|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
2-298 |
2.46e-79 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 244.36 E-value: 2.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 2 KQNTPHN----YRTGDSNEIT----RQYFDSLLIEMRHIDSVI-PSTTFELYGENFSTPIMTAALSHLNNSRANGMVEMA 72
Cdd:pfam01070 2 RKRLPRFafdyLDGGAGDEVTlrrnRAAFDRIRLRPRVLRDVSnRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 73 KGAMAANAVMWTGMGDDAELEAIT-ATGAKTIKIIKPHSDNNTIFKKIEHAEKCGVLALGMDIDHSFNNKGEFDNVLGLP 151
Cdd:pfam01070 82 RAAAAAGIPFVLSTVSSTSLEEVAaAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGFT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 152 MSGK----------------------------------------TLDEIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVK 191
Cdd:pfam01070 162 LPPRltprnlldlalhprwalgvlrrggaggaaafvgsqfdpalTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAGVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 192 GIVVSHHHG-IMDFAVPPLMVLPKIARVVDRSIPIFVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVI 270
Cdd:pfam01070 242 GIVVSNHGGrQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHAL 321
|
330 340
....*....|....*....|....*...
gi 506406053 271 EEMTQELAGVMARTCSKDIASIDSSVIW 298
Cdd:pfam01070 322 EILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
1-293 |
1.56e-54 |
|
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: 179.18 E-value: 1.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 1 MKQNTPHN----YRTGDSNEIT----RQYFDSLLIEMRHI-DSVIPSTTFELYGENFSTPIMTAALSHLNNSRANGMVEM 71
Cdd:cd02809 7 ARRRLPKAvfdyIDGGAGDEVTlrrnRAAFDRIRLRPRVLrDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPDGELAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 72 AKGAMAANAVM--WTGMGddAELEAI--TATGAKTIKIIKPHSDNNTIfKKIEHAEKCGVLALGMDIDHsfnnkgefdnv 147
Cdd:cd02809 87 ARAAAAAGIPFtlSTVST--TSLEEVaaAAPGPRWFQLYVPRDREITE-DLLRRAEAAGYKALVLTVDT----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 148 lglPMSG--KTLDEIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHG-IMDFAVPPLMVLPKIARVVDRSIP 224
Cdd:cd02809 153 ---PVLGrrLTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGrQLDGAPATIDALPEIVAAVGGRIE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506406053 225 IFVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMARTCSKDIASID 293
Cdd:cd02809 230 VLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLD 298
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
19-298 |
5.71e-41 |
|
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: 145.28 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 19 RQYFDSLLIE---MRHIDSVipSTTFELYGENFSTPIMTA--ALSHLNNSRANgmVEMAKGAMAANAVMwtGMGddaele 93
Cdd:COG1304 40 RAAFDRVRLRprvLEDVSEI--DLSTTLLGKRLAAPFLIApmGGGGLAHPDGE--LALARAAAAAGIPM--GLS------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 94 aitATGAKTIKIIKPHSDNNTIF---------------KKIEHAEkCGVLALGMDIDHSFNNKGEFDNVLGLPMSGK--- 155
Cdd:COG1304 108 ---TQSTTSLEEVAAAAPAPLWFqlyvpkdrgftddllRRAEAAG-ADALVLTVDTPVLGRRERDLREGFSQPPRLTprn 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 156 -----------------------------TLDEIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHGI-MDFA 205
Cdd:COG1304 184 lleaathprwalglaslaawldtnfdpslTWDDIAWLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRqLDGG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 206 VPPLMVLPKIARVVDRSIPIFVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMARTC 285
Cdd:COG1304 264 PPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTG 343
|
330
....*....|...
gi 506406053 286 SKDIASIDSSVIW 298
Cdd:COG1304 344 CRSLAELRRALLV 356
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
25-289 |
1.77e-27 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 109.54 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 25 LLIEMRHIDSvipSTTfeLYGENFSTPIMTAALSHLNNSRANGMVEMAKGAMAANAVMWTGMGDDAELEAItATGAKTIK 104
Cdd:PLN02535 53 VLVDVSKIDM---STT--ILGYTISAPIMIAPTAMHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEV-ASSCNAVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 105 IIKPHsdnntIFKK-------IEHAEKCGVLALGMDIDHSFNNKGEFD-----------NVLGL--------------PM 152
Cdd:PLN02535 127 FLQLY-----VYKRrdiaaqlVQRAEKNGYKAIVLTADVPRLGRREADiknkmispqlkNFEGLlstevvsdkgsgleAF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 153 SGKTLD------EIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHG-IMDFAVPPLMVLPKIARVVDRSIPI 225
Cdd:PLN02535 202 ASETFDaslswkDIEWLRSITNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGArQLDYSPATISVLEEVVQAVGGRVPV 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506406053 226 FVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMART-CS--KDI 289
Cdd:PLN02535 282 LLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSgCPsvKDI 348
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
2-298 |
2.46e-79 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 244.36 E-value: 2.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 2 KQNTPHN----YRTGDSNEIT----RQYFDSLLIEMRHIDSVI-PSTTFELYGENFSTPIMTAALSHLNNSRANGMVEMA 72
Cdd:pfam01070 2 RKRLPRFafdyLDGGAGDEVTlrrnRAAFDRIRLRPRVLRDVSnRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 73 KGAMAANAVMWTGMGDDAELEAIT-ATGAKTIKIIKPHSDNNTIFKKIEHAEKCGVLALGMDIDHSFNNKGEFDNVLGLP 151
Cdd:pfam01070 82 RAAAAAGIPFVLSTVSSTSLEEVAaAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGFT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 152 MSGK----------------------------------------TLDEIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVK 191
Cdd:pfam01070 162 LPPRltprnlldlalhprwalgvlrrggaggaaafvgsqfdpalTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAGVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 192 GIVVSHHHG-IMDFAVPPLMVLPKIARVVDRSIPIFVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVI 270
Cdd:pfam01070 242 GIVVSNHGGrQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHAL 321
|
330 340
....*....|....*....|....*...
gi 506406053 271 EEMTQELAGVMARTCSKDIASIDSSVIW 298
Cdd:pfam01070 322 EILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
1-293 |
1.56e-54 |
|
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: 179.18 E-value: 1.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 1 MKQNTPHN----YRTGDSNEIT----RQYFDSLLIEMRHI-DSVIPSTTFELYGENFSTPIMTAALSHLNNSRANGMVEM 71
Cdd:cd02809 7 ARRRLPKAvfdyIDGGAGDEVTlrrnRAAFDRIRLRPRVLrDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPDGELAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 72 AKGAMAANAVM--WTGMGddAELEAI--TATGAKTIKIIKPHSDNNTIfKKIEHAEKCGVLALGMDIDHsfnnkgefdnv 147
Cdd:cd02809 87 ARAAAAAGIPFtlSTVST--TSLEEVaaAAPGPRWFQLYVPRDREITE-DLLRRAEAAGYKALVLTVDT----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 148 lglPMSG--KTLDEIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHG-IMDFAVPPLMVLPKIARVVDRSIP 224
Cdd:cd02809 153 ---PVLGrrLTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGrQLDGAPATIDALPEIVAAVGGRIE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506406053 225 IFVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMARTCSKDIASID 293
Cdd:cd02809 230 VLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLD 298
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
19-298 |
5.71e-41 |
|
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: 145.28 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 19 RQYFDSLLIE---MRHIDSVipSTTFELYGENFSTPIMTA--ALSHLNNSRANgmVEMAKGAMAANAVMwtGMGddaele 93
Cdd:COG1304 40 RAAFDRVRLRprvLEDVSEI--DLSTTLLGKRLAAPFLIApmGGGGLAHPDGE--LALARAAAAAGIPM--GLS------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 94 aitATGAKTIKIIKPHSDNNTIF---------------KKIEHAEkCGVLALGMDIDHSFNNKGEFDNVLGLPMSGK--- 155
Cdd:COG1304 108 ---TQSTTSLEEVAAAAPAPLWFqlyvpkdrgftddllRRAEAAG-ADALVLTVDTPVLGRRERDLREGFSQPPRLTprn 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 156 -----------------------------TLDEIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHGI-MDFA 205
Cdd:COG1304 184 lleaathprwalglaslaawldtnfdpslTWDDIAWLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRqLDGG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 206 VPPLMVLPKIARVVDRSIPIFVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMARTC 285
Cdd:COG1304 264 PPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTG 343
|
330
....*....|...
gi 506406053 286 SKDIASIDSSVIW 298
Cdd:COG1304 344 CRSLAELRRALLV 356
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
9-282 |
5.16e-37 |
|
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: 134.65 E-value: 5.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 9 YRTGDSNEITRQY----FDSLLIE---MRHIDSVIPSTTFelYGENFSTPIMTAALSHLNNSRANGMVEMAKGAMAANAV 81
Cdd:cd02922 19 YSSGADDEITLREnleaFQRIRFRprvLRDVEKVDTSTTI--LGHKVSLPFFISPAALAKLAHPDGELNLARAAGKHGIL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 82 MWTGMGDDAELEAIT---ATGAKTIKIIKPHSDNNTIFKKIEHAEKCGVLALGMDID----------------------H 136
Cdd:cd02922 97 QMISTNASCSLEEIVdarPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDapvlgkrerderlkaeeavsdgP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 137 SFNNKGEFDNVLGLPMSGK-----TLDEIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHG-IMDFAVPPLM 210
Cdd:cd02922 177 AGKKTKAKGGGAGRAMSGFidptlTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGrQLDTAPAPIE 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506406053 211 VLPKIARV---VDRSIPIFVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMA 282
Cdd:cd02922 257 VLLEIRKHcpeVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMR 331
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
15-292 |
5.46e-34 |
|
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: 126.79 E-value: 5.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 15 NEITRQYFDSLLIEMRHIDSVIPSTTFELYGENFSTPIMTAALSHLNNSRANGMVEMAKGAMAANAVMWTGMGDDAELEA 94
Cdd:cd04737 38 RENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLAHATGEVATARGMAEVGSLFSISTYSNTSLEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 95 ITATGAKTIKIIKPHSDNNTIFKK--IEHAEKCGVLALGMDIDHSFNNKGEFDNV------LGLPM---------SGKTL 157
Cdd:cd04737 118 IAKASNGGPKWFQLYMSKDDGFNRslLDRAKAAGAKAIILTADATVGGNREADIRnkfqfpFGMPNlnhfsegtgKGKGI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 158 DEIK------------EFVNA-TKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHGIMDFAVP-PLMVLPKIARVVDRSI 223
Cdd:cd04737 198 SEIYaaakqklspadiEFIAKiSGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPaSFDSLPEIAEAVNHRV 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506406053 224 PIFVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMARTCSKDIASI 292
Cdd:cd04737 278 PIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDV 346
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
25-289 |
1.77e-27 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 109.54 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 25 LLIEMRHIDSvipSTTfeLYGENFSTPIMTAALSHLNNSRANGMVEMAKGAMAANAVMWTGMGDDAELEAItATGAKTIK 104
Cdd:PLN02535 53 VLVDVSKIDM---STT--ILGYTISAPIMIAPTAMHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEV-ASSCNAVR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 105 IIKPHsdnntIFKK-------IEHAEKCGVLALGMDIDHSFNNKGEFD-----------NVLGL--------------PM 152
Cdd:PLN02535 127 FLQLY-----VYKRrdiaaqlVQRAEKNGYKAIVLTADVPRLGRREADiknkmispqlkNFEGLlstevvsdkgsgleAF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 153 SGKTLD------EIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHG-IMDFAVPPLMVLPKIARVVDRSIPI 225
Cdd:PLN02535 202 ASETFDaslswkDIEWLRSITNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGArQLDYSPATISVLEEVVQAVGGRVPV 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506406053 226 FVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMART-CS--KDI 289
Cdd:PLN02535 282 LLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSgCPsvKDI 348
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
149-297 |
3.30e-27 |
|
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: 108.91 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 149 GLPMSGKTLDEIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHG-IMDFAVPPLMVLPKIARVVDRSIPIFV 227
Cdd:cd03332 234 VFSGPSLTWEDLAFLREWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGrQVDGSIAALDALPEIVEAVGDRLTVLF 313
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 228 DCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMARTCSKDIASIDSSVI 297
Cdd:cd03332 314 DSGVRTGADIMKALALGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
153-295 |
9.90e-24 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 99.33 E-value: 9.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 153 SGKTLDEIKEFVNAtklPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHG-IMDFAVPPLMVLPKIARVVDRSIPIFVDCGV 231
Cdd:PRK11197 233 SWKDLEWIRDFWDG---PMVIKGILDPEDARDAVRFGADGIVVSNHGGrQLDGVLSSARALPAIADAVKGDITILADSGI 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506406053 232 ASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMARTCSKDIASIDSS 295
Cdd:PRK11197 310 RNGLDVVRMIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRD 373
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
25-297 |
5.62e-23 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 97.10 E-value: 5.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 25 LLIEMRHIDsvipsTTFELYGENFSTPIMTAALSHLNNSRANGMVEMAKGAMAANAVMWTGMGDDAELEAITATGAKtIK 104
Cdd:PLN02979 50 ILIDVSKID-----MTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPG-IR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 105 IIK--PHSDNNTIFKKIEHAEKCGVLALGMDIDHSFNNKGEFD--NVLGLP-------MSGKTLDEIKEFVNA------- 166
Cdd:PLN02979 124 FFQlyVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDikNRFTLPpnltlknFEGLDLGKMDEANDSglasyva 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 167 ------------------TKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHG-IMDFAVPPLMVLPKIARVVDRSIPIFV 227
Cdd:PLN02979 204 gqidrtlswkdvqwlqtiTKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGArQLDYVPATISALEEVVKATQGRIPVFL 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 228 DCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMARTCSKDIASIDSSVI 297
Cdd:PLN02979 284 DGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 353
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
25-292 |
5.11e-22 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 94.41 E-value: 5.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 25 LLIEMRHIDSVIPSTTFELygenfSTPIMTAALSHLNNSRANGMVEMAKGAMAANAVMWTGMGDDAELEAITATGAKtIK 104
Cdd:PLN02493 51 ILIDVSKIDMTTTVLGFKI-----SMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPG-IR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 105 IIK--PHSDNNTIFKKIEHAEKCGVLALGMDIDHSFNNKGEFD--------------NVLGLPM--------SG------ 154
Cdd:PLN02493 125 FFQlyVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDiknrftlppnltlkNFEGLDLgkmdeandSGlasyva 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 155 ----KTLD--EIKEFVNATKLPFVIKGVLSEKDIYKCLEAGVKGIVVSHHHG-IMDFAVPPLMVLPKIARVVDRSIPIFV 227
Cdd:PLN02493 205 gqidRTLSwkDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGArQLDYVPATISALEEVVKATQGRIPVFL 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506406053 228 DCGVASGIDVFKALALGADAVSVGLTLIPHLNEAGADGVQNVIEEMTQELAGVMARTCSKDIASI 292
Cdd:PLN02493 285 DGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEI 349
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
172-294 |
1.92e-17 |
|
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: 81.42 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 172 VIKGVLSEKDIYKCLEAGVKGIVVSHHHG-IMDFAVPPLMVLPKIARVVDRsiPIFVDCGVASGIDVFKALALGADAVSV 250
Cdd:cd04736 240 LVKGIVTAEDAKRCIELGADGVILSNHGGrQLDDAIAPIEALAEIVAATYK--PVLIDSGIRRGSDIVKALALGANAVLL 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 506406053 251 GLTLIPHLNEAGADGVQNVIEEMTQELAGVMARTCSKDIASIDS 294
Cdd:cd04736 318 GRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
157-290 |
5.95e-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: 73.69 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 157 LDEIKEFVNATKLPFVIKGV---LSEKDIYKCLEAGVKGIVVSHHHGI---------------------MDFAVPPLMVL 212
Cdd:cd02811 167 LERIEELVKALSVPVIVKEVgfgISRETAKRLADAGVKAIDVAGAGGTswarvenyrakdsdqrlaeyfADWGIPTAASL 246
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506406053 213 PKiARVVDRSIPIFVDCGVASGIDVFKALALGADAVSVGLTLIPHLNEaGADGVQNVIEEMTQELAGVMARTCSKDIA 290
Cdd:cd02811 247 LE-VRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKAALE-GEEAVIETIEQIIEELRTAMFLTGAKNLA 322
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
184-251 |
5.72e-06 |
|
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: 46.71 E-value: 5.72e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506406053 184 KCLEAGVKGIVVSHH----HGIMdFAVPPLMVLPKIARVVDrsIPIFVDCGVASGIDVFKALALGADAVSVG 251
Cdd:cd04730 117 KAEAAGADALVAQGAeaggHRGT-FDIGTFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGADGVQMG 185
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
184-251 |
1.85e-05 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 45.49 E-value: 1.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506406053 184 KCLEAGVKGIVVSH-----HHGIMDfaVPPLMVLPKIARVVDrsIPIFVDCGVASGIDVFKALALGADAVSVG 251
Cdd:COG2070 119 KAEKAGADAVVAEGaeaggHRGADE--VSTFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGADGVQMG 187
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
186-283 |
5.51e-05 |
|
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: 44.25 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 186 LEAGVKGIVVSHHHG--------IMDFA-VPPLMVLPKIARVV------DRsIPIFVDCGVASGIDVFKALALGADAVSV 250
Cdd:pfam01645 223 AKAGADIILIDGYDGgtgaspktSIKHAgLPWELALAEAHQTLkenglrDR-VSLIADGGLRTGADVAKAAALGADAVYI 301
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506406053 251 G----------LTLIPHLN-------------------EAGADGVQNVIEEMTQELAGVMAR 283
Cdd:pfam01645 302 GtaalialgciMCRVCHTNtcpvgvatqdpelrkrldfEGAPERVVNYFRFLAEEVRELLAA 363
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
155-251 |
6.70e-05 |
|
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: 42.96 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 155 KTLDEIKEFVNatKLPFVIK-GVLSEKDIYKCLEAGVKGIVVSHH-HGIMDFAVPPLMVLPKIARVVDRSIPIFVDCGVA 232
Cdd:cd04722 103 ELIRELREAVP--DVKVVVKlSPTGELAAAAAEEAGVDEVGLGNGgGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGIN 180
|
90
....*....|....*....
gi 506406053 233 SGIDVFKALALGADAVSVG 251
Cdd:cd04722 181 DPEDAAEALALGADGVIVG 199
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
186-282 |
1.61e-04 |
|
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: 42.91 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 186 LEAGVK-----GIVVSHHHG--------IMDFA-VPPLMVLPKIARVVDRS-----IPIFVDCGVASGIDVFKALALGAD 246
Cdd:cd02808 230 IAAGVAaagadFITIDGAEGgtgaapltFIDHVgLPTELGLARAHQALVKNglrdrVSLIASGGLRTGADVAKALALGAD 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506406053 247 AVS-----------------------VGLTL-IPHLNEA-----GADGVQNVIEEMTQELAGVMA 282
Cdd:cd02808 310 AVGigtaalialgciqarkchtntcpVGVATqDPELRRRldvegKAERVANYLKSLAEELRELAA 374
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
222-294 |
2.17e-03 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 39.17 E-value: 2.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506406053 222 SIPIFVDCGVASGIDVFKALALGADAVSVGLTLIphlneagADGVQnVIEEMTQELAGVMARtcsKDIASIDS 294
Cdd:PRK02506 241 SIQIIGTGGVKTGRDAFEHILCGASMVQVGTALH-------KEGPA-VFERLTKELKAIMAE---KGYQSLED 302
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
215-293 |
4.82e-03 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 38.13 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506406053 215 IARVVDRSIPIfVDC-GVASGIDVFKALALGADAVSVGLTLIphlneagADGVQnVIEEMTQELAGVMARtcsKDIASID 293
Cdd:COG0167 229 VAQAVGGDIPI-IGVgGISTAEDALEFILAGASAVQVGTALF-------YEGPG-LVRRIIRGLEAYLEE---KGFSSIS 296
|
|
| |
