|
Name |
Accession |
Description |
Interval |
E-value |
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
1-378 |
0e+00 |
|
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: 536.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 1 MSDILTIADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTG 80
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 81 LTGMQHADGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQ 160
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 161 ILGQRHKDVRNGLSAPPKMTLANIIDLASKPRWCLGIAgtkrrtfrnivghakgvgdvsSLSSWTNEQFDPQLSWKDVAW 240
Cdd:COG1304 161 VLGRRERDLREGFSQPPRLTPRNLLEAATHPRWALGLA---------------------SLAAWLDTNFDPSLTWDDIAW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 241 IKERWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKAL 320
Cdd:COG1304 220 LRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKAL 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 499216877 321 CLGAKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQLRR 378
Cdd:COG1304 300 ALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
14-378 |
9.29e-179 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 500.14 E-value: 9.29e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 14 ARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTGMQHADGEMLA 93
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 94 AKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILGQRHKDVRNGL 173
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 174 SAPPKMTLANIIDLASKPRWCLGIAGTkrrtfrnivghakgvGDVSSLSSWTNEQFDPQLSWKDVAWIKERWGGKLILKG 253
Cdd:pfam01070 161 TLPPRLTPRNLLDLALHPRWALGVLRR---------------GGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 254 ILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKALCLGAKGTYIGRPF 333
Cdd:pfam01070 226 ILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPF 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 499216877 334 LYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQLRR 378
Cdd:pfam01070 306 LYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
8-373 |
9.05e-158 |
|
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: 444.97 E-value: 9.05e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 8 ADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTGMQHA 87
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 88 DGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILGQRhk 167
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 168 dvrnglsappkmtlaniidlaskprwclgiagtkrrtfrnivghakgvgdvsslsswtneqfdpqLSWKDVAWIKERWGG 247
Cdd:cd02809 159 -----------------------------------------------------------------LTWDDLAWLRSQWKG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 248 KLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKALCLGAKGT 327
Cdd:cd02809 174 PLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAV 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499216877 328 YIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGK 373
Cdd:cd02809 254 LIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
4-376 |
1.28e-150 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 430.21 E-value: 1.28e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 4 ILTIADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTG 83
Cdd:PRK11197 3 ISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 84 MQHADGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILG 163
Cdd:PRK11197 83 MYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 164 QRHKDVRNGLSAPPKmTLANIIDLASKPRWC--LGIAGtKRRTFRNI---VGHAKGVGDvssLSSWTNEQFDPQLSWKDV 238
Cdd:PRK11197 163 ARYRDAHSGMSGPNA-AMRRYLQAVTHPQWAwdVGLNG-RPHDLGNIsayLGKPTGLED---YIGWLGNNFDPSISWKDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 239 AWIKERWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLK 318
Cdd:PRK11197 238 EWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVR 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 499216877 319 ALCLGAKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQL 376
Cdd:PRK11197 318 MIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
|
|
| L_lactate_LldD |
NF033901 |
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ... |
9-378 |
2.19e-124 |
|
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: 363.37 E-value: 2.19e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 9 DLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTGMQHAD 88
Cdd:NF033901 8 DYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGLTGMYARR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 89 GEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILGQRHKD 168
Cdd:NF033901 88 GEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPTPGARYRD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 169 VRNGLSAPpKMTLANIIDLASKPRWC--LGIAGtKRRTFRNI---VGHAKGVGDvssLSSWTNEQFDPQLSWKDVAWIKE 243
Cdd:NF033901 168 AHSGMSGP-NAALRRMLQAVTHPQWAwdVGLLG-RPHDLGNIsayRGKPTGLED---YIGWLGNNFDPSISWKDLEWIRE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 244 RWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKALCLG 323
Cdd:NF033901 243 FWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIALG 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 499216877 324 AKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQLRR 378
Cdd:NF033901 323 ADSVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRDSLVQ 377
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
281-330 |
5.42e-03 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 37.95 E-value: 5.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 499216877 281 LDGASS----SIMVLEEIADTVGDRIEVhmDGGIRSGQDVLKALCLGAKGTYIG 330
Cdd:TIGR00007 50 LDGAKEggpvNLPVIKKIVRETGVPVQV--GGGIRSLEDVEKLLDLGVDRVIIG 101
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
1-378 |
0e+00 |
|
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: 536.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 1 MSDILTIADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTG 80
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 81 LTGMQHADGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQ 160
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 161 ILGQRHKDVRNGLSAPPKMTLANIIDLASKPRWCLGIAgtkrrtfrnivghakgvgdvsSLSSWTNEQFDPQLSWKDVAW 240
Cdd:COG1304 161 VLGRRERDLREGFSQPPRLTPRNLLEAATHPRWALGLA---------------------SLAAWLDTNFDPSLTWDDIAW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 241 IKERWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKAL 320
Cdd:COG1304 220 LRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKAL 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 499216877 321 CLGAKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQLRR 378
Cdd:COG1304 300 ALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
14-378 |
9.29e-179 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 500.14 E-value: 9.29e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 14 ARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTGMQHADGEMLA 93
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 94 AKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILGQRHKDVRNGL 173
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 174 SAPPKMTLANIIDLASKPRWCLGIAGTkrrtfrnivghakgvGDVSSLSSWTNEQFDPQLSWKDVAWIKERWGGKLILKG 253
Cdd:pfam01070 161 TLPPRLTPRNLLDLALHPRWALGVLRR---------------GGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 254 ILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKALCLGAKGTYIGRPF 333
Cdd:pfam01070 226 ILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPF 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 499216877 334 LYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQLRR 378
Cdd:pfam01070 306 LYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
8-373 |
9.05e-158 |
|
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: 444.97 E-value: 9.05e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 8 ADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTGMQHA 87
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 88 DGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILGQRhk 167
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 168 dvrnglsappkmtlaniidlaskprwclgiagtkrrtfrnivghakgvgdvsslsswtneqfdpqLSWKDVAWIKERWGG 247
Cdd:cd02809 159 -----------------------------------------------------------------LTWDDLAWLRSQWKG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 248 KLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKALCLGAKGT 327
Cdd:cd02809 174 PLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAV 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499216877 328 YIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGK 373
Cdd:cd02809 254 LIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
4-376 |
1.28e-150 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 430.21 E-value: 1.28e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 4 ILTIADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTG 83
Cdd:PRK11197 3 ISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 84 MQHADGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILG 163
Cdd:PRK11197 83 MYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 164 QRHKDVRNGLSAPPKmTLANIIDLASKPRWC--LGIAGtKRRTFRNI---VGHAKGVGDvssLSSWTNEQFDPQLSWKDV 238
Cdd:PRK11197 163 ARYRDAHSGMSGPNA-AMRRYLQAVTHPQWAwdVGLNG-RPHDLGNIsayLGKPTGLED---YIGWLGNNFDPSISWKDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 239 AWIKERWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLK 318
Cdd:PRK11197 238 EWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVR 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 499216877 319 ALCLGAKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQL 376
Cdd:PRK11197 318 MIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
|
|
| L_lactate_LldD |
NF033901 |
FMN-dependent L-lactate dehydrogenase LldD; LldD is an FMN-dependent L-lactate dehydrogenase. ... |
9-378 |
2.19e-124 |
|
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: 363.37 E-value: 2.19e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 9 DLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTGMQHAD 88
Cdd:NF033901 8 DYRAAAQRKLPPFLFHYIDGGAYAEHTLRRNVEDLADIALRQRVLKNMSELSLETKLFGETLAMPVALAPVGLTGMYARR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 89 GEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILGQRHKD 168
Cdd:NF033901 88 GEVQAARAAAAKGIPFTLSTVSVCPIEEVAPAIDRPMWFQLYVLKDRGFMRNALERAKAAGVTTLVFTVDMPTPGARYRD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 169 VRNGLSAPpKMTLANIIDLASKPRWC--LGIAGtKRRTFRNI---VGHAKGVGDvssLSSWTNEQFDPQLSWKDVAWIKE 243
Cdd:NF033901 168 AHSGMSGP-NAALRRMLQAVTHPQWAwdVGLLG-RPHDLGNIsayRGKPTGLED---YIGWLGNNFDPSISWKDLEWIRE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 244 RWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKALCLG 323
Cdd:NF033901 243 FWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIKILADSGIRNGLDVVRMIALG 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 499216877 324 AKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQLRR 378
Cdd:NF033901 323 ADSVLLGRAFVYALAAAGEAGVANLLDLIEKEMRVAMTLTGAKSIAEISRDSLVQ 377
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
9-377 |
4.43e-112 |
|
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: 330.71 E-value: 4.43e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 9 DLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTGMQHAD 88
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 89 GEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTK--PFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILGQRH 166
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPdqPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 167 KDVRNGLSAPPKMTLAniidlaskprwclgiagtkrrtfrniVGHAKGVGDVSSLSSWTneQFDPQLSWKDVAWIKERWG 246
Cdd:cd02922 162 RDERLKAEEAVSDGPA--------------------------GKKTKAKGGGAGRAMSG--FIDPTLTWDDIKWLRKHTK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 247 GKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEI---ADTVGDRIEVHMDGGIRSGQDVLKALCLG 323
Cdd:cd02922 214 LPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIrkhCPEVFDKIEVYVDGGVRRGTDVLKALCLG 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 499216877 324 AKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGkrlVTDMgkDQLR 377
Cdd:cd02922 294 AKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLG---VTSL--DQLG 342
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
8-376 |
3.04e-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: 312.29 E-value: 3.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 8 ADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTGMQHA 87
Cdd:cd03332 22 ERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 88 DGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTK-PFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILGQRH 166
Cdd:cd03332 102 DAELATARAAAELGVPYILSTASSSSIEDVAAAAGDaPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 167 KDVRNG-LSAPPKMTLANIIdlaSKPRWclgiagtkRRTFRNIVGH-AKGVGDVSSLSSWTNEQF-DPQLSWKDVAWIKE 243
Cdd:cd03332 182 RDLDLGyLPFLRGIGIANYF---SDPVF--------RKKLAEPVGEdPEAPPPMEAAVARFVSVFsGPSLTWEDLAFLRE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 244 RWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKALCLG 323
Cdd:cd03332 251 WTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALG 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 499216877 324 AKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQL 376
Cdd:cd03332 331 AKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
8-364 |
6.83e-102 |
|
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: 305.60 E-value: 6.83e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 8 ADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTGMQHA 87
Cdd:cd04736 1 EDYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 88 DGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRdKDFVLDLIDRAKAAKCSALVLTLDLQILGQRHK 167
Cdd:cd04736 81 NGDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 168 DVRNGLSAPPKMTLANIIDLASKPRWCLgiagtkrRTFRNIVGHAKG-----VGDVSSLSSWTNEQFDPQLSWKDVAWIK 242
Cdd:cd04736 160 DLRNGFAIPFRYTPRVLLDGILHPRWLL-------RFLRNGMPQLANfasddAIDVEVQAALMSRQMDASFNWQDLRWLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 243 ERWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDriEVHMDGGIRSGQDVLKALCL 322
Cdd:cd04736 233 DLWPHKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYK--PVLIDSGIRRGSDIVKALAL 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 499216877 323 GAKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCG 364
Cdd:cd04736 311 GANAVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIG 352
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
1-377 |
1.82e-96 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 291.74 E-value: 1.82e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 1 MSDILTIADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTG 80
Cdd:PLN02535 2 ADEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 81 LTGMQHADGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQ 160
Cdd:PLN02535 82 MHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 161 ILGQRHKDVRNGLSAPpkmTLANIIDLASKPrwclgiagtkrrtfrniVGHAKGvgdvSSLSSWTNEQFDPQLSWKDVAW 240
Cdd:PLN02535 162 RLGRREADIKNKMISP---QLKNFEGLLSTE-----------------VVSDKG----SGLEAFASETFDASLSWKDIEW 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 241 IKERWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKAL 320
Cdd:PLN02535 218 LRSITNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKAL 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 499216877 321 CLGAKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQLR 377
Cdd:PLN02535 298 ALGAQAVLVGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVR 354
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
3-371 |
7.33e-91 |
|
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: 277.02 E-value: 7.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 3 DILTIADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLT 82
Cdd:cd04737 4 DIINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 83 GMQHADGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTK-PFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQI 161
Cdd:cd04737 84 GLAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGgPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 162 LGQRHKDVRNGLSAPPKMTLANIIDLaskprwclgiagtkrrtfrnivGHAKGVGDvsslsSWTNEQFDPQLSWKDVAWI 241
Cdd:cd04737 164 GGNREADIRNKFQFPFGMPNLNHFSE----------------------GTGKGKGI-----SEIYAAAKQKLSPADIEFI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 242 KERWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKALC 321
Cdd:cd04737 217 AKISGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALA 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 499216877 322 LGAKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDM 371
Cdd:cd04737 297 SGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDV 346
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
3-376 |
7.01e-86 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 264.67 E-value: 7.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 3 DILTIADLKDLARRRVPKMFFDYADSGAWTESTYRANEEDFQKIKFRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLT 82
Cdd:PLN02493 2 EITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 83 GMQHADGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWFQLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQIL 162
Cdd:PLN02493 82 KMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 163 GQRHKDVRNGLSAPPKMTLANIIDLAskprwclgiagtkrrtfrniVGHAKGVGDvSSLSSWTNEQFDPQLSWKDVAWIK 242
Cdd:PLN02493 162 GRRESDIKNRFTLPPNLTLKNFEGLD--------------------LGKMDEAND-SGLASYVAGQIDRTLSWKDVQWLQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 243 ERWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRSGQDVLKALCL 322
Cdd:PLN02493 221 TITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALAL 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 499216877 323 GAKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRLVTDMGKDQL 376
Cdd:PLN02493 301 GASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 354
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
48-376 |
2.85e-74 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 235.00 E-value: 2.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 48 FRQRVMVDMSNRSLESTMIGQKVSMPVALAPTGLTGMQHADGEMLAAKAAEEFGVPFTLSTMSICSIEDVASATTKPFWF 127
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 128 QLYVLRDKDFVLDLIDRAKAAKCSALVLTLDLQILGQRHKDVRNGLSAPPKMTLANIIDLAskprwclgiagtkrrtfrn 207
Cdd:PLN02979 126 QLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLD------------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 208 iVGHAKGVGDvSSLSSWTNEQFDPQLSWKDVAWIKERWGGKLILKGILDKEDALMAAKTGADAIVVSNHGGRQLDGASSS 287
Cdd:PLN02979 187 -LGKMDEAND-SGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPAT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 288 IMVLEEIADTVGDRIEVHMDGGIRSGQDVLKALCLGAKGTYIGRPFLYGLGALGKEGVTKALEIIRKEMDITLALCGKRL 367
Cdd:PLN02979 265 ISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRS 344
|
....*....
gi 499216877 368 VTDMGKDQL 376
Cdd:PLN02979 345 LKEISRNHI 353
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
260-338 |
7.39e-09 |
|
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: 56.96 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 260 ALMAAKTGADAIVVSNHGGRQldGASSsimvlEEIADTVG--------------------DRIEVHMDGGIRSGQDVLKA 319
Cdd:pfam01645 219 AAGVAKAGADIILIDGYDGGT--GASP-----KTSIKHAGlpwelalaeahqtlkenglrDRVSLIADGGLRTGADVAKA 291
|
90
....*....|....*....
gi 499216877 320 LCLGAKGTYIGRPFLYGLG 338
Cdd:pfam01645 292 AALGADAVYIGTAALIALG 310
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
241-371 |
1.38e-08 |
|
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: 55.58 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 241 IKERWGGKLILK----GIlDKEDALMAAKTGADAIVVSNHGG-------------RQLDGAS-------SSIMVLEEIAD 296
Cdd:cd02811 173 LVKALSVPVIVKevgfGI-SRETAKRLADAGVKAIDVAGAGGtswarvenyrakdSDQRLAEyfadwgiPTAASLLEVRS 251
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499216877 297 TVGDrIEVHMDGGIRSGQDVLKALCLGAKGTYIGRPFlygLGAL--GKEGVTKALEIIRKEMDITLALCGKRLVTDM 371
Cdd:cd02811 252 ALPD-LPLIASGGIRNGLDIAKALALGADLVGMAGPF---LKAAleGEEAVIETIEQIIEELRTAMFLTGAKNLAEL 324
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
235-331 |
1.48e-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: 54.13 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 235 WKDVAWIKERWGG-KLILKGILDKEDALMAAKT-GADAIVVSNHGGRQLDGASSSIMVLEEIADTVGDRIEVHMDGGIRS 312
Cdd:cd04722 102 LELIRELREAVPDvKVVVKLSPTGELAAAAAEEaGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGIND 181
|
90
....*....|....*....
gi 499216877 313 GQDVLKALCLGAKGTYIGR 331
Cdd:cd04722 182 PEDAAEALALGADGVIVGS 200
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
238-334 |
4.81e-08 |
|
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: 53.26 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 238 VAWIKErWGGKLILKgILDKEDALMAAKTGADAIVVSN-----HGGRQLDGasssIMVL-EEIADTVGdrIEVHMDGGIR 311
Cdd:cd04730 95 VERLKA-AGIKVIPT-VTSVEEARKAEAAGADALVAQGaeaggHRGTFDIG----TFALvPEVRDAVD--IPVIAAGGIA 166
|
90 100
....*....|....*....|...
gi 499216877 312 SGQDVLKALCLGAKGTYIGRPFL 334
Cdd:cd04730 167 DGRGIAAALALGADGVQMGTRFL 189
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
260-339 |
1.24e-07 |
|
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: 52.93 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 260 ALMAAKTGADAIVVSNHGGRQldGASSsimvlEEIADTVG--------------------DRIEVHMDGGIRSGQDVLKA 319
Cdd:cd02808 231 AAGVAAAGADFITIDGAEGGT--GAAP-----LTFIDHVGlptelglarahqalvknglrDRVSLIASGGLRTGADVAKA 303
|
90 100
....*....|....*....|
gi 499216877 320 LCLGAKGTYIGRPFLYGLGA 339
Cdd:cd02808 304 LALGADAVGIGTAALIALGC 323
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
238-334 |
2.96e-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: 48.57 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 238 VAWIKErWGGKLILKGIlDKEDALMAAKTGADAIVVSN-----HGGRQLdgasSSIMVL-EEIADTVgdRIEVHMDGGIR 311
Cdd:COG2070 97 IERLKE-AGIKVIPIVT-SVREARKAEKAGADAVVAEGaeaggHRGADE----VSTFALvPEVRDAV--DIPVIAAGGIA 168
|
90 100
....*....|....*....|...
gi 499216877 312 SGQDVLKALCLGAKGTYIGRPFL 334
Cdd:COG2070 169 DGRGIAAALALGADGVQMGTRFL 191
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
241-360 |
4.47e-06 |
|
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: 47.89 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 241 IKERWGGKLILKGILDKEDALMAAKTGADAIVVSN-----HGGRQLDGASSSIMVLEEIADTVGdrIEVHMDGGIRSGQD 315
Cdd:pfam03060 130 FRLHFAGVALIPTISSAKEARIAEARGADALIVQGpeaggHQGTPEYGDKGLFRLVPQVPDAVD--IPVIAAGGIWDRRG 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 499216877 316 VLKALCLGAKGTYIGRPFLyglgaLGKEGVTKA---LEIIRKEMDITL 360
Cdd:pfam03060 208 VAAALALGASGVQMGTRFL-----LTKESGAHDahkQKITEAGEDDTL 250
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
264-338 |
6.43e-06 |
|
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: 48.32 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 264 AKTG--ADAIVVSNH-GGrqlDGAS--SSI----MVLEE-IADT----VG----DRIEVHMDGGIRSGQDVLKALCLGAK 325
Cdd:COG0069 388 AKTGayADFITIDGGeGG---TGAAplESIkhagLPWELgLAEVhqtlVGnglrDRIRLIADGKLKTGRDVAIAAALGAD 464
|
90
....*....|...
gi 499216877 326 GTYIGRPFLYGLG 338
Cdd:COG0069 465 EFGFARAFMVALG 477
|
|
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
264-324 |
3.42e-03 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 39.47 E-value: 3.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499216877 264 AKTGADAIVVSNH-GGrqlDGAS--SSI--------MVLEE-----IADTVGDRIEVHMDGGIRSGQDVLKALCLGA 324
Cdd:PRK11750 1017 AKAYADLITISGYdGG---TGASplTSVkyagspweLGLAEthqalVANGLRHKIRLQVDGGLKTGLDVIKAAILGA 1090
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
281-330 |
5.42e-03 |
|
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]
Pssm-ID: 272850 [Multi-domain] Cd Length: 230 Bit Score: 37.95 E-value: 5.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 499216877 281 LDGASS----SIMVLEEIADTVGDRIEVhmDGGIRSGQDVLKALCLGAKGTYIG 330
Cdd:TIGR00007 50 LDGAKEggpvNLPVIKKIVRETGVPVQV--GGGIRSLEDVEKLLDLGVDRVIIG 101
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
236-330 |
7.92e-03 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 37.31 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499216877 236 KDVAWIKERWGGKLILKGIL----DKEDALM------AAKTGADAIVVSNhgGRQLDGASssIMVLEEIADTVGDRIEVH 305
Cdd:cd00945 101 EEIAAVVEAADGGLPLKVILetrgLKTADEIakaariAAEAGADFIKTST--GFGGGGAT--VEDVKLMKEAVGGRVGVK 176
|
90 100
....*....|....*....|....*
gi 499216877 306 MDGGIRSGQDVLKALCLGAKGTYIG 330
Cdd:cd00945 177 AAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| |
