 WLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKA 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 502804773 327 LALGAKGVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHILV 384
Cdd:COG1304 299 LALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
18-384 |
4.93e-151 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 430.41 E-value: 4.93e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 18 ARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMNARRGEVQA 97
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 98 ARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSRYRDYHSGL 177
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 178 AGAAGTvgAIRRLGQAMRHPRWAWDVGLLGRPHQLGniapvlgkntgledffAWMRTNFDPGVTWRDLDFIRDIWDGPLI 257
Cdd:pfam01070 161 TLPPRL--TPRNLLDLALHPRWALGVLRRGGAGGAA----------------AFVGSQFDPALTWDDLAWLRERWKGPLV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 258 IKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRMLALGAKGVLLG 337
Cdd:pfam01070 223 VKGILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLG 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 502804773 338 RAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHILV 384
Cdd:pfam01070 303 RPFLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
13-380 |
8.11e-141 |
|
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: 402.60 E-value: 8.11e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 13 DYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMNARR 92
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 93 GEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSRyrd 172
Cdd:cd02809 82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 173 yhsglagaagtvgairrlgqamrhprwawdvgllgrphqlgniapvlgkntgledffawmrtnfdpgVTWRDLDFIRDIW 252
Cdd:cd02809 159 -------------------------------------------------------------------LTWDDLAWLRSQW 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 253 DGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRMLALGAK 332
Cdd:cd02809 172 KGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGAD 251
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 502804773 333 GVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGR 380
Cdd:cd02809 252 AVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
13-383 |
1.89e-98 |
|
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: 297.66 E-value: 1.89e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 13 DYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMNARR 92
Cdd:cd03332 23 RLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFHPD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 93 GEVQAARAAEAAGIPFCLSTVSACPLDEVAAGV-NAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSRYR 171
Cdd:cd03332 103 AELATARAAAELGVPYILSTASSSSIEDVAAAAgDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRPR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 172 DYHSG----LAGaagtvgaiRRLGQAMRHPRWawdVGLLGRPHqlGNIAPVLGKNTGLEDFFAwmRTNFDPGVTWRDLDF 247
Cdd:cd03332 183 DLDLGylpfLRG--------IGIANYFSDPVF---RKKLAEPV--GEDPEAPPPMEAAVARFV--SVFSGPSLTWEDLAF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 248 IRDIWDGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRML 327
Cdd:cd03332 248 LREWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKAL 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 502804773 328 ALGAKGVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHIL 383
Cdd:cd03332 328 ALGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
13-380 |
4.52e-93 |
|
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: 283.26 E-value: 4.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 13 DYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMNARR 92
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 93 GEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRdRGFMRALLQKAKALGCSALIFTVDMPVPGSRYRD 172
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRERD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 173 YHSGLAGAAGTvgAIRRLGQAMRHPRWAWDVGLLGRPhQLGNIAPVlgKNTGLEDFFAWMRTNFDPGVTWRDLDFIRDIW 252
Cdd:cd04736 161 LRNGFAIPFRY--TPRVLLDGILHPRWLLRFLRNGMP-QLANFASD--DAIDVEVQAALMSRQMDASFNWQDLRWLRDLW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 253 DGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVddRLTVLVDGGVRSGLDVVRMLALGAK 332
Cdd:cd04736 236 PHKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAAT--YKPVLIDSGIRRGSDIVKALALGAN 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 502804773 333 GVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGR 380
Cdd:cd04736 314 AVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
13-381 |
5.03e-85 |
|
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: 262.15 E-value: 5.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 13 DYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMNARR 92
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 93 GEVQAARAAEAAGIPFCLSTVSACPLDEVAAGV--NAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSRY 170
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARppDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 171 RDYHSGLAGAAGTVGAIRRlgqamrhprWAWDVGLLGRPhqlgniapvlgkntgledffawMRTNFDPGVTWRDLDFIRD 250
Cdd:cd02922 162 RDERLKAEEAVSDGPAGKK---------TKAKGGGAGRA----------------------MSGFIDPTLTWDDIKWLRK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 251 IWDGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALP---PIADAVDDRLTVLVDGGVRSGLDVVRML 327
Cdd:cd02922 211 HTKLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLeirKHCPEVFDKIEVYVDGGVRRGTDVLKAL 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 502804773 328 ALGAKGVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRH 381
Cdd:cd02922 291 CLGAKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLGVTSLDQLGPS 344
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
10-375 |
3.37e-80 |
|
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: 250.05 E-value: 3.37e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 10 SVLDYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMN 89
Cdd:cd04737 7 NLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 90 ARRGEVQAARAAEAAGIPFCLSTVSACPLDEVA-AGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGS 168
Cdd:cd04737 87 HATGEVATARGMAEVGSLFSISTYSNTSLEEIAkASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGGN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 169 RYRDYHSGLAgaagtvgairrlgqamrhprwawdvgllgRPHQLGNIA-PVLGKNTGLEDFFAWmrTNFDPGVTWRDLDF 247
Cdd:cd04737 167 READIRNKFQ-----------------------------FPFGMPNLNhFSEGTGKGKGISEIY--AAAKQKLSPADIEF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 248 IRDIWDGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRML 327
Cdd:cd04737 216 IAKISGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKAL 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 502804773 328 ALGAKGVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDI 375
Cdd:cd04737 296 ASGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTI 343
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
10-380 |
5.56e-74 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 234.34 E-value: 5.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 10 SVLDYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMN 89
Cdd:PLN02535 7 NVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 90 ARRGEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSR 169
Cdd:PLN02535 87 HPEGEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGRR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 170 YRDyhsglagaagtvgairrLGQAMRHPRWAWDVGLLgrphqlgNIAPVLGKNTGLEdffAWMRTNFDPGVTWRDLDFIR 249
Cdd:PLN02535 167 EAD-----------------IKNKMISPQLKNFEGLL-------STEVVSDKGSGLE---AFASETFDASLSWKDIEWLR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 250 DIWDGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRMLAL 329
Cdd:PLN02535 220 SITNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALAL 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502804773 330 GAKGVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGR 380
Cdd:PLN02535 300 GAQAVLVGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITR 350
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
10-386 |
1.61e-65 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 212.67 E-value: 1.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 10 SVLDYRELARRRLPPFLFEYIDGGSYAEVTLERNLADLAGTALRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMN 89
Cdd:PLN02493 5 NVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 90 ARRGEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWFQLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSR 169
Cdd:PLN02493 85 HPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 170 YRDYHSGLAGAAG-TVGAIRRLgqamrhprwawDVGLLGRPHQLGNIAPVLGKntgledffawmrtnFDPGVTWRDLDFI 248
Cdd:PLN02493 165 ESDIKNRFTLPPNlTLKNFEGL-----------DLGKMDEANDSGLASYVAGQ--------------IDRTLSWKDVQWL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 249 RDIWDGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRMLA 328
Cdd:PLN02493 220 QTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALA 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 502804773 329 LGAKGVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHILVDD 386
Cdd:PLN02493 300 LGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHITTE 357
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
52-381 |
1.24e-56 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 189.55 E-value: 1.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 52 LRQRVLTDVSQLDLTTTLFGQKLGLPVALAPIGLAGMNARRGEVQAARAAEAAGIPFCLSTVSACPLDEVAAGVNAPFWF 131
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 132 QLYMIRDRGFMRALLQKAKALGCSALIFTVDMPVPGSRYRDYHSGLAGAAG-TVGAIRRLgqamrhprwawDVGLLGRPH 210
Cdd:PLN02979 126 QLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNlTLKNFEGL-----------DLGKMDEAN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 211 QLGNIAPVLGKntgledffawmrtnFDPGVTWRDLDFIRDIWDGPLIIKGVLDSEDAQMAVRVGADGIVVSNHGGRQLDG 290
Cdd:PLN02979 195 DSGLASYVAGQ--------------IDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 291 VPSTARALPPIADAVDDRLTVLVDGGVRSGLDVVRMLALGAKGVLLGRAWVYALAAGGQAGVAHVLRLIEAEMRVAMALT 370
Cdd:PLN02979 261 VPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALS 340
|
330
....*....|.
gi 502804773 371 GSRDIGAIGRH 381
Cdd:PLN02979 341 GCRSLKEISRN 351
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
245-377 |
5.18e-16 |
|
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: 78.31 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 245 LDFIRDI---WDGPLIIKGV---LDSEDAQMAVRVGADGIVVSNHGG---------RQLD------------GVPsTARA 297
Cdd:cd02811 167 LERIEELvkaLSVPVIVKEVgfgISRETAKRLADAGVKAIDVAGAGGtswarvenyRAKDsdqrlaeyfadwGIP-TAAS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 298 LPPIADAVDDrLTVLVDGGVRSGLDVVRMLALGAKGVLLGRAWVYALAAGGQAGVAHvLRLIEAEMRVAMALTGSRDIGA 377
Cdd:cd02811 246 LLEVRSALPD-LPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAALEGEEAVIET-IEQIIEELRTAMFLTGAKNLAE 323
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
238-338 |
3.54e-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: 50.28 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 238 PGVTWRDLDFIRDIW-DGPLIIKGVLDSEDAQMAVRV-GADGIVVSNHGGRQLDGVPSTARALPPIADAVDDRLTVLVDG 315
Cdd:cd04722 98 AREDLELIRELREAVpDVKVVVKLSPTGELAAAAAEEaGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGG 177
|
90 100
....*....|....*....|...
gi 502804773 316 GVRSGLDVVRMLALGAKGVLLGR 338
Cdd:cd04722 178 GINDPEDAAEALALGADGVIVGS 200
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
254-341 |
9.06e-07 |
|
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: 49.40 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 254 GPLIIKGVLDSEDAQMAVRVGADGIVVSNH--GGRQLDGVPSTARALPPIADAVDdrLTVLVDGGVRSGLDVVRMLALGA 331
Cdd:cd04730 102 GIKVIPTVTSVEEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGA 179
|
90
....*....|
gi 502804773 332 KGVLLGRAWV 341
Cdd:cd04730 180 DGVQMGTRFL 189
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
267-384 |
1.14e-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: 50.23 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 267 AQMAVRVGADGIVVSNHGG-------RQLD--GVPSTArALPPIADAVD-----DRLTVLVDGGVRSGLDVVRMLALGAK 332
Cdd:cd02808 231 AAGVAAAGADFITIDGAEGgtgaaplTFIDhvGLPTEL-GLARAHQALVknglrDRVSLIASGGLRTGADVAKALALGAD 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 333 GVLLGRAWVYALAA-----------------------------GGQAGVAHVLRLIEAEMRVAMALTGSRDIGAIGRHIL 383
Cdd:cd02808 310 AVGIGTAALIALGCiqarkchtntcpvgvatqdpelrrrldveGKAERVANYLKSLAEELRELAAALGKRSLELLGRSDL 389
|
.
gi 502804773 384 V 384
Cdd:cd02808 390 L 390
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
265-337 |
5.90e-06 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 47.41 E-value: 5.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502804773 265 EDAQMAVRVGADGIVVSNH--GG-RQLDGVPSTARaLPPIADAVDdrLTVLVDGGVRSGLDVVRMLALGAKGVLLG 337
Cdd:COG2070 115 REARKAEKAGADAVVAEGAeaGGhRGADEVSTFAL-VPEVRDAVD--IPVIAAGGIADGRGIAAALALGADGVQMG 187
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
254-362 |
1.02e-04 |
|
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.
Pssm-ID: 367316 [Multi-domain] Cd Length: 331 Bit Score: 44.04 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 254 GPLIIKGVLDSEDAQMAVRVGADGIVVSN-----HGGRQLDGVPSTARALPPIADAVDdrLTVLVDGGVRSGLDVVRMLA 328
Cdd:pfam03060 136 GVALIPTISSAKEARIAEARGADALIVQGpeaggHQGTPEYGDKGLFRLVPQVPDAVD--IPVIAAGGIWDRRGVAAALA 213
|
90 100 110
....*....|....*....|....*....|....
gi 502804773 329 LGAKGVLLGRAWVYALAAGgqAGVAHVLRLIEAE 362
Cdd:pfam03060 214 LGASGVQMGTRFLLTKESG--AHDAHKQKITEAG 245
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
270-344 |
1.33e-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: 43.47 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502804773 270 AVRVGADGIVVSNHGG---------RQLDGVPSTArALPP-----IADAVDDRLTVLVDGGVRSGLDVVRMLALGAKGVL 335
Cdd:pfam01645 222 VAKAGADIILIDGYDGgtgaspktsIKHAGLPWEL-ALAEahqtlKENGLRDRVSLIADGGLRTGADVAKAAALGADAVY 300
|
....*....
gi 502804773 336 LGRAWVYAL 344
Cdd:pfam01645 301 IGTAALIAL 309
|
|
| |
