SitesBLAST
Comparing Ac3H11_2719 FitnessBrowser__acidovorax_3H11:Ac3H11_2719 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)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 97% coverage: 9:271/271 of query aligns to 4:257/257 of 6slbAAA
- active site: Q64 (≠ G70), F69 (≠ M75), L80 (≠ R94), N84 (≠ Q98), A108 (= A122), S111 (≠ D125), A130 (≠ S144), F131 (= F145), L136 (≠ I150), P138 (= P152), D139 (≠ G153), A224 (≠ E238), G234 (≠ H248)
- binding (~{E})-6-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-6-oxidanylidene-hex-3-enoic acid: R58 (≠ S64), A62 (= A68), Q64 (≠ G70), D65 (≠ N71), L66 (≠ V72), Y76 (≠ F82), A108 (= A122), F131 (= F145), D139 (≠ G153)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 97% coverage: 9:271/271 of query aligns to 1:245/245 of 6slaAAA
- active site: Q61 (≠ G70), L68 (≠ Q77), N72 (≠ Q98), A96 (= A122), S99 (≠ D125), A118 (≠ S144), F119 (= F145), L124 (≠ I150), P126 (= P152), N127 (≠ G153), A212 (≠ E238), G222 (≠ H248)
- binding ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] 2-(2,5-dihydrooxepin-7-yl)ethanethioate: L21 (≠ R29), A59 (= A68), Q61 (≠ G70), D62 (≠ N71), L63 (≠ V72), L68 (≠ Q77), Y71 (≠ I97), A94 (≠ I120), G95 (= G121), A96 (= A122), F119 (= F145), I122 (≠ V148), L124 (≠ I150), N127 (≠ G153), F234 (= F260), K237 (= K263)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
37% identity, 97% coverage: 10:271/271 of query aligns to 5:256/256 of 3h81A
- active site: A64 (≠ G70), M69 (= M75), T79 (≠ R94), F83 (≠ Q98), G107 (≠ A122), E110 (≠ D125), P129 (≠ S144), E130 (≠ F145), V135 (≠ I150), P137 (= P152), G138 (= G153), L223 (≠ E238), F233 (≠ H248)
- binding calcium ion: F233 (≠ H248), Q238 (≠ H253)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
37% identity, 96% coverage: 10:269/271 of query aligns to 6:255/255 of 3q0jC
- active site: A65 (≠ G70), M70 (= M75), T80 (≠ R94), F84 (≠ Q98), G108 (≠ A122), E111 (≠ D125), P130 (≠ S144), E131 (≠ F145), V136 (≠ I150), P138 (= P152), G139 (= G153), L224 (≠ E238), F234 (≠ H248)
- binding acetoacetyl-coenzyme a: Q23 (≠ E27), A24 (≠ T28), L25 (≠ R29), A27 (= A31), A63 (= A68), G64 (= G69), A65 (≠ G70), D66 (≠ N71), I67 (≠ V72), K68 (= K73), M70 (= M75), F84 (≠ Q98), G107 (= G121), G108 (≠ A122), E111 (≠ D125), P130 (≠ S144), E131 (≠ F145), P138 (= P152), G139 (= G153), M140 (≠ D154)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 96% coverage: 10:269/271 of query aligns to 6:255/255 of 3q0gC
- active site: A65 (≠ G70), M70 (= M75), T80 (≠ R94), F84 (≠ Q98), G108 (≠ A122), E111 (≠ D125), P130 (≠ S144), E131 (≠ F145), V136 (≠ I150), P138 (= P152), G139 (= G153), L224 (≠ E238), F234 (≠ H248)
- binding coenzyme a: L25 (≠ R29), A63 (= A68), I67 (≠ V72), K68 (= K73), Y104 (≠ P118), P130 (≠ S144), E131 (≠ F145), L134 (≠ V148)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 96% coverage: 10:269/271 of query aligns to 5:250/250 of 3q0gD
- active site: A64 (≠ G70), M69 (= M75), T75 (≠ R94), F79 (≠ Q98), G103 (≠ A122), E106 (≠ D125), P125 (≠ S144), E126 (≠ F145), V131 (≠ I150), P133 (= P152), G134 (= G153), L219 (≠ E238), F229 (≠ H248)
- binding Butyryl Coenzyme A: F225 (≠ Q244), F241 (= F260)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 96% coverage: 13:271/271 of query aligns to 9:259/259 of 5zaiC
- active site: A65 (≠ G70), F70 (≠ M75), S82 (≠ R90), R86 (= R94), G110 (≠ A122), E113 (≠ D125), P132 (≠ S144), E133 (≠ F145), I138 (= I150), P140 (= P152), G141 (= G153), A226 (≠ E238), F236 (≠ H248)
- binding coenzyme a: K24 (≠ T28), L25 (≠ R29), A63 (= A68), G64 (= G69), A65 (≠ G70), D66 (≠ N71), I67 (≠ V72), P132 (≠ S144), R166 (≠ T178), F248 (= F260), K251 (= K263)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
34% identity, 96% coverage: 9:268/271 of query aligns to 5:257/260 of 2hw5C
- active site: A68 (≠ G70), M73 (= M75), S83 (≠ R94), L87 (≠ Q98), G111 (≠ A122), E114 (≠ D125), P133 (≠ S144), E134 (≠ F145), T139 (≠ I150), P141 (= P152), G142 (= G153), K227 (≠ E238), F237 (≠ H248)
- binding crotonyl coenzyme a: K26 (≠ E27), A27 (≠ T28), L28 (≠ R29), A30 (= A31), K62 (≠ S64), I70 (≠ V72), F109 (≠ I120)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
34% identity, 96% coverage: 9:268/271 of query aligns to 4:251/254 of 2dubA
- active site: A67 (≠ G70), M72 (= M75), S82 (= S92), G105 (≠ A122), E108 (≠ D125), P127 (≠ S144), E128 (≠ F145), T133 (≠ I150), P135 (= P152), G136 (= G153), K221 (≠ E238), F231 (≠ H248)
- binding octanoyl-coenzyme a: K25 (≠ E27), A26 (≠ T28), L27 (≠ R29), A29 (= A31), A65 (= A68), A67 (≠ G70), D68 (≠ N71), I69 (≠ V72), K70 (= K73), G105 (≠ A122), E108 (≠ D125), P127 (≠ S144), E128 (≠ F145), G136 (= G153), A137 (≠ D154)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 96% coverage: 9:268/271 of query aligns to 5:257/260 of 1dubA
- active site: A68 (≠ G70), M73 (= M75), S83 (≠ Y87), L87 (≠ D91), G111 (≠ A122), E114 (≠ D125), P133 (≠ S144), E134 (≠ F145), T139 (≠ I150), P141 (= P152), G142 (= G153), K227 (≠ E238), F237 (≠ H248)
- binding acetoacetyl-coenzyme a: K26 (≠ E27), A27 (≠ T28), L28 (≠ R29), A30 (= A31), A66 (= A68), A68 (≠ G70), D69 (≠ N71), I70 (≠ V72), Y107 (≠ P118), G110 (= G121), G111 (≠ A122), E114 (≠ D125), P133 (≠ S144), E134 (≠ F145), L137 (≠ V148), G142 (= G153), F233 (≠ Q244), F249 (= F260)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 96% coverage: 9:268/271 of query aligns to 3:255/258 of 1ey3A
- active site: A66 (≠ G70), M71 (= M75), S81 (≠ Y87), L85 (≠ D91), G109 (≠ A122), E112 (≠ D125), P131 (≠ S144), E132 (≠ F145), T137 (≠ I150), P139 (= P152), G140 (= G153), K225 (≠ E238), F235 (≠ H248)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E27), L26 (≠ R29), A28 (= A31), A64 (= A68), G65 (= G69), A66 (≠ G70), D67 (≠ N71), I68 (≠ V72), L85 (≠ D91), W88 (≠ R94), G109 (≠ A122), P131 (≠ S144), L135 (≠ V148), G140 (= G153)
P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus (Rat) (see 3 papers)
35% identity, 96% coverage: 9:268/271 of query aligns to 35:287/290 of P14604
- E144 (≠ D125) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F145) mutation to D: Reduces activity 1250-fold.; mutation to Q: Reduces activity 330000-fold.
Sites not aligning to the query:
- 1:29 modified: transit peptide, Mitochondrion
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
34% identity, 96% coverage: 9:268/271 of query aligns to 5:255/258 of 1mj3A
- active site: A68 (≠ G70), M73 (= M75), S83 (≠ R94), L85 (vs. gap), G109 (≠ A122), E112 (≠ D125), P131 (≠ S144), E132 (≠ F145), T137 (≠ I150), P139 (= P152), G140 (= G153), K225 (≠ E238), F235 (≠ H248)
- binding hexanoyl-coenzyme a: K26 (≠ E27), A27 (≠ T28), L28 (≠ R29), A30 (= A31), A66 (= A68), G67 (= G69), A68 (≠ G70), D69 (≠ N71), I70 (≠ V72), G109 (≠ A122), P131 (≠ S144), E132 (≠ F145), L135 (≠ V148), G140 (= G153)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
34% identity, 97% coverage: 8:271/271 of query aligns to 5:261/261 of 5jbxB
- active site: A67 (≠ G70), R72 (= R78), L84 (≠ R94), R88 (≠ Q98), G112 (≠ A122), E115 (≠ D125), T134 (≠ S144), E135 (≠ F145), I140 (= I150), P142 (= P152), G143 (= G153), A228 (≠ E238), L238 (≠ H248)
- binding coenzyme a: S24 (≠ E27), R25 (≠ T28), R26 (= R29), A28 (= A31), A65 (= A68), D68 (= D74), L69 (≠ M75), K70 (≠ Q76), L110 (≠ I120), G111 (= G121), T134 (≠ S144), E135 (≠ F145), L138 (≠ V148), R168 (≠ T178)
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
34% identity, 94% coverage: 15:268/271 of query aligns to 18:268/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
37% identity, 78% coverage: 9:219/271 of query aligns to 2:189/224 of 3p85A
- active site: L62 (≠ G70), L67 (≠ M75), P68 (≠ Q76), G92 (≠ A122), E95 (≠ D125), T114 (≠ S144), H115 (≠ F145), L120 (≠ I150), P122 (= P152), T123 (≠ G153)
- binding calcium ion: D43 (= D51), D45 (≠ S53)
Sites not aligning to the query:
3rrvB Crystal structure of an enoyl-coa hydratase/isomerase from mycobacterium paratuberculosis (see paper)
33% identity, 93% coverage: 12:263/271 of query aligns to 10:253/254 of 3rrvB
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
34% identity, 91% coverage: 23:269/271 of query aligns to 39:279/285 of Q7CQ56
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 100% coverage: 1:271/271 of query aligns to 1:266/266 of O53561
- K135 (≠ L140) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 140:147, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K147) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
34% identity, 91% coverage: 23:269/271 of query aligns to 39:279/285 of 4i42A
- active site: G86 (= G70), R91 (≠ M75), Y97 (≠ I81), H105 (≠ V89), L109 (vs. gap), G133 (≠ A122), V136 (≠ D125), G156 (≠ F145), S161 (≠ I150), D163 (≠ P152), G164 (= G153), A250 (≠ S240), Y258 (≠ H248)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ T28), R45 (= R29), S84 (≠ A68), G85 (= G69), G86 (= G70), D87 (≠ N71), Q88 (≠ V72), K89 (= K73), Y97 (≠ I81), V108 (vs. gap), Y129 (≠ P118), G133 (≠ A122), T155 (≠ S144), S161 (≠ I150), T254 (≠ Q244), F270 (= F260), K273 (= K263)
Query Sequence
>Ac3H11_2719 FitnessBrowser__acidovorax_3H11:Ac3H11_2719
MSEQSPTPFLLIERDGPVLTARLNRPETRNALTDPAHMDELVALCRQIRADHSIKALVLT
GEGSAFCAGGNVKDMQQRGGIFAGSPYEVRDSYRDTIQRIPLALYELDVPVIAAVNGPAI
GAGLDLACMCDIRIASDKALFAESFVKVGIVPGDGGAWLLPRVIGMPKASLLAFTGDTID
AAKALSWGLVADVFPADQLLGQAQALAQRIALNPSHALRLTKRLLREGQHVRLDTLLELS
SAYQALSHHTEDHLEAVNAFLDKRPAQFTGR
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