|
Name |
Accession |
Description |
Interval |
E-value |
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
25-374 |
0e+00 |
|
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: 574.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 25 YDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNP 104
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 105 lEGEKDVARGCGQGvtKVPQMISTLASCSPEEIIEAAPSDkQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPS 184
Cdd:cd02922 81 -DGELNLARAAGKH--GILQMISTNASCSLEEIVDARPPD-QPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 185 LGQKEKDMKLKFSNTKAGFKAMKKTNvEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGV 264
Cdd:cd02922 157 LGKRERDERLKAEEAVSDGPAGKKTK-AKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 265 SGVVLSNHGGRQLDFSRAPIEVLAETMPILEQrnLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRN 344
Cdd:cd02922 236 DGIVLSNHGGRQLDTAPAPIEVLLEIRKHCPE--VFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEE 313
|
330 340 350
....*....|....*....|....*....|
gi 5107653 345 GVEKAIEILRDEIEMSMRLLGVTSIAELKP 374
Cdd:cd02922 314 GVEKAIQILKDEIETTMRLLGVTSLDQLGP 343
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
31-379 |
8.29e-157 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 445.82 E-value: 8.29e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 31 ASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPlEGEKD 110
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHP-DGELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 111 VARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQKEK 190
Cdd:pfam01070 80 LARAAAA--AGIPFVLSTVSSTSLEEVAAAAGGPL---WFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 191 DMKLKFS---------NTKAGFKAMKKTNVEESQGASRA---LSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIK 258
Cdd:pfam01070 155 DLRNGFTlpprltprnLLDLALHPRWALGVLRRGGAGGAaafVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 259 AAEIGVSGVVLSNHGGRQLDFSRAPIEVLAEtmpILEQrnLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYAN 338
Cdd:pfam01070 235 AVEAGVDGIVVSNHGGRQLDGAPATIDALPE---IVAA--VGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 5107653 339 SCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLLDL 379
Cdd:pfam01070 310 AAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
18-377 |
1.46e-128 |
|
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: 374.47 E-value: 1.46e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 18 LDNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATA 97
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 98 LCKLGNPlEGEKDVARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVNSDRKITDDLVKNVEKLGVKALF 177
Cdd:COG1304 81 GGGLAHP-DGELALARAAAA--AGIPMGLSTQSTTSLEEVAAAAPAPL---WFQLYVPKDRGFTDDLLRRAEAAGADALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 178 VTVDAPSLGQKEKDMKLKFS-------NTKAGFkAMKKTNVEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGV 250
Cdd:COG1304 155 LTVDTPVLGRRERDLREGFSqpprltpRNLLEA-ATHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 251 QRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMpileqRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGL 330
Cdd:COG1304 234 LSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIR-----AAVGGRIPVIADGGIRRGLDVAKALALGADAVGL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 5107653 331 GRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLL 377
Cdd:COG1304 309 GRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
19-372 |
9.25e-99 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 298.67 E-value: 9.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 19 DNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATAL 98
Cdd:PLN02535 3 DEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 99 CKLGNPlEGEKDVARGCGQGVTKVpqMISTLASCSPEEIieaAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFV 178
Cdd:PLN02535 83 HKLAHP-EGEIATARAAAACNTIM--VLSFMASCTVEEV---ASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 179 TVDAPSLGQKEKDMKLK-FSNTKAGFKAMKKTNVEESQGAS-RAL-SKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTED 255
Cdd:PLN02535 157 TADVPRLGRREADIKNKmISPQLKNFEGLLSTEVVSDKGSGlEAFaSETFDASLSWKDIEWLRSITNLPILIKGVLTRED 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 256 VIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMpileqRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFL 335
Cdd:PLN02535 237 AIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVV-----QAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVI 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 5107653 336 YANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAEL 372
Cdd:PLN02535 312 YGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDI 348
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
25-374 |
0e+00 |
|
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: 574.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 25 YDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNP 104
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 105 lEGEKDVARGCGQGvtKVPQMISTLASCSPEEIIEAAPSDkQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPS 184
Cdd:cd02922 81 -DGELNLARAAGKH--GILQMISTNASCSLEEIVDARPPD-QPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 185 LGQKEKDMKLKFSNTKAGFKAMKKTNvEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGV 264
Cdd:cd02922 157 LGKRERDERLKAEEAVSDGPAGKKTK-AKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 265 SGVVLSNHGGRQLDFSRAPIEVLAETMPILEQrnLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRN 344
Cdd:cd02922 236 DGIVLSNHGGRQLDTAPAPIEVLLEIRKHCPE--VFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEE 313
|
330 340 350
....*....|....*....|....*....|
gi 5107653 345 GVEKAIEILRDEIEMSMRLLGVTSIAELKP 374
Cdd:cd02922 314 GVEKAIQILKDEIETTMRLLGVTSLDQLGP 343
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
31-379 |
8.29e-157 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 445.82 E-value: 8.29e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 31 ASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPlEGEKD 110
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHP-DGELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 111 VARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQKEK 190
Cdd:pfam01070 80 LARAAAA--AGIPFVLSTVSSTSLEEVAAAAGGPL---WFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 191 DMKLKFS---------NTKAGFKAMKKTNVEESQGASRA---LSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIK 258
Cdd:pfam01070 155 DLRNGFTlpprltprnLLDLALHPRWALGVLRRGGAGGAaafVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 259 AAEIGVSGVVLSNHGGRQLDFSRAPIEVLAEtmpILEQrnLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYAN 338
Cdd:pfam01070 235 AVEAGVDGIVVSNHGGRQLDGAPATIDALPE---IVAA--VGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 5107653 339 SCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLLDL 379
Cdd:pfam01070 310 AAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
25-374 |
5.24e-137 |
|
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: 393.74 E-value: 5.24e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 25 YDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNP 104
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 105 lEGEKDVARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPS 184
Cdd:cd02809 81 -DGELATARAAAA--AGIPFTLSTVSTTSLEEVAAAAPGPR---WFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 185 LGQKekdmklkfsntkagfkamkktnveesqgasralskfidpsLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGV 264
Cdd:cd02809 155 LGRR----------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 265 SGVVLSNHGGRQLDFSRAPIEVLAETMpileqRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRN 344
Cdd:cd02809 195 DGIVVSNHGGRQLDGAPATIDALPEIV-----AAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEA 269
|
330 340 350
....*....|....*....|....*....|
gi 5107653 345 GVEKAIEILRDEIEMSMRLLGVTSIAELKP 374
Cdd:cd02809 270 GVAHVLEILRDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
18-377 |
1.46e-128 |
|
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: 374.47 E-value: 1.46e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 18 LDNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATA 97
Cdd:COG1304 1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 98 LCKLGNPlEGEKDVARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVNSDRKITDDLVKNVEKLGVKALF 177
Cdd:COG1304 81 GGGLAHP-DGELALARAAAA--AGIPMGLSTQSTTSLEEVAAAAPAPL---WFQLYVPKDRGFTDDLLRRAEAAGADALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 178 VTVDAPSLGQKEKDMKLKFS-------NTKAGFkAMKKTNVEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGV 250
Cdd:COG1304 155 LTVDTPVLGRRERDLREGFSqpprltpRNLLEA-ATHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 251 QRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMpileqRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGL 330
Cdd:COG1304 234 LSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIR-----AAVGGRIPVIADGGIRRGLDVAKALALGADAVGL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 5107653 331 GRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLL 377
Cdd:COG1304 309 GRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
19-372 |
9.25e-99 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 298.67 E-value: 9.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 19 DNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATAL 98
Cdd:PLN02535 3 DEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 99 CKLGNPlEGEKDVARGCGQGVTKVpqMISTLASCSPEEIieaAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFV 178
Cdd:PLN02535 83 HKLAHP-EGEIATARAAAACNTIM--VLSFMASCTVEEV---ASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 179 TVDAPSLGQKEKDMKLK-FSNTKAGFKAMKKTNVEESQGAS-RAL-SKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTED 255
Cdd:PLN02535 157 TADVPRLGRREADIKNKmISPQLKNFEGLLSTEVVSDKGSGlEAFaSETFDASLSWKDIEWLRSITNLPILIKGVLTRED 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 256 VIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMpileqRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFL 335
Cdd:PLN02535 237 AIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVV-----QAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVI 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 5107653 336 YANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAEL 372
Cdd:PLN02535 312 YGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDI 348
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
23-377 |
2.01e-95 |
|
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: 290.72 E-value: 2.01e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 23 NLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLG 102
Cdd:cd03332 20 DPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 103 NPlEGEKDVARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKQiqWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDA 182
Cdd:cd03332 100 HP-DAELATARAAAE--LGVPYILSTASSSSIEDVAAAAGDAPR--WFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 183 PSLGQKEKDMKLK-------------FSNT--KAGFKAMKKTNVEE--SQGASRA--LSKFIDPSLTWKDIEELKKKTKL 243
Cdd:cd03332 175 WSLGWRPRDLDLGylpflrgigianyFSDPvfRKKLAEPVGEDPEAppPMEAAVArfVSVFSGPSLTWEDLAFLREWTDL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 244 PIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAEtmpILEQrnLKDKLEVFVDGGVRRGTDVLKALCL 323
Cdd:cd03332 255 PIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPE---IVEA--VGDRLTVLFDSGVRTGADIMKALAL 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 5107653 324 GAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLL 377
Cdd:cd03332 330 GAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
21-372 |
1.16e-86 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 268.14 E-value: 1.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 21 IINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCK 100
Cdd:PLN02493 3 ITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 101 LGNPlEGEKDVARGCGQGVTkvpqmISTLASCSPEEIIEAAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTV 180
Cdd:PLN02493 83 MAHP-DGEYATARAASAAGT-----IMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 181 DAPSLGQKEKDMKLKFSN----TKAGFKAMKKTNVEESQ--GASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTE 254
Cdd:PLN02493 157 DTPRLGRRESDIKNRFTLppnlTLKNFEGLDLGKMDEANdsGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 255 DVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMPILEQRnlkdkLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPF 334
Cdd:PLN02493 237 DARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGR-----IPVFLDGGVRRGTDVFKALALGASGIFIGRPV 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 5107653 335 LYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAEL 372
Cdd:PLN02493 312 VFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEI 349
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
21-373 |
2.52e-76 |
|
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: 240.81 E-value: 2.52e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 21 IINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCK 100
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 101 LGNPlEGEKDVARGCGQGVTKVPqmISTLASCSPEEIIEAAPsdKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTV 180
Cdd:cd04737 85 LAHA-TGEVATARGMAEVGSLFS--ISTYSNTSLEEIAKASN--GGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 181 DAPSLGQKEKDMKLKFSnTKAGFKAMKKTNVEESQGAS----RALSKfidPSLTWKDIEELKKKTKLPIVIKGVQRTEDV 256
Cdd:cd04737 160 DATVGGNREADIRNKFQ-FPFGMPNLNHFSEGTGKGKGiseiYAAAK---QKLSPADIEFIAKISGLPVIVKGIQSPEDA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 257 IKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAEtmpILEQRNlkDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLY 336
Cdd:cd04737 236 DVAINAGADGIWVSNHGGRQLDGGPASFDSLPE---IAEAVN--HRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLY 310
|
330 340 350
....*....|....*....|....*....|....*..
gi 5107653 337 ANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELK 373
Cdd:cd04737 311 GLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVK 347
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
65-372 |
2.76e-70 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 225.76 E-value: 2.76e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 65 FKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPlEGEKDVARGCGQGVTkvpqmISTLASCSPEEIIEAAPSD 144
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHP-DGEYATARAASAAGT-----IMTLSSWATSSVEEVASTG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 145 KQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQKEKDMKLKFSN----TKAGFKAMKKTNVEESQ--GAS 218
Cdd:PLN02979 120 PGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLppnlTLKNFEGLDLGKMDEANdsGLA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 219 RALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMPILEQRn 298
Cdd:PLN02979 200 SYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGR- 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5107653 299 lkdkLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAEL 372
Cdd:PLN02979 279 ----IPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEI 348
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
26-374 |
6.25e-67 |
|
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: 217.01 E-value: 6.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 26 DFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPl 105
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 106 EGEKDVARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVnSDRKITDDLVKNVEKLGVKALFVTVDAPSL 185
Cdd:cd04736 81 NGDLALARAAAK--AGIPFVLSTASNMSIEDVARQADGDL---WFQLYV-VHRELAELLVKRALAAGYTTLVLTTDVAVN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 186 GQKEKDMKLKFS----------------------------NTKAGFKAMKKTNVEeSQGAsrALSKFIDPSLTWKDIEEL 237
Cdd:cd04736 155 GYRERDLRNGFAipfrytprvlldgilhprwllrflrngmPQLANFASDDAIDVE-VQAA--LMSRQMDASFNWQDLRWL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 238 KKKTKLPIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMpileQRNLKDkleVFVDGGVRRGTDV 317
Cdd:cd04736 232 RDLWPHKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIV----AATYKP---VLIDSGIRRGSDI 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 5107653 318 LKALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKP 374
Cdd:cd04736 305 VKALALGANAVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
26-377 |
1.07e-60 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 201.02 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 26 DFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLgNPL 105
Cdd:PRK11197 8 DYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGM-YAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 106 EGEKDVARGCGQgvTKVPQMISTLASCSPEEIieaAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSL 185
Cdd:PRK11197 87 RGEVQAARAADA--KGIPFTLSTVSVCPIEEV---APAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 186 GQKEKDMKLKFSNTKAG----FKAMKKT----------------NVEESQGASRALSKFI-------DPSLTWKDIEELK 238
Cdd:PRK11197 162 GARYRDAHSGMSGPNAAmrryLQAVTHPqwawdvglngrphdlgNISAYLGKPTGLEDYIgwlgnnfDPSISWKDLEWIR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 239 KKTKLPIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAetmPILEQrnLKDKLEVFVDGGVRRGTDVL 318
Cdd:PRK11197 242 DFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALP---AIADA--VKGDITILADSGIRNGLDVV 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 5107653 319 KALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLL 377
Cdd:PRK11197 317 RMIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
91-332 |
1.43e-19 |
|
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: 86.10 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 91 FYVSATALCKLGNPLEgekdVARGCGQGvTKVPQMISTLASCSPEE-------IIEAAPSDKQIQWYQLYVNSDRKITDD 163
Cdd:cd04722 1 VILALLAGGPSGDPVE----LAKAAAEA-GADAIIVGTRSSDPEEAetddkevLKEVAAETDLPLGVQLAINDAAAAVDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 164 LVKNVEKLGVKALFVTVDAPSLgqkekdmklkfsntkagfkamkktnveesqgasralskfidPSLTWKDIEELKKKT-K 242
Cdd:cd04722 76 AAAAARAAGADGVEIHGAVGYL-----------------------------------------AREDLELIRELREAVpD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 243 LPIVIKGVQRTEDV-IKAAEIGVSGVVLSNHGGRQLDFSRAPIevlaeTMPILEQRNLKDKLEVFVDGGVRRGTDVLKAL 321
Cdd:cd04722 115 VKVVVKLSPTGELAaAAAEEAGVDEVGLGNGGGGGGGRDAVPI-----ADLLLILAKRGSKVPVIAGGGINDPEDAAEAL 189
|
250
....*....|.
gi 5107653 322 CLGAKGVGLGR 332
Cdd:cd04722 190 ALGADGVIVGS 200
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
234-373 |
1.66e-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: 88.71 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 234 IEELKKKTKLPIVIK----GVQRtEDVIKAAEIGVSGVVLSNHGGrqLDFSRapIEV---------LAET-----MP--- 292
Cdd:cd02811 170 IEELVKALSVPVIVKevgfGISR-ETAKRLADAGVKAIDVAGAGG--TSWAR--VENyrakdsdqrLAEYfadwgIPtaa 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 293 -ILEQRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYAnSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAE 371
Cdd:cd02811 245 sLLEVRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKA-ALEGEEAVIETIEQIIEELRTAMFLTGAKNLAE 323
|
..
gi 5107653 372 LK 373
Cdd:cd02811 324 LK 325
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
234-379 |
7.38e-12 |
|
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: 66.41 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 234 IEELKKKT-KLPIVIK-----GVQRTEDVIKAAE---IGVSG---------VVLSNHGGRqldfsraPIEV-LAETMPIL 294
Cdd:cd02808 205 IEDLREATgGKPIGVKlvaghGEGDIAAGVAAAGadfITIDGaeggtgaapLTFIDHVGL-------PTELgLARAHQAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 295 EQRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYA-----------NSC-YG----------RNGVEKA--- 349
Cdd:cd02808 278 VKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIAlgciqarkchtNTCpVGvatqdpelrrRLDVEGKaer 357
|
170 180 190
....*....|....*....|....*....|....*
gi 5107653 350 ----IEILRDEIEMSMRLLGVTSIAELKP-DLLDL 379
Cdd:cd02808 358 vanyLKSLAEELRELAAALGKRSLELLGRsDLLAL 392
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
234-340 |
3.90e-11 |
|
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: 63.89 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 234 IEELKKKT-KLPIVIK-GVQRTEDVIKA--AEIGVSGVVLSNHGG-------RQLDFSRAPIEV-LAETMPILEQRNLKD 301
Cdd:pfam01645 193 IYDLKEINpKAPISVKlVSGHGVGTIAAgvAKAGADIILIDGYDGgtgaspkTSIKHAGLPWELaLAEAHQTLKENGLRD 272
|
90 100 110
....*....|....*....|....*....|....*....
gi 5107653 302 KLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSC 340
Cdd:pfam01645 273 RVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGC 311
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
248-337 |
2.12e-06 |
|
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439839 Cd Length: 728 Bit Score: 49.86 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 248 KGVQRTEdvIKAAEIGVSG---------VVLSNHGGrqldfsrAPIEV-LAETMPILEQRNLKDKLEVFVDGGVRRGTDV 317
Cdd:COG0069 385 KGVAKTG--AYADFITIDGgeggtgaapLESIKHAG-------LPWELgLAEVHQTLVGNGLRDRIRLIADGKLKTGRDV 455
|
90 100
....*....|....*....|
gi 5107653 318 LKALCLGAKGVGLGRPFLYA 337
Cdd:COG0069 456 AIAAALGADEFGFARAFMVA 475
|
|
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
287-379 |
2.40e-05 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 46.79 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 287 LAETMPILEQRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSC-YGR--------NGVEKAIEILRDE- 356
Cdd:PRK11750 1052 LAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCkYLRichlnncaTGVATQDEKLRKNh 1131
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 5107653 357 ----IEMS--------------MRLLGVTSIAEL--KPDLLDL 379
Cdd:PRK11750 1132 yhglPEMVmnyfefiaeetrewMAQLGVRSLEDLigRTDLLEE 1174
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
254-335 |
1.70e-03 |
|
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: 39.77 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5107653 254 EDVIKAAEIGVSGVVLSNH--GGRQLDFSRAPIEVLAEtmpileqrnLKDKLEVFV--DGGVRRGTDVLKALCLGAKGVG 329
Cdd:cd04730 113 EEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPE---------VRDAVDIPViaAGGIADGRGIAAALALGADGVQ 183
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....*.
gi 5107653 330 LGRPFL 335
Cdd:cd04730 184 MGTRFL 189
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