|
Name |
Accession |
Description |
Interval |
E-value |
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
13-351 |
1.15e-180 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 503.99 E-value: 1.15e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 13 AKKYLPKIAWDYFAAGADDCNTRDENILAYQRIRFRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGFHQLAWPDGEKST 92
Cdd:pfam01070 1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 93 ARAAKAMNTCYIASTYSTCTLEEISAAAPSSlRWFQLYIHRNRAASQQLVQRAEALGFQGLVLTADLPYTGKRRDDLRNG 172
Cdd:pfam01070 81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGP-LWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 173 FRLPPHMKVKNLEQ-----DFEGDDRSEYGLPPNS------LDPSVTWNDIYWLRSLTRLPIIIKGILTKEDAELAVRHG 241
Cdd:pfam01070 160 FTLPPRLTPRNLLDlalhpRWALGVLRRGGAGGAAafvgsqFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 242 VQGIIVSNHGGRQLDEGPATIDALVEVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTLWGLAYKGEEGLQD 321
Cdd:pfam01070 240 VDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAH 319
|
330 340 350
....*....|....*....|....*....|
gi 677973056 322 VLRILQDEFRLSMALAGCASVSEIGRHLVQ 351
Cdd:pfam01070 320 ALEILRDELERTMALLGCKSIADLTPSLLR 349
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
7-347 |
2.15e-170 |
|
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: 476.17 E-value: 2.15e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 7 SDFEAYAKKYLPKIAWDYFAAGADDCNTRDENILAYQRIRFRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGFHQLAWP 86
Cdd:cd02809 1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 87 DGEKSTARAAKAMNTCYIASTYSTCTLEEISAAAPSsLRWFQLYIHRNRAASQQLVQRAEALGFQGLVLTADLPYTGKRr 166
Cdd:cd02809 81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPG-PRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 167 ddlrngfrlpphmkvknleqdfegddrseyglppnsldpsVTWNDIYWLRSLTRLPIIIKGILTKEDAELAVRHGVQGII 246
Cdd:cd02809 159 ----------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 247 VSNHGGRQLDEGPATIDALVEVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTLWGLAYKGEEGLQDVLRIL 326
Cdd:cd02809 199 VSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHVLEIL 278
|
330 340
....*....|....*....|.
gi 677973056 327 QDEFRLSMALAGCASVSEIGR 347
Cdd:cd02809 279 RDELERAMALLGCASLADLDP 299
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
3-350 |
1.82e-163 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 460.75 E-value: 1.82e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 3 MVCLSDFEAYAKKYLPKIAWDYFAAGADDCNTRDENILAYQRIRFRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGFHQ 82
Cdd:COG1304 4 ILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 83 LAWPDGEKSTARAAKAMNTCYIASTYSTCTLEEISAAAPSSLrWFQLYIHRNRAASQQLVQRAEALGFQGLVLTADLPYT 162
Cdd:COG1304 84 LAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPL-WFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 163 GKRRDDLRNGFRLPPHMKVKNLEQdFEGDDRSEYGLPPNS------LDPSVTWNDIYWLRSLTRLPIIIKGILTKEDAEL 236
Cdd:COG1304 163 GRRERDLREGFSQPPRLTPRNLLE-AATHPRWALGLASLAawldtnFDPSLTWDDIAWLRERWPGPLIVKGVLSPEDARR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 237 AVRHGVQGIIVSNHGGRQLDEGPATIDALVEVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTLWGLAYKGE 316
Cdd:COG1304 242 AVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLAAGGE 321
|
330 340 350
....*....|....*....|....*....|....
gi 677973056 317 EGLQDVLRILQDEFRLSMALAGCASVSEIGRHLV 350
Cdd:COG1304 322 AGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
|
|
| FCB2_FMN |
cd02922 |
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ... |
7-348 |
6.67e-142 |
|
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: 405.83 E-value: 6.67e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 7 SDFEAYAKKYLPKIAWDYFAAGADDCNTRDENILAYQRIRFRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGFHQLAWP 86
Cdd:cd02922 1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 87 DGEKSTARAAKAMNTCYIASTYSTCTLEEISAAAPSSL-RWFQLYIHRNRAASQQLVQRAEALGFQGLVLTADLPYTGKR 165
Cdd:cd02922 81 DGELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQpLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 166 RDDLRNGF--RLPPHMKVKNLEQDFEGDDRseygLPPNSLDPSVTWNDIYWLRSLTRLPIIIKGILTKEDAELAVRHGVQ 243
Cdd:cd02922 161 ERDERLKAeeAVSDGPAGKKTKAKGGGAGR----AMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 244 GIIVSNHGGRQLDEGPATIDALVEVVE---AVQGRIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTLWGLAYKGEEGLQ 320
Cdd:cd02922 237 GIVLSNHGGRQLDTAPAPIEVLLEIRKhcpEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVE 316
|
330 340
....*....|....*....|....*...
gi 677973056 321 DVLRILQDEFRLSMALAGCASVSEIGRH 348
Cdd:cd02922 317 KAIQILKDEIETTMRLLGVTSLDQLGPS 344
|
|
| PLN02535 |
PLN02535 |
glycolate oxidase |
4-351 |
2.26e-136 |
|
glycolate oxidase
Pssm-ID: 215294 Cd Length: 364 Bit Score: 392.66 E-value: 2.26e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 4 VCLSDFEAYAKKYLPKIAWDYFAAGADDCNTRDENILAYQRIRFRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGFHQL 83
Cdd:PLN02535 6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 84 AWPDGEKSTARAAKAMNTCYIASTYSTCTLEEIsAAAPSSLRWFQLYIHRNRAASQQLVQRAEALGFQGLVLTADLPYTG 163
Cdd:PLN02535 86 AHPEGEIATARAAAACNTIMVLSFMASCTVEEV-ASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 164 KRRDDLRNGFRLPphmKVKNLEQDFEGDDRSEYG-----LPPNSLDPSVTWNDIYWLRSLTRLPIIIKGILTKEDAELAV 238
Cdd:PLN02535 165 RREADIKNKMISP---QLKNFEGLLSTEVVSDKGsgleaFASETFDASLSWKDIEWLRSITNLPILIKGVLTREDAIKAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 239 RHGVQGIIVSNHGGRQLDEGPATIDALVEVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTLWGLAYKGEEG 318
Cdd:PLN02535 242 EVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGEDG 321
|
330 340 350
....*....|....*....|....*....|...
gi 677973056 319 LQDVLRILQDEFRLSMALAGCASVSEIGRHLVQ 351
Cdd:PLN02535 322 VRKVIEMLKDELEITMALSGCPSVKDITRSHVR 354
|
|
| PLN02493 |
PLN02493 |
probable peroxisomal (S)-2-hydroxy-acid oxidase |
1-350 |
1.52e-125 |
|
probable peroxisomal (S)-2-hydroxy-acid oxidase
Pssm-ID: 166134 [Multi-domain] Cd Length: 367 Bit Score: 365.21 E-value: 1.52e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 1 MAMVCLSDFEAYAKKYLPKIAWDYFAAGADDCNTRDENILAYQRIRFRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGF 80
Cdd:PLN02493 1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 81 HQLAWPDGEKSTARAAKAMNTCYIASTYSTCTLEEISAAAPSsLRWFQLYIHRNRAASQQLVQRAEALGFQGLVLTADLP 160
Cdd:PLN02493 81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPG-IRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 161 YTGKRRDDLRNGFRLPPHMKVKNLEQDFEG--DDRSEYGLPP---NSLDPSVTWNDIYWLRSLTRLPIIIKGILTKEDAE 235
Cdd:PLN02493 160 RLGRRESDIKNRFTLPPNLTLKNFEGLDLGkmDEANDSGLASyvaGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 236 LAVRHGVQGIIVSNHGGRQLDEGPATIDALVEVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTLWGLAYKG 315
Cdd:PLN02493 240 IAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEG 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 677973056 316 EEGLQDVLRILQDEFRLSMALAGCASVSEIGR-HLV 350
Cdd:PLN02493 320 EAGVRKVLQMLRDEFELTMALSGCRSLKEISRnHIT 355
|
|
| LMO_FMN |
cd03332 |
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ... |
4-350 |
8.07e-119 |
|
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: 348.50 E-value: 8.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 4 VCLSDFEAYAKKYLPKIAWDYFAAGADDCNTRDENILAYQRIRFRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGFHQL 83
Cdd:cd03332 19 VDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQEL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 84 AWPDGEKSTARAAKAMNTCYIASTYSTCTLEEISAAAPSSLRWFQLYIHRNRAASQQLVQRAEALGFQGLVLTADLPYTG 163
Cdd:cd03332 99 FHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 164 KRRDDLRNGFRlpPHMKVKNLEQDFE------------GDDRSEYGLPPNSL--------DPSVTWNDIYWLRSLTRLPI 223
Cdd:cd03332 179 WRPRDLDLGYL--PFLRGIGIANYFSdpvfrkklaepvGEDPEAPPPMEAAVarfvsvfsGPSLTWEDLAFLREWTDLPI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 224 IIKGILTKEDAELAVRHGVQGIIVSNHGGRQLDEGPATIDALVEVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCVFI 303
Cdd:cd03332 257 VLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLI 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 677973056 304 GRPTLWGLAYKGEEGLQDVLRILQDEFRLSMALAGCASVSEIGRHLV 350
Cdd:cd03332 337 GRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
|
|
| LOX_like_FMN |
cd04737 |
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ... |
3-347 |
2.57e-110 |
|
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: 325.55 E-value: 2.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 3 MVCLSDFEAYAKKYLPKIAWDYFAAGADDCNTRDENILAYQRIRFRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGFHQ 82
Cdd:cd04737 5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 83 LAWPDGEKSTARAAKAMNTCYIASTYSTCTLEEISAAAPSSLRWFQLYIHRNRAASQQLVQRAEALGFQGLVLTADLPYT 162
Cdd:cd04737 85 LAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 163 GKRRDDLRNGFRLPPHMKVKN--LEQDFEGDDRSE-YGLPPNSLDPSvtwnDIYWLRSLTRLPIIIKGILTKEDAELAVR 239
Cdd:cd04737 165 GNREADIRNKFQFPFGMPNLNhfSEGTGKGKGISEiYAAAKQKLSPA----DIEFIAKISGLPVIVKGIQSPEDADVAIN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 240 HGVQGIIVSNHGGRQLDEGPATIDALVEVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTLWGLAYKGEEGL 319
Cdd:cd04737 241 AGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQGV 320
|
330 340
....*....|....*....|....*...
gi 677973056 320 QDVLRILQDEFRLSMALAGCASVSEIGR 347
Cdd:cd04737 321 ASVLEHLNKELKIVMQLAGTRTIEDVKR 348
|
|
| PLN02979 |
PLN02979 |
glycolate oxidase |
47-348 |
1.26e-108 |
|
glycolate oxidase
Pssm-ID: 166620 Cd Length: 366 Bit Score: 322.06 E-value: 1.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 47 FRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGFHQLAWPDGEKSTARAAKAMNTCYIASTYSTCTLEEISAAAPSsLRW 126
Cdd:PLN02979 46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPG-IRF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 127 FQLYIHRNRAASQQLVQRAEALGFQGLVLTADLPYTGKRRDDLRNGFRLPPHMKVKNLEQDFEG--DDRSEYGLPP---N 201
Cdd:PLN02979 125 FQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGkmDEANDSGLASyvaG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 202 SLDPSVTWNDIYWLRSLTRLPIIIKGILTKEDAELAVRHGVQGIIVSNHGGRQLDEGPATIDALVEVVEAVQGRIEVYVD 281
Cdd:PLN02979 205 QIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLD 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 677973056 282 GGIRKGSDVLKALALGAKCVFIGRPTLWGLAYKGEEGLQDVLRILQDEFRLSMALAGCASVSEIGRH 348
Cdd:PLN02979 285 GGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRN 351
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
8-347 |
1.57e-98 |
|
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: 295.97 E-value: 1.57e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 8 DFEAYAKKYLPKIAWDYFAAGADDCNTRDENILAYQRIRFRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGFHQLAWPD 87
Cdd:cd04736 2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 88 GEKSTARAAKAMNTCYIASTYSTCTLEEISAAAPSSLrWFQLY-IHRNRAasQQLVQRAEALGFQGLVLTADLPYTGKRR 166
Cdd:cd04736 82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDL-WFQLYvVHRELA--ELLVKRALAAGYTTLVLTTDVAVNGYRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 167 DDLRNGFRLP--------------PHMKVKNLE------QDFEGDDRS----EYGLPPNSLDPSVTWNDIYWLRSLTRLP 222
Cdd:cd04736 159 RDLRNGFAIPfrytprvlldgilhPRWLLRFLRngmpqlANFASDDAIdvevQAALMSRQMDASFNWQDLRWLRDLWPHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 223 IIIKGILTKEDAELAVRHGVQGIIVSNHGGRQLDEGPATIDALVEVVEAVQgrIEVYVDGGIRKGSDVLKALALGAKCVF 302
Cdd:cd04736 239 LLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATY--KPVLIDSGIRRGSDIVKALALGANAVL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 677973056 303 IGRPTLWGLAYKGEEGLQDVLRILQDEFRLSMALAGCASVSEIGR 347
Cdd:cd04736 317 LGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
1-355 |
4.78e-90 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 274.98 E-value: 4.78e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 1 MAMVCLSDFEAYAKKYLPKIAWDYFAAGADDCNTRDENILAYQRIRFRPRVLRDVSTIDIRTEILGTEISFPVGIAPTGF 80
Cdd:PRK11197 1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 81 HQLAWPDGEKSTARAAKAMNTCYIASTYSTCTLEEISAAAPSSLrWFQLYIHRNRAASQQLVQRAEALGFQGLVLTADLP 160
Cdd:PRK11197 81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPM-WFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 161 YTGKRRDDLRNGFRLP-------------------------PHM---------KVKNLEqDFegddrseYGLPPNSLDPS 206
Cdd:PRK11197 160 VPGARYRDAHSGMSGPnaamrrylqavthpqwawdvglngrPHDlgnisaylgKPTGLE-DY-------IGWLGNNFDPS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 207 VTWNDIYWLRSLTRLPIIIKGILTKEDAELAVRHGVQGIIVSNHGGRQLDEGPATIDALVEVVEAVQGRIEVYVDGGIRK 286
Cdd:PRK11197 232 ISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 287 GSDVLKALALGAKCVFIGRPTLWGLAYKGEEGLQDVLRILQDEFRLSMALAGCASVSEIGRH-LVQFSKL 355
Cdd:PRK11197 312 GLDVVRMIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDsLVQGNAA 381
|
|
| IDI-2_FMN |
cd02811 |
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ... |
214-344 |
3.96e-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: 86.78 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 214 WLRSLTRL------PIIIK----GIlTKEDAELAVRHGVQGIIVSNHGG---------RQLDEGPA-----------TID 263
Cdd:cd02811 166 WLERIEELvkalsvPVIVKevgfGI-SRETAKRLADAGVKAIDVAGAGGtswarvenyRAKDSDQRlaeyfadwgipTAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 264 ALVEVVEAVQGrIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTLwGLAYKGEEGLQDVLRILQDEFRLSMALAGCASVS 343
Cdd:cd02811 245 SLLEVRSALPD-LPLIASGGIRNGLDIAKALALGADLVGMAGPFL-KAALEGEEAVIETIEQIIEELRTAMFLTGAKNLA 322
|
.
gi 677973056 344 E 344
Cdd:cd02811 323 E 323
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
212-351 |
1.91e-10 |
|
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: 61.40 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 212 IYWLRSLT-RLPIIIK---GILTKEDAELAVRHGVQGIIVSNHGG-------RQLDE-GPATIDALVEVVEAVQG----- 274
Cdd:cd02808 205 IEDLREATgGKPIGVKlvaGHGEGDIAAGVAAAGADFITIDGAEGgtgaaplTFIDHvGLPTELGLARAHQALVKnglrd 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 275 RIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTL-----------------WGLAYKgEEGLQDVLRI------------ 325
Cdd:cd02808 285 RVSLIASGGLRTGADVAKALALGADAVGIGTAALialgciqarkchtntcpVGVATQ-DPELRRRLDVegkaervanylk 363
|
170 180
....*....|....*....|....*...
gi 677973056 326 -LQDEFRLSMALAGCASVSEIGR-HLVQ 351
Cdd:cd02808 364 sLAEELRELAAALGKRSLELLGRsDLLA 391
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
118-305 |
7.87e-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: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 118 AAAPSSLRWFQLYIHRNRAASQQLVQRAEALGFQGLVLTADLPYTgkrrddlrngfrlpphmkvknleqdfegddrseyg 197
Cdd:cd04722 53 AAETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL----------------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 198 lppnsldPSVTWNDIYWLRSLTR-LPIIIKGILT-KEDAELAVRHGVQGIIVSNHGGRQLDEGPATIDALVEVVEAVQGR 275
Cdd:cd04722 98 -------AREDLELIRELREAVPdVKVVVKLSPTgELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSK 170
|
170 180 190
....*....|....*....|....*....|
gi 677973056 276 IEVYVDGGIRKGSDVLKALALGAKCVFIGR 305
Cdd:cd04722 171 VPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
212-306 |
2.10e-06 |
|
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: 48.67 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 212 IYWLRSL-TRLPIIIKGILTKEDAELAVRHGVQGIIVsnhGGrqldeGPATID--------------ALVEVVEAVQGR- 275
Cdd:cd00381 126 IKFIKKKyPNVDVIAGNVVTAEAARDLIDAGADGVKV---GI-----GPGSICttrivtgvgvpqatAVADVAAAARDYg 197
|
90 100 110
....*....|....*....|....*....|.
gi 677973056 276 IEVYVDGGIRKGSDVLKALALGAKCVFIGRP 306
Cdd:cd00381 198 VPVIADGGIRTSGDIVKALAAGADAVMLGSL 228
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
212-308 |
4.80e-06 |
|
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: 48.10 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 212 IYWLRSLT-RLPIIIKgiLTKEDAELAVRHGVQG-----IIVSNHGGRQLDEGPATID--------ALVEVVEAV----- 272
Cdd:pfam01645 193 IYDLKEINpKAPISVK--LVSGHGVGTIAAGVAKagadiILIDGYDGGTGASPKTSIKhaglpwelALAEAHQTLkengl 270
|
90 100 110
....*....|....*....|....*....|....*.
gi 677973056 273 QGRIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTL 308
Cdd:pfam01645 271 RDRVSLIADGGLRTGADVAKAAALGADAVYIGTAAL 306
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
230-304 |
3.29e-05 |
|
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: 44.78 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 230 TKEDAELAVRHGVQGIIVSN-----HGGRQLdegpATIDALV-EVVEAVqgRIEVYVDGGIRKGSDVLKALALGAKCVFI 303
Cdd:cd04730 111 SVEEARKAEAAGADALVAQGaeaggHRGTFD----IGTFALVpEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQM 184
|
.
gi 677973056 304 G 304
Cdd:cd04730 185 G 185
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
264-305 |
1.01e-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: 43.92 E-value: 1.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 677973056 264 ALVEVVEAVQGR-IEVYVDGGIRKGSDVLKALALGAKCVFIGR 305
Cdd:pfam00478 311 AIYDVAEAAKKYgVPVIADGGIKYSGDIVKALAAGADAVMLGS 353
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
230-304 |
4.00e-04 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 41.64 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 677973056 230 TKEDAELAVRHGVQGIIVSN-----HGGRQldegPATIDALV-EVVEAVqgRIEVYVDGGIRKGSDVLKALALGAKCVFI 303
Cdd:COG2070 113 SVREARKAEKAGADAVVAEGaeaggHRGAD----EVSTFALVpEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQM 186
|
.
gi 677973056 304 G 304
Cdd:COG2070 187 G 187
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
259-301 |
4.98e-04 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 41.01 E-value: 4.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 677973056 259 PATIDALVEVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCV 301
Cdd:PRK04302 157 PEVVEDAVEAVKKVNPDVKVLCGAGISTGEDVKAALELGADGV 199
|
|
| OYE_like_4_FMN |
cd04735 |
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ... |
256-309 |
5.46e-04 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240086 [Multi-domain] Cd Length: 353 Bit Score: 41.43 E-value: 5.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 677973056 256 DEGPATIDAlveVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCVFIGRPTLW 309
Cdd:cd04735 268 DDNQTIMEL---VKERIAGRLPLIAVGSINTPDDALEALETGADLVAIGRGLLV 318
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
263-305 |
1.17e-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: 41.00 E-value: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 677973056 263 DALVEVVEAVQG-----RIEVYVDGGIRKGSDVLKALALGAKCVFIGR 305
Cdd:COG0069 423 LGLAEVHQTLVGnglrdRIRLIADGKLKTGRDVAIAAALGADEFGFAR 470
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
281-305 |
1.79e-03 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 39.95 E-value: 1.79e-03
10 20
....*....|....*....|....*
gi 677973056 281 DGGIRKGSDVLKALALGAKCVFIGR 305
Cdd:PTZ00314 350 DGGIKNSGDICKALALGADCVMLGS 374
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
264-305 |
2.01e-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: 2.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 677973056 264 ALVEVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCVFIGR 305
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 ... |
258-304 |
7.27e-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: 37.31 E-value: 7.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 677973056 258 GPATIDALVEVVEAVQGRIEVYVDGGIRKGSDVLKALALGAKCVFIG 304
Cdd:cd00945 155 GGATVEDVKLMKEAVGGRVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| |
