|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
1-310 |
6.55e-161 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 452.37 E-value: 6.55e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGpEALRWMQLY 80
Cdd:pfam01070 39 VLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALARAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFEtnDLAFSPKGNF-----GDNSGLAE 155
Cdd:pfam01070 118 VPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGFTLPPRLTPRNLL--DLALHPRWALgvlrrGGAGGAAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 156 YVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVE 235
Cdd:pfam01070 196 FVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIP 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761924 236 VFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRK 310
Cdd:pfam01070 276 VLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
1-305 |
2.11e-145 |
|
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: 411.07 E-value: 2.11e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLY 80
Cdd:cd02809 45 VLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPDGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRfddvrnrfklppqlrmknfetndlafspkgnfgdnsglaeyvaqa 160
Cdd:cd02809 124 VPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR--------------------------------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 161 idpsLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDG 240
Cdd:cd02809 159 ----LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761924 241 GVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 305
Cdd:cd02809 235 GIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
1-309 |
8.94e-143 |
|
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: 406.83 E-value: 8.94e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLY 80
Cdd:COG1304 52 VLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAP-APLWFQLY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFEtnDLAFSPKGNFGdNSGLAEYVAQA 160
Cdd:COG1304 131 VPKDRGFTDDLLRRAEAAGADALVLTVDTPVLGRRERDLREGFSQPPRLTPRNLL--EAATHPRWALG-LASLAAWLDTN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 161 IDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDG 240
Cdd:COG1304 208 FDPSLTWDDIAWLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADG 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761924 241 GVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 309
Cdd:COG1304 288 GIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
1-305 |
2.00e-125 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 363.27 E-value: 2.00e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLY 80
Cdd:PLN02979 50 ILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFETNDLAfspKGNFGDNSGLAEYVAQA 160
Cdd:PLN02979 129 VYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLG---KMDEANDSGLASYVAGQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 161 IDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDG 240
Cdd:PLN02979 206 IDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDG 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761924 241 GVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 305
Cdd:PLN02979 286 GVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISR 350
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
1-310 |
6.55e-161 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 452.37 E-value: 6.55e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGpEALRWMQLY 80
Cdd:pfam01070 39 VLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALARAAAAAGIPFVLSTVSSTSLEEVAAAA-GGPLWFQLY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFEtnDLAFSPKGNF-----GDNSGLAE 155
Cdd:pfam01070 118 VPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGFTLPPRLTPRNLL--DLALHPRWALgvlrrGGAGGAAA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 156 YVAQAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVE 235
Cdd:pfam01070 196 FVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIP 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761924 236 VFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRK 310
Cdd:pfam01070 276 VLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
1-305 |
2.11e-145 |
|
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: 411.07 E-value: 2.11e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLY 80
Cdd:cd02809 45 VLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPDGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRfddvrnrfklppqlrmknfetndlafspkgnfgdnsglaeyvaqa 160
Cdd:cd02809 124 VPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR--------------------------------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 161 idpsLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDG 240
Cdd:cd02809 159 ----LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761924 241 GVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 305
Cdd:cd02809 235 GIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
1-309 |
8.94e-143 |
|
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: 406.83 E-value: 8.94e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLY 80
Cdd:COG1304 52 VLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAP-APLWFQLY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFEtnDLAFSPKGNFGdNSGLAEYVAQA 160
Cdd:COG1304 131 VPKDRGFTDDLLRRAEAAGADALVLTVDTPVLGRRERDLREGFSQPPRLTPRNLL--EAATHPRWALG-LASLAAWLDTN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 161 IDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDG 240
Cdd:COG1304 208 FDPSLTWDDIAWLRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADG 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761924 241 GVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 309
Cdd:COG1304 288 GIRRGLDVAKALALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLV 356
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
1-305 |
2.00e-125 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 363.27 E-value: 2.00e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLY 80
Cdd:PLN02979 50 ILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFETNDLAfspKGNFGDNSGLAEYVAQA 160
Cdd:PLN02979 129 VYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLG---KMDEANDSGLASYVAGQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 161 IDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDG 240
Cdd:PLN02979 206 IDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDG 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761924 241 GVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 305
Cdd:PLN02979 286 GVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISR 350
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
1-305 |
1.28e-124 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 361.36 E-value: 1.28e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPeALRWMQLY 80
Cdd:PLN02493 51 ILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPPQLRMKNFETNDLAfspKGNFGDNSGLAEYVAQA 160
Cdd:PLN02493 130 VYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLG---KMDEANDSGLASYVAGQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 161 IDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDG 240
Cdd:PLN02493 207 IDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDG 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761924 241 GVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDK 305
Cdd:PLN02493 287 GVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISR 351
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
1-309 |
9.67e-120 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 348.75 E-value: 9.67e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAeAGPEALRWMQLY 80
Cdd:PLN02535 53 VLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEVA-SSCNAVRFLQLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPpqlRMKNFETndlAFSPKGNFGDNSGLAEYVAQA 160
Cdd:PLN02535 132 VYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLGRREADIKNKMISP---QLKNFEG---LLSTEVVSDKGSGLEAFASET 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 161 IDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDG 240
Cdd:PLN02535 206 FDASLSWKDIEWLRSITNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDG 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761924 241 GVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVR 309
Cdd:PLN02535 286 GVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVR 354
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
2-301 |
1.22e-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: 329.94 E-value: 1.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 2 LRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPE-ALRWMQLY 80
Cdd:cd02922 46 LRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPDGELNLARAAGKHGILQMISTNASCSLEEIVDARPPdQPLFFQLY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKlppqlrmknfETNDLAFSPKGNFGDNSGLAEYVAQA 160
Cdd:cd02922 126 VNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRERDERLKAE----------EAVSDGPAGKKTKAKGGGAGRAMSGF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 161 IDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVE---AVEGKVEVF 237
Cdd:cd02922 196 IDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIRKhcpEVFDKIEVY 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958761924 238 LDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVK 301
Cdd:cd02922 276 VDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLGVTSLD 339
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
1-308 |
2.49e-112 |
|
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: 330.40 E-value: 2.49e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 1 MLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLY 80
Cdd:cd03332 66 MLRGVTERDLSVELFGRTLAAPLLLAPIGVQELFHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 81 IYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKlpPQLRMKNFE--TNDLAF------SPKGNFGDNSG 152
Cdd:cd03332 146 WPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLGWRPRDLDLGYL--PFLRGIGIAnyFSDPVFrkklaePVGEDPEAPPP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 153 LAEYVAQAI----DPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVE 228
Cdd:cd03332 224 MEAAVARFVsvfsGPSLTWEDLAFLREWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 229 AVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV 308
Cdd:cd03332 304 AVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
2-306 |
1.06e-100 |
|
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: 299.74 E-value: 1.06e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 2 LRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYI 81
Cdd:cd04737 54 LQGVESPDTSTELLGIKLKTPIIMAPIAAHGLAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYM 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 82 YKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPpqLRMKNFEtNDLAFSPKGnfgdnSGLAEYVAQAi 161
Cdd:cd04737 134 SKDDGFNRSLLDRAKAAGAKAIILTADATVGGNREADIRNKFQFP--FGMPNLN-HFSEGTGKG-----KGISEIYAAA- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 162 DPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDALPEIVEAVEGKVEVFLDGG 241
Cdd:cd04737 205 KQKLSPADIEFIAKISGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSG 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761924 242 VRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKT 306
Cdd:cd04737 285 VRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKRT 349
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
2-314 |
2.22e-82 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 253.79 E-value: 2.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 2 LRNVADIDLSTSVLGQRVSMPIC---VGATAMqcMAHvDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALrWMQ 78
Cdd:PRK11197 52 LKDMSDLSLETTLFGEKLSMPVAlapVGLTGM--YAR-RGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPM-WFQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 79 LYIYKDREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLPP-------QLRMKNFETNDLAFSPK----GN- 146
Cdd:PRK11197 128 LYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPGARYRDAHSGMSGPNaamrrylQAVTHPQWAWDVGLNGRphdlGNi 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 147 ---FGDNSGLAEYVAQA---IDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATI 220
Cdd:PRK11197 208 sayLGKPTGLEDYIGWLgnnFDPSISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 221 DALPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNV 300
Cdd:PRK11197 288 RALPAIADAVKGDITILADSGIRNGLDVVRMIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSI 367
|
330
....*....|....
gi 1958761924 301 KVIDKTLVRKNPLA 314
Cdd:PRK11197 368 SEITRDSLVQGNAA 381
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
2-305 |
1.27e-76 |
|
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: 238.58 E-value: 1.27e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 2 LRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALrWMQLYI 81
Cdd:cd04736 46 LVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPNGDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDL-WFQLYV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 82 YKdREVSSQLVKRAEQMGYKAIFVTVDTPYLGNRFDDVRNRFKLP--------------PQLRMKNFETNDLAfspKGNF 147
Cdd:cd04736 125 VH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRERDLRNGFAIPfrytprvlldgilhPRWLLRFLRNGMPQ---LANF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 148 G--DNSGLAEYVA---QAIDPSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILVSNHGARQLDGVPATIDA 222
Cdd:cd04736 201 AsdDAIDVEVQAAlmsRQMDASFNWQDLRWLRDLWPHKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 223 LPEIVEAVegKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKV 302
Cdd:cd04736 281 LAEIVAAT--YKPVLIDSGIRRGSDIVKALALGANAVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIAS 358
|
...
gi 1958761924 303 IDK 305
Cdd:cd04736 359 LTP 361
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
4-301 |
7.03e-19 |
|
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: 85.24 E-value: 7.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 4 NVADIDLSTSVLGQRVSMPICVGAtamqcM-------AHVDGELAtvRACQTMGTGMMLSS----------WATSSIeeV 66
Cdd:cd02811 36 DLDDIDLSTEFLGKRLSAPLLISA-----MtggsekaKEINRNLA--EAAEELGIAMGVGSqraaledpelAESFTV--V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 67 AEAGPEALRWMQLYIYKDREVSSQLVKRAEQM-GYKAIFVTVDtpylgnrfddvrnrfklPPQlrmknfEtndlAFSPKG 145
Cdd:cd02811 107 REAPPNGPLIANLGAVQLNGYGVEEARRAVEMiEADALAIHLN-----------------PLQ------E----AVQPEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 146 --NFgdnSGLaeyvaqaidpslsWDDIKWLRRLTSLPIVVK----GILRgDDAQEAVKHGVDGILVSNHG---------A 210
Cdd:cd02811 160 drDF---RGW-------------LERIEELVKALSVPVIVKevgfGISR-ETAKRLADAGVKAIDVAGAGgtswarvenY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 211 RQLD------------GVPaTIDALPEIVEAVEgKVEVFLDGGVRKGTDVLKALALGARAVFVGRPIIwGLAFQGEKGVQ 278
Cdd:cd02811 223 RAKDsdqrlaeyfadwGIP-TAASLLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVI 299
|
330 340
....*....|....*....|...
gi 1958761924 279 DVLEILKEEFRLAMALSGCQNVK 301
Cdd:cd02811 300 ETIEQIIEELRTAMFLTGAKNLA 322
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
152-263 |
6.06e-09 |
|
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: 54.90 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 152 GLAEYVAQAIDPSLSWDDIKWLR-RLTSLPIVVKGILRGDDAQEAVK-HGVDGILVSNHGARQLDGVPATIDALPEIVEA 229
Cdd:cd04722 87 GVEIHGAVGYLAREDLELIRELReAVPDVKVVVKLSPTGELAAAAAEeAGVDEVGLGNGGGGGGGRDAVPIADLLLILAK 166
|
90 100 110
....*....|....*....|....*....|....
gi 1958761924 230 VEGKVEVFLDGGVRKGTDVLKALALGARAVFVGR 263
Cdd:cd04722 167 RGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
180-264 |
1.37e-08 |
|
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: 55.42 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 180 PIVVK---GILRGDDAQEAVKHGVDGILVSNH----GA-----RQLDGVPaTIDALPEIVEAV--EG---KVEVFLDGGV 242
Cdd:pfam01645 204 PISVKlvsGHGVGTIAAGVAKAGADIILIDGYdggtGAspktsIKHAGLP-WELALAEAHQTLkeNGlrdRVSLIADGGL 282
|
90 100
....*....|....*....|..
gi 1958761924 243 RKGTDVLKALALGARAVFVGRP 264
Cdd:pfam01645 283 RTGADVAKAAALGADAVYIGTA 304
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
170-263 |
1.81e-08 |
|
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: 55.24 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 170 IKWLRRLT-SLPIVVK---GILRGDDAQEAVKHGVDGILVSNH----GARQLD-----GVPaTIDALPEIVEA-----VE 231
Cdd:cd02808 205 IEDLREATgGKPIGVKlvaGHGEGDIAAGVAAAGADFITIDGAeggtGAAPLTfidhvGLP-TELGLARAHQAlvkngLR 283
|
90 100 110
....*....|....*....|....*....|..
gi 1958761924 232 GKVEVFLDGGVRKGTDVLKALALGARAVFVGR 263
Cdd:cd02808 284 DRVSLIASGGLRTGADVAKALALGADAVGIGT 315
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
190-262 |
4.23e-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: 47.09 E-value: 4.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958761924 190 DDAQEAVKHGVDGILVSN-----HGARQLDGvpaTIDALPEIVEAVegKVEVFLDGGVRKGTDVLKALALGARAVFVG 262
Cdd:cd04730 113 EEARKAEAAGADALVAQGaeaggHRGTFDIG---TFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 185
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
192-262 |
1.58e-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: 45.87 E-value: 1.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958761924 192 AQEAVKHGVDGILVSNHGA---RQLDGVPaTIDALPEIVEAVegKVEVFLDGGVRKGTDVLKALALGARAVFVG 262
Cdd:COG2070 117 ARKAEKAGADAVVAEGAEAgghRGADEVS-TFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMG 187
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
170-264 |
6.66e-05 |
|
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: 44.05 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761924 170 IKWLRRL-TSLPIVVKGILRGDDAQEAVKHGVDGILV-----SNHGARQLDGV--P-ATidALPEIVEAVEG-KVEVFLD 239
Cdd:cd00381 126 IKFIKKKyPNVDVIAGNVVTAEAARDLIDAGADGVKVgigpgSICTTRIVTGVgvPqAT--AVADVAAAARDyGVPVIAD 203
|
90 100
....*....|....*....|....*
gi 1958761924 240 GGVRKGTDVLKALALGARAVFVGRP 264
Cdd:cd00381 204 GGIRTSGDIVKALAAGADAVMLGSL 228
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
163-205 |
9.97e-03 |
|
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.
Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 36.37 E-value: 9.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1958761924 163 PSLSWDDIKWLRRLTSLPIVVKGILRGDDAQEAVKHGVDGILV 205
Cdd:pfam02581 134 PPLGLEGLKAIAEAVEIPVVAIGGITPENVPEVIEAGADGVAV 176
|
|
| |
