|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
15-362 |
5.55e-179 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 500.52 E-value: 5.55e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 15 AKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVDGELAT 94
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 95 VRACQSLGTGMMLSSWATSSIEEVAEAGpEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNR 174
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 175 FKLPPQLRMKNFETSTLSFSPEENF---GDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVKHG 251
Cdd:pfam01070 160 FTLPPRLTPRNLLDLALHPRWALGVlrrGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 252 LNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKGVQD 331
Cdd:pfam01070 240 VDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAH 319
|
330 340 350
....*....|....*....|....*....|.
gi 11068137 332 VLEILKEEFRLAMALSGCQNVKVIDKTLVRK 362
Cdd:pfam01070 320 ALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
9-357 |
1.34e-167 |
|
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: 469.62 E-value: 1.34e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 9 NDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHV 88
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 89 DGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPeALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRL 168
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 169 ddvrnrfklppqlrmknfetstlsfspeenfgddsglaayvakaidpsiSWEDIKWLRRLTSLPIVAKGILRGDDAREAV 248
Cdd:cd02809 160 -------------------------------------------------TWDDLAWLRSQWKGPLILKGILTPEDALRAV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 249 KHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKG 328
Cdd:cd02809 191 DAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAG 270
|
330 340
....*....|....*....|....*....
gi 11068137 329 VQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:cd02809 271 VAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
2-361 |
2.22e-163 |
|
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: 461.14 E-value: 2.22e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 2 LPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATA 81
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 82 MQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPeALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDT 161
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAP-APLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 162 PYLGNRLDDVRNRFKLPPQLRMKNFETSTLSfsPEENFGDdSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRG 241
Cdd:COG1304 160 PVLGRRERDLREGFSQPPRLTPRNLLEAATH--PRWALGL-ASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 242 DDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGL 321
Cdd:COG1304 237 EDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 11068137 322 AFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 361
Cdd:COG1304 317 AAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
8-357 |
1.53e-141 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 406.42 E-value: 1.53e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 8 INDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAH 87
Cdd:PLN02493 6 VTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 88 VDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPeALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNR 167
Cdd:PLN02493 86 PDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 168 LDDVRNRFKLPPQLRMKNFETSTLSFSPEENfgdDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREA 247
Cdd:PLN02493 165 ESDIKNRFTLPPNLTLKNFEGLDLGKMDEAN---DSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 248 VKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEK 327
Cdd:PLN02493 242 IQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEA 321
|
330 340 350
....*....|....*....|....*....|
gi 11068137 328 GVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:PLN02493 322 GVRKVLQMLRDEFELTMALSGCRSLKEISR 351
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
15-362 |
5.55e-179 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 500.52 E-value: 5.55e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 15 AKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVDGELAT 94
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 95 VRACQSLGTGMMLSSWATSSIEEVAEAGpEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNR 174
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 175 FKLPPQLRMKNFETSTLSFSPEENF---GDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVKHG 251
Cdd:pfam01070 160 FTLPPRLTPRNLLDLALHPRWALGVlrrGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 252 LNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKGVQD 331
Cdd:pfam01070 240 VDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAH 319
|
330 340 350
....*....|....*....|....*....|.
gi 11068137 332 VLEILKEEFRLAMALSGCQNVKVIDKTLVRK 362
Cdd:pfam01070 320 ALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
9-357 |
1.34e-167 |
|
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: 469.62 E-value: 1.34e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 9 NDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHV 88
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 89 DGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPeALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRL 168
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 169 ddvrnrfklppqlrmknfetstlsfspeenfgddsglaayvakaidpsiSWEDIKWLRRLTSLPIVAKGILRGDDAREAV 248
Cdd:cd02809 160 -------------------------------------------------TWDDLAWLRSQWKGPLILKGILTPEDALRAV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 249 KHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKG 328
Cdd:cd02809 191 DAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAG 270
|
330 340
....*....|....*....|....*....
gi 11068137 329 VQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:cd02809 271 VAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
2-361 |
2.22e-163 |
|
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: 461.14 E-value: 2.22e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 2 LPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATA 81
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 82 MQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPeALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDT 161
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAP-APLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 162 PYLGNRLDDVRNRFKLPPQLRMKNFETSTLSfsPEENFGDdSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRG 241
Cdd:COG1304 160 PVLGRRERDLREGFSQPPRLTPRNLLEAATH--PRWALGL-ASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 242 DDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGL 321
Cdd:COG1304 237 EDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 11068137 322 AFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 361
Cdd:COG1304 317 AAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
8-357 |
1.53e-141 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 406.42 E-value: 1.53e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 8 INDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAH 87
Cdd:PLN02493 6 VTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 88 VDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPeALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNR 167
Cdd:PLN02493 86 PDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 168 LDDVRNRFKLPPQLRMKNFETSTLSFSPEENfgdDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREA 247
Cdd:PLN02493 165 ESDIKNRFTLPPNLTLKNFEGLDLGKMDEAN---DSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 248 VKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEK 327
Cdd:PLN02493 242 IQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEA 321
|
330 340 350
....*....|....*....|....*....|
gi 11068137 328 GVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:PLN02493 322 GVRKVLQMLRDEFELTMALSGCRSLKEISR 351
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
1-361 |
1.61e-136 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 393.43 E-value: 1.61e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 1 MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGAT 80
Cdd:PLN02535 1 MADEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 81 AMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAeAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVD 160
Cdd:PLN02535 81 AMHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEVA-SSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 161 TPYLGNRLDDVRNRFKLPpqlRMKNFETStlsFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILR 240
Cdd:PLN02535 160 VPRLGRREADIKNKMISP---QLKNFEGL---LSTEVVSDKGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 241 GDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWG 320
Cdd:PLN02535 234 REDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYG 313
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 11068137 321 LAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 361
Cdd:PLN02535 314 LAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVR 354
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
9-353 |
1.61e-130 |
|
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: 377.32 E-value: 1.61e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 9 NDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHV 88
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 89 DGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPE-ALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNR 167
Cdd:cd02922 81 DGELNLARAAGKHGILQMISTNASCSLEEIVDARPPdQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 168 LDDVRNRFklppqlrmknfeTSTLSFSPEENFGDDS--GLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAR 245
Cdd:cd02922 161 ERDERLKA------------EEAVSDGPAGKKTKAKggGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 246 EAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVE---AVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLA 322
Cdd:cd02922 229 LAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIRKhcpEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALS 308
|
330 340 350
....*....|....*....|....*....|.
gi 11068137 323 FQGEKGVQDVLEILKEEFRLAMALSGCQNVK 353
Cdd:cd02922 309 AYGEEGVEKAIQILKDEIETTMRLLGVTSLD 339
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
10-360 |
1.39e-129 |
|
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: 376.62 E-value: 1.39e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 10 DYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVD 89
Cdd:cd03332 23 RLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFHPD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 90 GELATVRACQSLGTGMMLSSWATSSIEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLD 169
Cdd:cd03332 103 AELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRPR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 170 DVRNRFKlpPQLR-------------MKNFETStlsfsPEENFGDDSGLAAYVAKAI----DPSISWEDIKWLRRLTSLP 232
Cdd:cd03332 183 DLDLGYL--PFLRgigianyfsdpvfRKKLAEP-----VGEDPEAPPPMEAAVARFVsvfsGPSLTWEDLAFLREWTDLP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 233 IVAKGILRGDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVF 312
Cdd:cd03332 256 IVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVL 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 11068137 313 VGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV 360
Cdd:cd03332 336 IGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
51-357 |
1.00e-126 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 368.67 E-value: 1.00e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 51 PRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPeALRWLQ 130
Cdd:PLN02979 48 PRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 131 LYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQLRMKNFETSTLSFSPEENfgdDSGLAAYVA 210
Cdd:PLN02979 127 LYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEAN---DSGLASYVA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 211 KAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFL 290
Cdd:PLN02979 204 GQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFL 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11068137 291 DGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:PLN02979 284 DGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISR 350
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
5-358 |
1.13e-117 |
|
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: 345.20 E-value: 1.13e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 5 LICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQR 84
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 85 MAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYL 164
Cdd:cd04737 85 LAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 165 GNRLDDVRNRFKLPpqLRMKNFEtstlsfSPEENFGDDSGLAaYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDA 244
Cdd:cd04737 165 GNREADIRNKFQFP--FGMPNLN------HFSEGTGKGKGIS-EIYAAAKQKLSPADIEFIAKISGLPVIVKGIQSPEDA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 245 REAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQ 324
Cdd:cd04737 236 DVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALG 315
|
330 340 350
....*....|....*....|....*....|....
gi 11068137 325 GEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKT 358
Cdd:cd04737 316 GAQGVASVLEHLNKELKIVMQLAGTRTIEDVKRT 349
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
10-357 |
1.63e-90 |
|
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: 275.94 E-value: 1.63e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 10 DYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVD 89
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 90 GELATVRACQSLGTGMMLSSWATSSIEEVAEAGPEALrWLQLYIYKdREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLD 169
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDL-WFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 170 DVRNRFKLP--------------PQLRMKNFETSTL---SFSPEENFGDDSGlAAYVAKAIDPSISWEDIKWLRRLTSLP 232
Cdd:cd04736 160 DLRNGFAIPfrytprvlldgilhPRWLLRFLRNGMPqlaNFASDDAIDVEVQ-AALMSRQMDASFNWQDLRWLRDLWPHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 233 IVAKGILRGDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVegKVEVFLDGGVRKGTDVLKALALGAKAVF 312
Cdd:cd04736 239 LLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAAT--YKPVLIDSGIRRGSDIVKALALGANAVL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 11068137 313 VGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 357
Cdd:cd04736 317 LGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
7-366 |
2.55e-88 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 271.13 E-value: 2.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 7 CINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPIC---VGATAMq 83
Cdd:PRK11197 5 AASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVAlapVGLTGM- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 84 rMAHvDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPEALrWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPY 163
Cdd:PRK11197 84 -YAR-RGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPM-WFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 164 LGNRLDDVRNRFKLP-------------PQ------LRMKNFETSTLSfspeENFGDDSGLAAYVA---KAIDPSISWED 221
Cdd:PRK11197 161 PGARYRDAHSGMSGPnaamrrylqavthPQwawdvgLNGRPHDLGNIS----AYLGKPTGLEDYIGwlgNNFDPSISWKD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 222 IKWLRRLTSLPIVAKGILRGDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVL 301
Cdd:PRK11197 237 LEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11068137 302 KALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLA 366
Cdd:PRK11197 317 RMIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSLVQGNAA 381
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
56-353 |
1.38e-14 |
|
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: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 56 NVAETDLSTSVLGQRVSMPICVgaTAM----QRMAHVDGELAtvRACQSLGTGMMLSS----------WATSSIeeVAEA 121
Cdd:cd02811 36 DLDDIDLSTEFLGKRLSAPLLI--SAMtggsEKAKEINRNLA--EAAEELGIAMGVGSqraaledpelAESFTV--VREA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 122 GPEALRWLQLYIYKDREVTKKLVRQAEKM-GYKAIFVTVdtpylgnrlddvrNrfklPPQ-LRMknfetstlsfsPEenf 199
Cdd:cd02811 110 PPNGPLIANLGAVQLNGYGVEEARRAVEMiEADALAIHL-------------N----PLQeAVQ-----------PE--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 200 GD-D-SGLaayvakaidpsisWEDIKWLRRLTSLPIVAK----GILRgDDAREAVKHGLNGILVSNHG---------ARQ 264
Cdd:cd02811 159 GDrDfRGW-------------LERIEELVKALSVPVIVKevgfGISR-ETAKRLADAGVKAIDVAGAGgtswarvenYRA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 265 LD------------GVPaTIDVLPEIVEAVEgKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVwGLAFQGEKGVQDV 332
Cdd:cd02811 225 KDsdqrlaeyfadwGIP-TAASLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVIET 301
|
330 340
....*....|....*....|.
gi 11068137 333 LEILKEEFRLAMALSGCQNVK 353
Cdd:cd02811 302 IEQIIEELRTAMFLTGAKNLA 322
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
204-315 |
2.59e-08 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 53.36 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 204 GLAAYVAKAIDPSISWEDIKWLR-RLTSLPIVAKGILRGDDAREAVK-HGLNGILVSNHGARQLDGVPATIDVLPEIVEA 281
Cdd:cd04722 87 GVEIHGAVGYLAREDLELIRELReAVPDVKVVVKLSPTGELAAAAAEeAGVDEVGLGNGGGGGGGRDAVPIADLLLILAK 166
|
90 100 110
....*....|....*....|....*....|....
gi 11068137 282 VEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGR 315
Cdd:cd04722 167 RGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
199-314 |
3.49e-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: 47.48 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 199 FGDDSGLAAYVAKAidpsisweDIKWLRRLTSLpivakgilrgDDAREAVKHGLNGILVSN-----HGARQLDGvpaTID 273
Cdd:cd04730 88 FGPPAEVVERLKAA--------GIKVIPTVTSV----------EEARKAEAAGADALVAQGaeaggHRGTFDIG---TFA 146
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 11068137 274 VLPEIVEAVegKVEVFLDGGVRKGTDVLKALALGAKAVFVG 314
Cdd:cd04730 147 LVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 185
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
232-316 |
1.46e-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: 46.56 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 232 PIVAK---GILRGDDAREAVKHGLNGILVSNH----GA-----RQLDGVPaTIDVLPEIVEAV--EG---KVEVFLDGGV 294
Cdd:pfam01645 204 PISVKlvsGHGVGTIAAGVAKAGADIILIDGYdggtGAspktsIKHAGLP-WELALAEAHQTLkeNGlrdRVSLIADGGL 282
|
90 100
....*....|....*....|..
gi 11068137 295 RKGTDVLKALALGAKAVFVGRP 316
Cdd:pfam01645 283 RTGADVAKAAALGADAVYIGTA 304
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
267-315 |
3.51e-05 |
|
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.
Pssm-ID: 239202 [Multi-domain] Cd Length: 392 Bit Score: 45.22 E-value: 3.51e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 11068137 267 GVPATIDVLpeIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGR 315
Cdd:cd02808 269 GLARAHQAL--VKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGT 315
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
244-314 |
7.07e-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: 43.95 E-value: 7.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11068137 244 AREAVKHGLNGILVSNHGA---RQLDGVPaTIDVLPEIVEAVegKVEVFLDGGVRKGTDVLKALALGAKAVFVG 314
Cdd:COG2070 117 ARKAEKAGADAVVAEGAEAgghRGADEVS-TFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 187
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
222-315 |
2.27e-04 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 43.03 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 222 IKWLRRLT-SLPIVAKGILRGDDAREAVKHGLNGI-------------LVSNHGARQLDGVpatIDVLPEiveAVEGKVE 287
Cdd:PTZ00314 273 IKKLKSNYpHVDIIAGNVVTADQAKNLIDAGADGLrigmgsgsicitqEVCAVGRPQASAV---YHVARY---ARERGVP 346
|
90 100
....*....|....*....|....*...
gi 11068137 288 VFLDGGVRKGTDVLKALALGAKAVFVGR 315
Cdd:PTZ00314 347 CIADGGIKNSGDICKALALGADCVMLGS 374
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
222-316 |
3.34e-04 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 42.12 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11068137 222 IKWLRRL-TSLPIVAKGILRGDDAREAVKHGLNGILV-----SNHGARQLDGV--P---ATIDVlpeiVEAVEG-KVEVF 289
Cdd:cd00381 126 IKFIKKKyPNVDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTRIVTGVgvPqatAVADV----AAAARDyGVPVI 201
|
90 100
....*....|....*....|....*..
gi 11068137 290 LDGGVRKGTDVLKALALGAKAVFVGRP 316
Cdd:cd00381 202 ADGGIRTSGDIVKALAAGADAVMLGSL 228
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|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
265-314 |
8.58e-03 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 37.46 E-value: 8.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 11068137 265 LDGVPATIDVLPEIVEAVEGKVEVflDGGVRKGTDVLKALALGAKAVFVG 314
Cdd:pfam00977 55 KEGRPVNLDVVEEIAEEVFIPVQV--GGGIRSLEDVERLLSAGADRVIIG 102
|
|
| |
