|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
13-349 |
3.58e-171 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 480.11 E-value: 3.58e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 13 AREHLSKSTWDFIEGGADDCCTRDENMAAFKKIRLRPRYLKDVSKVDMRTTIQGAEISAPICIAPTGFHRLAWPDGEMST 92
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 93 ARAAQAASICYITSTYASCSLEDIVAAAPrGLRWFQLYVHPNRQINKQMIQKVESLGFKALVITVDVPKVGNRRNDITN- 171
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAG-GPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 172 -------------QVDLMKKLLLKDLGSPEMGNVMPYFQMSpIDPSICWEDLSWFQSMTRLPIILKGILTKEDAELAVKH 238
Cdd:pfam01070 160 ftlpprltprnllDLALHPRWALGVLRRGGAGGAAAFVGSQ-FDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 239 NVHGIIVSNHGGRQLDEVPASIDALTEVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGRPILWGLAYKGEHGVK 318
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVA 318
|
330 340 350
....*....|....*....|....*....|.
gi 78050047 319 EVLDILKNEFHTSMTLTGCRSVAEINQDLIQ 349
Cdd:pfam01070 319 HALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
8-345 |
4.46e-169 |
|
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: 472.70 E-value: 4.46e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 8 DFREHAREHLSKSTWDFIEGGADDCCTRDENMAAFKKIRLRPRYLKDVSKVDMRTTIQGAEISAPICIAPTGFHRLAWPD 87
Cdd:cd02809 2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 88 GEMSTARAAQAASICYITSTYASCSLEDIVAAAPrGLRWFQLYVHPNRQINKQMIQKVESLGFKALVITVDVPKVGNRrn 167
Cdd:cd02809 82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 168 ditnqvdlmkklllkdlgspemgnvmpyfqmspidpsICWEDLSWFQSMTRLPIILKGILTKEDAELAVKHNVHGIIVSN 247
Cdd:cd02809 159 -------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVVSN 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 248 HGGRQLDEVPASIDALTEVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGRPILWGLAYKGEHGVKEVLDILKNE 327
Cdd:cd02809 202 HGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEILRDE 281
|
330
....*....|....*...
gi 78050047 328 FHTSMTLTGCRSVAEINQ 345
Cdd:cd02809 282 LERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
1-348 |
1.74e-150 |
|
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: 428.01 E-value: 1.74e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 1 MP-LVCLTDFREHAREHLSKSTWDFIEGGADDCCTRDENMAAFKKIRLRPRYLKDVSKVDMRTTIQGAEISAPICIAPTG 79
Cdd:COG1304 1 MSrILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 80 FHRLAWPDGEMSTARAAQAASICYITSTYASCSLEDiVAAAPRGLRWFQLYVHPNRQINKQMIQKVESLGFKALVITVDV 159
Cdd:COG1304 81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEE-VAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 160 PKVGNRRNDITNQV--------DLMKKLLLKDLGSPEMGNVMPYFQMSpIDPSICWEDLSWFQSMTRLPIILKGILTKED 231
Cdd:COG1304 160 PVLGRRERDLREGFsqpprltpRNLLEAATHPRWALGLASLAAWLDTN-FDPSLTWDDIAWLRERWPGPLIVKGVLSPED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 232 AELAVKHNVHGIIVSNHGGRQLDEVPASIDALTEVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGRPILWGLAY 311
Cdd:COG1304 239 ARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAA 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 78050047 312 KGEHGVKEVLDILKNEFHTSMTLTGCRSVAEINQDLI 348
Cdd:COG1304 319 GGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
8-344 |
7.89e-135 |
|
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: 387.72 E-value: 7.89e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 8 DFREHAREHLSKSTWDFIEGGADDCCTRDENMAAFKKIRLRPRYLKDVSKVDMRTTIQGAEISAPICIAPTGFHRLAWPD 87
Cdd:cd02922 2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 88 GEMSTARAAQAASICYITSTYASCSLEDIVAAAPRGL-RWFQLYVHPNRQINKQMIQKVESLGFKALVITVDVPKVGNRR 166
Cdd:cd02922 82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQpLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 167 NDITNQVDLMKKLLLKDLGSPEMGNVMPYFQMSPIDPSICWEDLSWFQSMTRLPIILKGILTKEDAELAVKHNVHGIIVS 246
Cdd:cd02922 162 RDERLKAEEAVSDGPAGKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 247 NHGGRQLDEVPASIDALTEVV---AAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGRPILWGLAYKGEHGVKEVLDI 323
Cdd:cd02922 242 NHGGRQLDTAPAPIEVLLEIRkhcPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKAIQI 321
|
330 340
....*....|....*....|.
gi 78050047 324 LKNEFHTSMTLTGCRSVAEIN 344
Cdd:cd02922 322 LKDEIETTMRLLGVTSLDQLG 342
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
4-352 |
1.53e-129 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 374.94 E-value: 1.53e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 4 VCLTDFREHAREHLSKSTWDFIEGGADDCCTRDENMAAFKKIRLRPRYLKDVSKVDMRTTIQGAEISAPICIAPTGFHRL 83
Cdd:PLN02535 6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 84 AWPDGEMSTARAAQAASICYITSTYASCSLEDiVAAAPRGLRWFQLYVHPNRQINKQMIQKVESLGFKALVITVDVPKVG 163
Cdd:PLN02535 86 AHPEGEIATARAAAACNTIMVLSFMASCTVEE-VASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 164 NRRNDITNQVDLMKKLLLKDLGSPEM----GNVMPYFQMSPIDPSICWEDLSWFQSMTRLPIILKGILTKEDAELAVKHN 239
Cdd:PLN02535 165 RREADIKNKMISPQLKNFEGLLSTEVvsdkGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLTREDAIKAVEVG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 240 VHGIIVSNHGGRQLDEVPASIDALTEVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGRPILWGLAYKGEHGVKE 319
Cdd:PLN02535 245 VAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDGVRK 324
|
330 340 350
....*....|....*....|....*....|...
gi 78050047 320 VLDILKNEFHTSMTLTGCRSVAEINQDLIQFSR 352
Cdd:PLN02535 325 VIEMLKDELEITMALSGCPSVKDITRSHVRTER 357
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
1-348 |
3.73e-114 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 335.93 E-value: 3.73e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 1 MPLVCLTDFREHAREHLSKSTWDFIEGGADDCCTRDENMAAFKKIRLRPRYLKDVSKVDMRTTIQGAEISAPICIAPTGF 80
Cdd:PLN02493 1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 81 HRLAWPDGEMSTARAAQAASICYITSTYASCSLEDIVAAAPrGLRWFQLYVHPNRQINKQMIQKVESLGFKALVITVDVP 160
Cdd:PLN02493 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 161 KVGNRRNDITNQVDLMKKLLLKDLGSPEMGNV-------MPYFQMSPIDPSICWEDLSWFQSMTRLPIILKGILTKEDAE 233
Cdd:PLN02493 160 RLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMdeandsgLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 234 LAVKHNVHGIIVSNHGGRQLDEVPASIDALTEVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGRPILWGLAYKG 313
Cdd:PLN02493 240 IAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEG 319
|
330 340 350
....*....|....*....|....*....|....*
gi 78050047 314 EHGVKEVLDILKNEFHTSMTLTGCRSVAEINQDLI 348
Cdd:PLN02493 320 EAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 354
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
4-348 |
8.04e-114 |
|
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: 335.79 E-value: 8.04e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 4 VCLTDFREHAREHLSKSTWDFIEGGADDCCTRDENMAAFKKIRLRPRYLKDVSKVDMRTTIQGAEISAPICIAPTGFHRL 83
Cdd:cd03332 19 VDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 84 AWPDGEMSTARAAQAASICYITSTYASCSLEDIVAAAPRGLRWFQLYVHPNRQINKQMIQKVESLGFKALVITVDVPKVG 163
Cdd:cd03332 99 FHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 164 NRRNDITN--------------------QVDLMKKLLLKDLGSPEMGNVMPYFQMSPIDPSICWEDLSWFQSMTRLPIIL 223
Cdd:cd03332 179 WRPRDLDLgylpflrgigianyfsdpvfRKKLAEPVGEDPEAPPPMEAAVARFVSVFSGPSLTWEDLAFLREWTDLPIVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 224 KGILTKEDAELAVKHNVHGIIVSNHGGRQLDEVPASIDALTEVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGR 303
Cdd:cd03332 259 KGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGR 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 78050047 304 PILWGLAYKGEHGVKEVLDILKNEFHTSMTLTGCRSVAEINQDLI 348
Cdd:cd03332 339 PYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
47-348 |
1.99e-101 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 303.57 E-value: 1.99e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 47 LRPRYLKDVSKVDMRTTIQGAEISAPICIAPTGFHRLAWPDGEMSTARAAQAASICYITSTYASCSLEDIVAAAPrGLRW 126
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 127 FQLYVHPNRQINKQMIQKVESLGFKALVITVDVPKVGNRRNDITNQVDLMKKLLLKDLGSPEMGNV-------MPYFQMS 199
Cdd:PLN02979 125 FQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMdeandsgLASYVAG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 200 PIDPSICWEDLSWFQSMTRLPIILKGILTKEDAELAVKHNVHGIIVSNHGGRQLDEVPASIDALTEVVAAVKGKVEVYLD 279
Cdd:PLN02979 205 QIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLD 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78050047 280 GGIRTGNDVLKALALGAKCVFVGRPILWGLAYKGEHGVKEVLDILKNEFHTSMTLTGCRSVAEINQDLI 348
Cdd:PLN02979 285 GGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHI 353
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
3-345 |
1.40e-99 |
|
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: 298.20 E-value: 1.40e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 3 LVCLTDFREHAREHLSKSTWDFIEGGADDCCTRDENMAAFKKIRLRPRYLKDVSKVDMRTTIQGAEISAPICIAPTGFHR 82
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 83 LAWPDGEMSTARAAQAASICYITSTYASCSLEDIVAAAPRGLRWFQLYVHPNRQINKQMIQKVESLGFKALVITVDVPKV 162
Cdd:cd04737 85 LAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 163 GNRRNDITNQ-VDLMKKLLLKDLGSPEMGNVMPYFQMSPIDPSICWEDLSWFQSMTRLPIILKGILTKEDAELAVKHNVH 241
Cdd:cd04737 165 GNREADIRNKfQFPFGMPNLNHFSEGTGKGKGISEIYAAAKQKLSPADIEFIAKISGLPVIVKGIQSPEDADVAINAGAD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 242 GIIVSNHGGRQLDEVPASIDALTEVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGRPILWGLAYKGEHGVKEVL 321
Cdd:cd04737 245 GIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGVASVL 324
|
330 340
....*....|....*....|....
gi 78050047 322 DILKNEFHTSMTLTGCRSVAEINQ 345
Cdd:cd04737 325 EHLNKELKIVMQLAGTRTIEDVKR 348
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
8-344 |
1.36e-92 |
|
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: 280.95 E-value: 1.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 8 DFREHAREHLSKSTWDFIEGGADDCCTRDENMAAFKKIRLRPRYLKDVSKVDMRTTIQGAEISAPICIAPTGFHRLAWPD 87
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 88 GEMSTARAAQAASICYITSTYASCSLEDiVAAAPRGLRWFQLYVhPNRQINKQMIQKVESLGFKALVITVDVPKVGNRRN 167
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIED-VARQADGDLWFQLYV-VHRELAELLVKRALAAGYTTLVLTTDVAVNGYRER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 168 DITNQVDLMKKLLLKDL----------------GSPEMGN-VMPYFQ--------MS-PIDPSICWEDLSWFQSMTRLPI 221
Cdd:cd04736 160 DLRNGFAIPFRYTPRVLldgilhprwllrflrnGMPQLANfASDDAIdvevqaalMSrQMDASFNWQDLRWLRDLWPHKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 222 ILKGILTKEDAELAVKHNVHGIIVSNHGGRQLDEVPASIDALTEVVAAVkgKVEVYLDGGIRTGNDVLKALALGAKCVFV 301
Cdd:cd04736 240 LVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAAT--YKPVLIDSGIRRGSDIVKALALGANAVLL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 78050047 302 GRPILWGLAYKGEHGVKEVLDILKNEFHTSMTLTGCRSVAEIN 344
Cdd:cd04736 318 GRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLT 360
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
1-348 |
5.50e-92 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 279.99 E-value: 5.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 1 MPLVCLTDFREHAREHLSKSTWDFIEGGADDCCTRDENMAAFKKIRLRPRYLKDVSKVDMRTTIQGAEISAPICIAPTGF 80
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 81 HRLAWPDGEMSTARAAQAASICYITSTYASCSLEDIVAAAPRGLrWFQLYVHPNRQINKQMIQKVESLGFKALVITVDVP 160
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPM-WFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 161 KVGNRRNDITNQVDLMKKLLLKD---------------LGSP-EMGNVMPYFQmSPI-------------DPSICWEDLS 211
Cdd:PRK11197 160 VPGARYRDAHSGMSGPNAAMRRYlqavthpqwawdvglNGRPhDLGNISAYLG-KPTgledyigwlgnnfDPSISWKDLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 212 WFQSMTRLPIILKGILTKEDAELAVKHNVHGIIVSNHGGRQLDEVPASIDALTEVVAAVKGKVEVYLDGGIRTGNDVLKA 291
Cdd:PRK11197 239 WIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRM 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 78050047 292 LALGAKCVFVGRPILWGLAYKGEHGVKEVLDILKNEFHTSMTLTGCRSVAEINQDLI 348
Cdd:PRK11197 319 IALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
220-342 |
4.07e-18 |
|
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: 83.70 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 220 PIILK----GIlTKEDAELAVKHNVHGIIVSNHGG---------RQLDEVPASID-----------ALTEVVAAVKgKVE 275
Cdd:cd02811 180 PVIVKevgfGI-SRETAKRLADAGVKAIDVAGAGGtswarvenyRAKDSDQRLAEyfadwgiptaaSLLEVRSALP-DLP 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78050047 276 VYLDGGIRTGNDVLKALALGAKCVFVGRPILwGLAYKGEHGVKEVLDILKNEFHTSMTLTGCRSVAE 342
Cdd:cd02811 258 LIASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVIETIEQIIEELRTAMFLTGAKNLAE 323
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
93-303 |
2.92e-10 |
|
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: 59.14 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 93 ARAAQAASICYITSTYASCSLEDI---------VAAAPRGLRWFQLYVHPNRQINKQMIQKVESLGFKALVITVDVPKVg 163
Cdd:cd04722 19 KAAAEAGADAIIVGTRSSDPEEAEtddkevlkeVAAETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 164 nrrnditnqvdlmkklllkdlgspemgnvmpyfqmspidPSICWEDLSWF-QSMTRLPIILKGILT-KEDAELAVKHNVH 241
Cdd:cd04722 98 ---------------------------------------AREDLELIRELrEAVPDVKVVVKLSPTgELAAAAAEEAGVD 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78050047 242 GIIVSNHGGRQLDEVPASIDALTEVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGR 303
Cdd:cd04722 139 EVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
220-303 |
3.66e-06 |
|
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: 48.31 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 220 PIILK---GILTKEDAELAVKHNVHGIIVSNHGG-------RQLDEV--PaSIDALTEVV-----AAVKGKVEVYLDGGI 282
Cdd:cd02808 216 PIGVKlvaGHGEGDIAAGVAAAGADFITIDGAEGgtgaaplTFIDHVglP-TELGLARAHqalvkNGLRDRVSLIASGGL 294
|
90 100
....*....|....*....|.
gi 78050047 283 RTGNDVLKALALGAKCVFVGR 303
Cdd:cd02808 295 RTGADVAKALALGADAVGIGT 315
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
235-306 |
1.51e-05 |
|
Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.
Pssm-ID: 396287 [Multi-domain] Cd Length: 367 Bit Score: 46.17 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 235 AVKHNVHGIIVSNHGGRQLDEVPASID--------ALTEVVAAVK-----GKVEVYLDGGIRTGNDVLKALALGAKCVFV 301
Cdd:pfam01645 222 VAKAGADIILIDGYDGGTGASPKTSIKhaglpwelALAEAHQTLKenglrDRVSLIADGGLRTGADVAKAAALGADAVYI 301
|
....*
gi 78050047 302 GRPIL 306
Cdd:pfam01645 302 GTAAL 306
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
262-304 |
6.21e-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: 44.43 E-value: 6.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 78050047 262 ALTEVVAAVKG-KVEVYLDGGIRTGNDVLKALALGAKCVFVGRP 304
Cdd:cd00381 185 AVADVAAAARDyGVPVIADGGIRTSGDIVKALAAGADAVMLGSL 228
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
228-302 |
2.33e-04 |
|
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: 42.09 E-value: 2.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78050047 228 TKEDAELAVKHNVHGIIVSNH--GGRQLDEVPASIDALTEVVAAVKgkVEVYLDGGIRTGNDVLKALALGAKCVFVG 302
Cdd:cd04730 111 SVEEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGADGVQMG 185
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
279-303 |
2.54e-04 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 42.65 E-value: 2.54e-04
10 20
....*....|....*....|....*
gi 78050047 279 DGGIRTGNDVLKALALGAKCVFVGR 303
Cdd:PTZ00314 350 DGGIKNSGDICKALALGADCVMLGS 374
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
262-303 |
6.35e-04 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 41.61 E-value: 6.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 78050047 262 ALTEVVAAVKG-KVEVYLDGGIRTGNDVLKALALGAKCVFVGR 303
Cdd:pfam00478 311 AIYDVAEAAKKyGVPVIADGGIKYSGDIVKALAAGADAVMLGS 353
|
|
| BtpA |
COG0434 |
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis]; |
229-352 |
9.83e-04 |
|
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440203 Cd Length: 268 Bit Score: 40.16 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 229 KEDAELAVKHNVHGIIVSNHGGR--QLDEV-PASIDALTEVVAAVKGKVEVYLdgGI---RtgNDVLKALAL----GAK- 297
Cdd:COG0434 41 LRDARALQEGGVDGIIVENFGDApfLKDDVdPETVAAMAAVAGAVRKEVSVPV--GVnvlR--NDAIAALAIaaatGADf 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78050047 298 ---CVFVGrpilwglAYKGEHGV-----KEVL---------------DILKnEFHTSMtltGCRSVAEINQDLIQFSR 352
Cdd:COG0434 117 vrvNVFTG-------AYATDQGLiegnaAELLryrrrlgaedvkilaDVHV-KHASPL---GDRPLEEAARDTVERGL 183
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
261-303 |
1.53e-03 |
|
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: 40.62 E-value: 1.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 78050047 261 DALTEVVAA-----VKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGR 303
Cdd:COG0069 423 LGLAEVHQTlvgngLRDRIRLIADGKLKTGRDVAIAAALGADEFGFAR 470
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
262-303 |
1.60e-03 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 39.81 E-value: 1.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 78050047 262 ALTEVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVGR 303
Cdd:COG0516 186 AAMDTVTEARMAIAIAADGGIGYIHDNAKALAAGADAVMLGS 227
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
256-302 |
1.91e-03 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 38.85 E-value: 1.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 78050047 256 VPASIDALTEVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCVFVG 302
Cdd:cd00945 155 GGATVEDVKLMKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
228-306 |
2.07e-03 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 39.32 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78050047 228 TKEDAELAVKHNVHGIIVSNH--GG-RQLDEVPaSIDALTEVVAAVKgkVEVYLDGGIRTGNDVLKALALGAKCVFVG-R 303
Cdd:COG2070 113 SVREARKAEKAGADAVVAEGAeaGGhRGADEVS-TFALVPEVRDAVD--IPVIAAGGIADGRGIAAALALGADGVQMGtR 189
|
...
gi 78050047 304 PIL 306
Cdd:COG2070 190 FLA 192
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
265-299 |
2.49e-03 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 38.70 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|....*
gi 78050047 265 EVVAAVKGKVEVYLDGGIRTGNDVLKALALGAKCV 299
Cdd:PRK04302 165 EAVKKVNPDVKVLCGAGISTGEDVKAALELGADGV 199
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
257-302 |
8.47e-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: 37.07 E-value: 8.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 78050047 257 PASIDALTEVVAAVKGKVEVylDGGIRTGNDVLKALALGAKCVFVG 302
Cdd:pfam00977 59 PVNLDVVEEIAEEVFIPVQV--GGGIRSLEDVERLLSAGADRVIIG 102
|
|
| |
