SitesBLAST
Comparing WP_012566957.1 NCBI__GCF_000016185.1:WP_012566957.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6a50A Structure of benzoylformate decarboxylases in complex with cofactor tpp
28% identity, 98% coverage: 11:515/517 of query aligns to 12:521/527 of 6a50A
- binding magnesium ion: N117 (≠ A117), L118 (≠ I118), R120 (= R120), D428 (= D415), N455 (= N442), T457 (≠ A444)
- binding thiamine diphosphate: N23 (= N22), P24 (= P23), E47 (= E48), H70 (= H71), T377 (≠ I364), S378 (≠ T365), G401 (= G387), L403 (= L390), G427 (= G414), D428 (= D415), G429 (= G416), S430 (= S417), Y433 (= Y420), N455 (= N442), T457 (≠ A444), Y458 (= Y445), G459 (≠ R446), M460 (≠ I447), L461 (= L448)
5deiA Benzoylformate decarboxylase from pseudomonas putida
28% identity, 98% coverage: 11:515/517 of query aligns to 11:520/524 of 5deiA
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), E27 (= E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (≠ A112), N111 (≠ S113), Y159 (≠ A160), P253 (vs. gap), H280 (≠ G282), S375 (≠ A363), G400 (= G387), L402 (= L390), D427 (= D415), N454 (= N442), T456 (≠ A444), Y457 (= Y445), A459 (≠ I447), L460 (= L448), F463 (≠ E451)
- binding bicarbonate ion: S25 (≠ T25), H69 (= H71), L109 (= L111)
- binding calcium ion: N185 (≠ P185), D186 (= D186), D427 (= D415), N454 (= N442), T456 (≠ A444)
- binding magnesium ion: N116 (≠ A117), L117 (≠ I118), R119 (= R120)
- binding thiamine diphosphate: N22 (= N22), P23 (= P23), E46 (= E48), H69 (= H71), T376 (≠ I364), S377 (≠ T365), L402 (= L390), G426 (= G414), D427 (= D415), G428 (= G416), S429 (= S417), Y432 (= Y420), T456 (≠ A444), Y457 (= Y445), G458 (≠ R446), A459 (≠ I447), L460 (= L448)
Sites not aligning to the query:
3fsjX Crystal structure of benzoylformate decarboxylase in complex with the inhibitor mbp (see paper)
28% identity, 98% coverage: 11:515/517 of query aligns to 11:520/524 of 3fsjX
- active site: G24 (= G24), S25 (≠ T25), E27 (= E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (≠ A112), N111 (≠ S113), H280 (≠ G282), G400 (= G387), D427 (= D415), N454 (= N442), T456 (≠ A444), Y457 (= Y445), A459 (≠ I447), L460 (= L448)
- binding calcium ion: D427 (= D415), N454 (= N442), T456 (≠ A444)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(S)-hydroxy[(R)-hydroxy(methoxy)phosphoryl]phenylmethyl}-5-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: H280 (≠ G282), T376 (≠ I364), S377 (≠ T365), F396 (≠ L383), G400 (= G387), L402 (= L390), G426 (= G414), D427 (= D415), G428 (= G416), S429 (= S417), Y432 (= Y420), T456 (≠ A444), Y457 (= Y445), G458 (≠ R446), A459 (≠ I447), L460 (= L448), F463 (≠ E451)
Sites not aligning to the query:
1mczA Benzoylformate decarboxylase from pseudomonas putida complexed with an inhibitor, r-mandelate (see paper)
28% identity, 98% coverage: 11:515/517 of query aligns to 11:520/524 of 1mczA
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), E27 (= E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (≠ A112), N111 (≠ S113), Y159 (≠ A160), P253 (vs. gap), H280 (≠ G282), S375 (≠ A363), G400 (= G387), L402 (= L390), D427 (= D415), N454 (= N442), T456 (≠ A444), Y457 (= Y445), A459 (≠ I447), L460 (= L448), F463 (≠ E451)
- binding magnesium ion: N116 (≠ A117), L117 (≠ I118), R119 (= R120), D427 (= D415), N454 (= N442), T456 (≠ A444)
- binding (r)-mandelic acid: S25 (≠ T25), H69 (= H71), L109 (= L111), H280 (≠ G282), T376 (≠ I364), F463 (≠ E451)
- binding thiamine diphosphate: N22 (= N22), P23 (= P23), E46 (= E48), H69 (= H71), T376 (≠ I364), S377 (≠ T365), G400 (= G387), L402 (= L390), G426 (= G414), D427 (= D415), G428 (= G416), S429 (= S417), Y432 (= Y420), Y457 (= Y445), G458 (≠ R446), A459 (≠ I447), L460 (= L448)
Sites not aligning to the query:
3fznA Intermediate analogue in benzoylformate decarboxylase (see paper)
28% identity, 98% coverage: 11:515/517 of query aligns to 11:520/523 of 3fznA
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), E27 (= E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (≠ A112), N111 (≠ S113), Y159 (≠ A160), P253 (vs. gap), H280 (≠ G282), S375 (≠ A363), G400 (= G387), L402 (= L390), D427 (= D415), N454 (= N442), T456 (≠ A444), Y457 (= Y445), A459 (≠ I447), L460 (= L448), F463 (≠ E451)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(S)-hydroxy[(R)-hydroxy(methoxy)phosphoryl]phenylmethyl}-5-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: N22 (= N22), P23 (= P23), G24 (= G24), S25 (≠ T25), E46 (= E48), H69 (= H71), H280 (≠ G282), T376 (≠ I364), S377 (≠ T365), G400 (= G387), L402 (= L390), G426 (= G414), D427 (= D415), G428 (= G416), S429 (= S417), Y432 (= Y420), N454 (= N442), T456 (≠ A444), Y457 (= Y445), G458 (≠ R446), A459 (≠ I447)
- binding magnesium ion: D427 (= D415), N454 (= N442), T456 (≠ A444)
- binding phosphate ion: Q286 (≠ D288), L288 (= L290), K289 (≠ V291), P290 (= P292)
1bfdA Benzoylformate decarboxylase from pseudomonas putida (see paper)
28% identity, 98% coverage: 11:515/517 of query aligns to 11:520/523 of 1bfdA
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), E27 (= E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (≠ A112), N111 (≠ S113), Y159 (≠ A160), P253 (vs. gap), H280 (≠ G282), S375 (≠ A363), G400 (= G387), L402 (= L390), D427 (= D415), N454 (= N442), T456 (≠ A444), Y457 (= Y445), A459 (≠ I447), L460 (= L448), F463 (≠ E451)
- binding calcium ion: D427 (= D415), N454 (= N442), T456 (≠ A444)
- binding magnesium ion: N116 (≠ A117), L117 (≠ I118), R119 (= R120)
- binding thiamine diphosphate: T376 (≠ I364), S377 (≠ T365), L402 (= L390), G426 (= G414), D427 (= D415), G428 (= G416), S429 (= S417), Y432 (= Y420), T456 (≠ A444), Y457 (= Y445), G458 (≠ R446), A459 (≠ I447), L460 (= L448)
3f6bX Crystal structure of benzoylformate decarboxylase in complex with the pyridyl inhibitor paa (see paper)
28% identity, 98% coverage: 11:515/517 of query aligns to 11:520/525 of 3f6bX
- active site: G24 (= G24), E46 (= E48), L108 (≠ P110), L109 (= L111), T110 (≠ A112), N111 (≠ S113), G400 (= G387), D427 (= D415), N454 (= N442), T456 (≠ A444), Y457 (= Y445), A459 (≠ I447), L460 (= L448)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-2-[(1S,2E)-1-hydroxy-3-pyridin-3-ylprop-2-en-1-yl]-4-methyl-1,3-thiazol-3-ium: N22 (= N22), P23 (= P23), G24 (= G24), S25 (≠ T25), E46 (= E48), H69 (= H71)
Sites not aligning to the query:
1pi3A E28q mutant benzoylformate decarboxylase from pseudomonas putida
27% identity, 98% coverage: 11:515/517 of query aligns to 11:520/523 of 1pi3A
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), Q27 (≠ E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (≠ A112), N111 (≠ S113), Y159 (≠ A160), P253 (vs. gap), H280 (≠ G282), S375 (≠ A363), G400 (= G387), L402 (= L390), D427 (= D415), N454 (= N442), T456 (≠ A444), Y457 (= Y445), A459 (≠ I447), L460 (= L448), F463 (≠ E451)
- binding calcium ion: D427 (= D415), N454 (= N442), T456 (≠ A444)
- binding magnesium ion: N116 (≠ A117), L117 (≠ I118), R119 (= R120)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: T376 (≠ I364), S377 (≠ T365), L402 (= L390), G426 (= G414), G428 (= G416), S429 (= S417), Y432 (= Y420), N454 (= N442), T456 (≠ A444), Y457 (= Y445), G458 (≠ R446), A459 (≠ I447), L460 (= L448)
6qsiA Pseudomonas fluorescens pf-5 thiamine diphosphate-dependent 4- hydroxybenzoylformate decarboxylase (see paper)
31% identity, 98% coverage: 11:515/517 of query aligns to 11:520/525 of 6qsiA
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), E27 (= E27), E46 (= E48), H69 (= H71), M108 (≠ P110), L109 (= L111), A110 (= A112), Y159 (≠ A160), P253 (≠ L260), H280 (≠ Y283), S375 (≠ A363), G400 (= G387), L402 (= L390), Y457 (= Y445), A459 (≠ I447), L460 (= L448), F463 (≠ Y452)
- binding thiamine diphosphate: N22 (= N22), P23 (= P23), E46 (= E48), H69 (= H71), T376 (≠ I364), S377 (vs. gap), L402 (= L390), G426 (= G414), G428 (= G416), S429 (= S417), Y432 (= Y420), N454 (= N442), T456 (≠ A444), Y457 (= Y445), G458 (≠ R446), A459 (≠ I447), L460 (= L448)
7orxCCC jostii RHA1 thiamine diphosphate-dependent 4-hydroxybenzoylformate decarboxylase
30% identity, 99% coverage: 4:514/517 of query aligns to 8:523/531 of 7orxCCC
- active site: N26 (= N22), G28 (= G24), S29 (≠ T25), N30 (≠ S26), E31 (= E27), E50 (= E48), H73 (= H71), M112 (≠ P110), L113 (= L111), S114 (≠ A112), N115 (≠ S113), Y163 (≠ A160), P257 (vs. gap), H284 (≠ Y283), S379 (≠ A363), G404 (= G388), L406 (= L390), D431 (= D415), N458 (= N442), T460 (≠ A444), Y461 (= Y445), A463 (≠ I447), L464 (= L448), F467 (≠ E451)
- binding thiamine diphosphate: N26 (= N22), S29 (≠ T25), E50 (= E48), H73 (= H71), T380 (≠ I364), S381 (≠ T365), G404 (= G388), L406 (= L390), G430 (= G414), G432 (= G416), S433 (= S417), Y436 (= Y420), N458 (= N442), T460 (≠ A444), Y461 (= Y445), G462 (≠ R446)
4q9dB X-ray structure of a putative thiamin diphosphate-dependent enzyme isolated from mycobacterium smegmatis (see paper)
27% identity, 97% coverage: 11:513/517 of query aligns to 13:513/519 of 4q9dB
- active site: N24 (= N22), G26 (= G24), S27 (≠ T25), T28 (≠ S26), E29 (= E27), Q47 (vs. gap), E48 (vs. gap), H71 (= H71), V107 (≠ F107), D108 (= D108), Y110 (≠ P110), L111 (= L111), N112 (≠ A112), N113 (≠ S113), L161 (≠ A160), P252 (= P253), Y279 (= Y283), M374 (≠ D361), S376 (≠ A363), G401 (= G388), I403 (≠ L390), D432 (= D415), N459 (= N442), E461 (≠ A444), Y462 (= Y445), I464 (= I447)
- binding magnesium ion: D432 (= D415), N459 (= N442), E461 (≠ A444)
Sites not aligning to the query:
4k9qA The crystal structure of benzoylformate decarboxylase from polynucleobacter necessarius
26% identity, 97% coverage: 11:513/517 of query aligns to 12:520/531 of 4k9qA
- active site: N23 (= N22), G25 (= G24), S26 (≠ T25), T27 (≠ S26), E28 (= E27), E47 (= E48), H70 (= H71), N106 (≠ D108), E107 (≠ P109), L110 (≠ A112), T111 (≠ S113), L160 (≠ A160), T251 (vs. gap), Y278 (= Y283), V370 (≠ D361), C373 (≠ I364), G398 (= G388), L400 (= L390), D429 (= D415), N456 (= N442), E458 (≠ A444), Y459 (= Y445), G460 (≠ R446), I461 (= I447), L462 (= L448), F465 (≠ Y452)
- binding magnesium ion: D429 (= D415), N456 (= N442), E458 (≠ A444)
- binding thiamine diphosphate: P374 (≠ T365), S375 (= S366), L400 (= L390), G428 (= G414), D429 (= D415), G430 (= G416), S431 (= S417), Y434 (= Y420), N456 (= N442), E458 (≠ A444), Y459 (= Y445), G460 (≠ R446), I461 (= I447), L462 (= L448)
Sites not aligning to the query:
6lpiB Crystal structure of ahas holo-enzyme (see paper)
25% identity, 100% coverage: 1:515/517 of query aligns to 6:517/539 of 6lpiB
- active site: I27 (≠ N22), G29 (= G24), G30 (≠ T25), S31 (= S26), I32 (≠ E27), E53 (= E48), C76 (≠ H71), F115 (≠ P110), Q116 (≠ L111), E117 (≠ A112), K165 (≠ A160), M256 (≠ L249), A283 (≠ F280), V375 (≠ G367), G401 (= G388), M403 (≠ L390), D428 (= D415), N455 (= N442), A457 (= A444), L458 (vs. gap), L460 (vs. gap), V461 (vs. gap), Q464 (≠ I447)
- binding flavin-adenine dinucleotide: R155 (≠ A146), G212 (= G208), G213 (= G209), G214 (= G210), T236 (≠ R230), L237 (≠ V231), M238 (≠ L232), L254 (≠ P247), M256 (≠ L249), H257 (≠ E250), G276 (= G273), A277 (= A274), R278 (= R275), D280 (≠ P277), R282 (≠ A279), A283 (≠ F280), D300 (≠ G296), I301 (≠ V297), D319 (vs. gap), V320 (vs. gap), M380 (≠ R372), G398 (≠ T386)
- binding magnesium ion: D428 (= D415), N455 (= N442)
- binding thiamine diphosphate: E53 (= E48), C76 (≠ H71), P79 (= P74), G376 (≠ A368), Q377 (≠ P369), H378 (≠ C370), G401 (= G388), M403 (≠ L390), G427 (= G414), D428 (= D415), G429 (= G416), S430 (= S417), M433 (≠ Y420), N455 (= N442), A457 (= A444), L458 (vs. gap), G459 (vs. gap), L460 (vs. gap), V461 (vs. gap)
P0DUV9 2-hydroxyacyl-CoA lyase; AcHACL; HACL; 2-hydroxyisobutyryl-CoA lyase; EC 4.1.-.- from Actinomycetospora chiangmaiensis (strain DSM 45062 / JCM 15998 / CCTCC AA 205017 / NBRC 104400 / YIM 0006) (see paper)
35% identity, 25% coverage: 388:517/517 of query aligns to 433:553/590 of P0DUV9
- G433 (= G388) binding thiamine diphosphate
- D460 (= D415) binding Mg(2+)
- GA 461:462 (≠ GS 416:417) binding thiamine diphosphate
- N487 (= N442) binding Mg(2+)
- NRAWNI 487:492 (≠ NRAYRI 442:447) binding thiamine diphosphate
- A489 (= A444) binding Mg(2+)
- E493 (≠ L448) mutation to A: 10-fold decrease of 2-HIB-CoA cleavage rate, 6-fold increase in KM.; mutation to K: No cleavage of 2-HIB-CoA.; mutation to Q: 50-fold decrease of 2-HIB-CoA cleavage rate, 1.5-fold increase in KM.
Sites not aligning to the query:
- 43 binding 2-hydroxyisobutanoyl-CoA
- 255 binding 2-hydroxyisobutanoyl-CoA
- 273:274 binding 2-hydroxyisobutanoyl-CoA
- 362 binding 2-hydroxyisobutanoyl-CoA
- 410:412 binding thiamine diphosphate
- 417 binding 2-hydroxyisobutanoyl-CoA
- 561:564 binding 2-hydroxyisobutanoyl-CoA
- 566:590 C-terminal lid
7pt4B Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with a covalently bound reaction intermediate as well as products formyl-coa and acetone (see paper)
35% identity, 25% coverage: 388:517/517 of query aligns to 419:539/584 of 7pt4B
- binding magnesium ion: D446 (= D415), N473 (= N442), A475 (= A444)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1r,11r,15s,17r)-19-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-1,11,15,17-tetrahydroxy-12,12-dimethyl-15,17-dioxido-6,10-dioxo-14,16,18-trioxa-2-thia-5,9-diaza-15,17-diphosphanonadec-1-yl}-5-(2-{[(r)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: G419 (= G388), L421 (= L390), G445 (= G414), D446 (= D415), G447 (= G416), A448 (≠ S417), N473 (= N442), A475 (= A444), W476 (≠ Y445), N477 (≠ R446), I478 (= I447), E479 (≠ L448)
Sites not aligning to the query:
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1r,11r,15s,17r)-19-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-1,11,15,17-tetrahydroxy-12,12-dimethyl-15,17-dioxido-6,10-dioxo-14,16,18-trioxa-2-thia-5,9-diaza-15,17-diphosphanonadec-1-yl}-5-(2-{[(r)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: 257, 259, 260, 279, 352, 395, 396, 397, 398, 399, 403, 404, 547, 561
7pt4A Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with a covalently bound reaction intermediate as well as products formyl-coa and acetone (see paper)
35% identity, 25% coverage: 388:517/517 of query aligns to 419:539/580 of 7pt4A
- binding magnesium ion: D446 (= D415), N473 (= N442), A475 (= A444)
- binding thiamine diphosphate: G419 (= G388), L421 (= L390), G445 (= G414), D446 (= D415), G447 (= G416), A448 (≠ S417), N473 (= N442), A475 (= A444), W476 (≠ Y445), N477 (≠ R446), I478 (= I447), E479 (≠ L448)
Sites not aligning to the query:
- binding s-{(9r,13s,15r)-17-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-9,13,15-trihydroxy-10,10-dimethyl-13,15-dioxido-4,8-dioxo-12,14,16-trioxa-3,7-diaza-13,15-diphosphaheptadec-1-yl} thioformate : 241, 256, 257, 259, 260, 278, 279, 352, 403, 404, 552
- binding thiamine diphosphate: 396, 397, 398
7pt1A Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with substrate 2-hib-coa and inactive cofactor 3-deaza-thdp (see paper)
35% identity, 25% coverage: 388:517/517 of query aligns to 419:539/574 of 7pt1A
- binding S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} 2-hydroxy-2-methylpropanethioate: G419 (= G388)
- binding magnesium ion: D446 (= D415), N473 (= N442), A475 (= A444)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: G419 (= G388), L421 (= L390), G445 (= G414), D446 (= D415), G447 (= G416), A448 (≠ S417), N473 (= N442), A475 (= A444), W476 (≠ Y445), N477 (≠ R446), I478 (= I447), E479 (≠ L448)
Sites not aligning to the query:
- binding S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} 2-hydroxy-2-methylpropanethioate: 113, 114, 256, 257, 259, 260, 279, 352, 403, 404, 547, 552
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: 51, 74, 77, 396, 397, 398
P09342 Acetolactate synthase 1, chloroplastic; ALS I; Acetohydroxy-acid synthase I; Acetolactate synthase I; EC 2.2.1.6 from Nicotiana tabacum (Common tobacco) (see 2 papers)
28% identity, 37% coverage: 328:517/517 of query aligns to 441:638/667 of P09342
Sites not aligning to the query:
- 161 modified: Disulfide link with 307
- 194 P→Q: In C3; highly resistant to sulfonylurea herbicides.
- 307 modified: Disulfide link with 161
P09114 Acetolactate synthase 2, chloroplastic; ALS II; Acetohydroxy-acid synthase II; Acetolactate synthase II; EC 2.2.1.6 from Nicotiana tabacum (Common tobacco) (see paper)
29% identity, 26% coverage: 381:517/517 of query aligns to 497:635/664 of P09114
- W568 (vs. gap) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
Sites not aligning to the query:
- 191 P→A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
2ihuA Carboxyethylarginine synthase from streptomyces clavuligerus: putative reaction intermediate complex (see paper)
30% identity, 27% coverage: 37:178/517 of query aligns to 36:178/562 of 2ihuA
Sites not aligning to the query:
- active site: 23, 25, 26, 27, 28, 265, 292, 400, 426, 428, 453, 480, 482, 483, 485, 486, 489, 551
- binding magnesium ion: 453, 480, 482
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: 401, 402, 403, 428, 452, 453, 454, 455, 482, 483, 484, 485, 486, 551
Query Sequence
>WP_012566957.1 NCBI__GCF_000016185.1:WP_012566957.1
MNGAEALAQGLRSAGLDTVFANPGTSEMHLVGALAAVPGMRLVPGLFEGVLSGAADAHAR
LTGRPAGLLLHLGPGLANATANLHNASRAGSPVVSIVGEHRSSLLPFDPPLASDIEAIAR
PYAGWVRRLERPEEAAEAARAAVAAALGTPARHAVLIVPADVAWGEAGRPDTGGDAPAAR
VDPVPDARIELMADMLRTGGHASALLLGGGLLDGRGSLLAGRIAAATGCRVLSETFPTAQ
RRGAGLPYLERLPYFPADVLQTLDGVRSLVLAGAREPVAFFGYPGRPDRLVPEGCGVDRL
CGPGEDGHAALEALAGLLGAGSSDPVLLPEQRPLRPEGRLTVDAVGQAIGSLLPENAIVV
DEAITSGAPCYRFTVQAPTHDWLSLTGGSLGFGLPAALGAAMAAPGRKVLALVGDGSALY
TNQALWSLARTGADVVVVVFANRAYRILQLEYANMGLGSPAPAAQDLMRLDTPDLDFVSL
ARGFGILAARADEAGEFTRILERALAEPGPFLIETVV
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory