SitesBLAST
Comparing Ac3H11_2775 FitnessBrowser__acidovorax_3H11:Ac3H11_2775 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
43% identity, 92% coverage: 23:279/279 of query aligns to 5:259/259 of 5zaiC
- active site: A65 (= A84), F70 (≠ R89), S82 (≠ M102), R86 (= R106), G110 (= G129), E113 (= E132), P132 (= P151), E133 (= E152), I138 (≠ L157), P140 (= P159), G141 (= G160), A226 (≠ D246), F236 (≠ V256)
- binding coenzyme a: K24 (≠ Q42), L25 (≠ I43), A63 (= A82), G64 (= G83), A65 (= A84), D66 (= D85), I67 (= I86), P132 (= P151), R166 (= R185), F248 (= F268), K251 (= K271)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
42% identity, 91% coverage: 25:278/279 of query aligns to 8:260/261 of 5jbxB
- active site: A67 (= A84), R72 (= R89), L84 (≠ M102), R88 (≠ S105), G112 (= G129), E115 (= E132), T134 (≠ P151), E135 (= E152), I140 (≠ L157), P142 (= P159), G143 (= G160), A228 (≠ D246), L238 (≠ V256)
- binding coenzyme a: S24 (≠ D41), R25 (≠ Q42), R26 (≠ I43), A28 (= A45), A65 (= A82), D68 (= D85), L69 (≠ I86), K70 (= K87), L110 (≠ M127), G111 (= G128), T134 (≠ P151), E135 (= E152), L138 (= L155), R168 (= R185)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
42% identity, 90% coverage: 26:277/279 of query aligns to 7:250/250 of 3q0gD
- active site: A64 (= A84), M69 (≠ R89), T75 (≠ S95), F79 (≠ R99), G103 (= G129), E106 (= E132), P125 (= P151), E126 (= E152), V131 (≠ L157), P133 (= P159), G134 (= G160), L219 (≠ D246), F229 (≠ V256)
- binding Butyryl Coenzyme A: F225 (= F252), F241 (= F268)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
40% identity, 90% coverage: 27:276/279 of query aligns to 9:257/260 of 2hw5C
- active site: A68 (= A84), M73 (≠ R89), S83 (≠ R99), L87 (≠ Q103), G111 (= G129), E114 (= E132), P133 (= P151), E134 (= E152), T139 (≠ L157), P141 (= P159), G142 (= G160), K227 (≠ D246), F237 (≠ V256)
- binding crotonyl coenzyme a: K26 (≠ D41), A27 (≠ Q42), L28 (≠ I43), A30 (= A45), K62 (≠ R78), I70 (= I86), F109 (≠ M127)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
43% identity, 90% coverage: 26:277/279 of query aligns to 8:255/255 of 3q0jC
- active site: A65 (= A84), M70 (≠ R89), T80 (≠ R100), F84 (≠ K104), G108 (= G129), E111 (= E132), P130 (= P151), E131 (= E152), V136 (≠ L157), P138 (= P159), G139 (= G160), L224 (≠ D246), F234 (≠ V256)
- binding acetoacetyl-coenzyme a: Q23 (≠ D41), A24 (≠ Q42), L25 (≠ I43), A27 (= A45), A63 (= A82), G64 (= G83), A65 (= A84), D66 (= D85), I67 (= I86), K68 (= K87), M70 (≠ R89), F84 (≠ K104), G107 (= G128), G108 (= G129), E111 (= E132), P130 (= P151), E131 (= E152), P138 (= P159), G139 (= G160), M140 (≠ G161)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
43% identity, 90% coverage: 26:277/279 of query aligns to 8:255/255 of 3q0gC
- active site: A65 (= A84), M70 (≠ R89), T80 (≠ R100), F84 (≠ K104), G108 (= G129), E111 (= E132), P130 (= P151), E131 (= E152), V136 (≠ L157), P138 (= P159), G139 (= G160), L224 (≠ D246), F234 (≠ V256)
- binding coenzyme a: L25 (≠ I43), A63 (= A82), I67 (= I86), K68 (= K87), Y104 (= Y125), P130 (= P151), E131 (= E152), L134 (= L155)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
43% identity, 90% coverage: 26:277/279 of query aligns to 7:254/256 of 3h81A
- active site: A64 (= A84), M69 (≠ R89), T79 (≠ R100), F83 (≠ K104), G107 (= G129), E110 (= E132), P129 (= P151), E130 (= E152), V135 (≠ L157), P137 (= P159), G138 (= G160), L223 (≠ D246), F233 (≠ V256)
- binding calcium ion: F233 (≠ V256), Q238 (≠ V261)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
39% identity, 89% coverage: 28:276/279 of query aligns to 12:251/254 of 2dubA
- active site: A67 (= A84), M72 (≠ R89), S82 (= S105), G105 (= G129), E108 (= E132), P127 (= P151), E128 (= E152), T133 (≠ L157), P135 (= P159), G136 (= G160), K221 (≠ D246), F231 (≠ V256)
- binding octanoyl-coenzyme a: K25 (≠ D41), A26 (≠ Q42), L27 (≠ I43), A29 (= A45), A65 (= A82), A67 (= A84), D68 (= D85), I69 (= I86), K70 (= K87), G105 (= G129), E108 (= E132), P127 (= P151), E128 (= E152), G136 (= G160), A137 (≠ G161)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
39% identity, 89% coverage: 28:276/279 of query aligns to 13:255/258 of 1mj3A
- active site: A68 (= A84), M73 (≠ R89), S83 (vs. gap), L85 (vs. gap), G109 (= G129), E112 (= E132), P131 (= P151), E132 (= E152), T137 (≠ L157), P139 (= P159), G140 (= G160), K225 (≠ D246), F235 (≠ V256)
- binding hexanoyl-coenzyme a: K26 (≠ D41), A27 (≠ Q42), L28 (≠ I43), A30 (= A45), A66 (= A82), G67 (= G83), A68 (= A84), D69 (= D85), I70 (= I86), G109 (= G129), P131 (= P151), E132 (= E152), L135 (= L155), G140 (= G160)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
39% identity, 89% coverage: 28:276/279 of query aligns to 11:255/258 of 1ey3A
- active site: A66 (= A84), M71 (≠ R89), S81 (≠ R100), L85 (≠ K104), G109 (= G129), E112 (= E132), P131 (= P151), E132 (= E152), T137 (≠ L157), P139 (= P159), G140 (= G160), K225 (≠ D246), F235 (≠ V256)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D41), L26 (≠ I43), A28 (= A45), A64 (= A82), G65 (= G83), A66 (= A84), D67 (= D85), I68 (= I86), L85 (≠ K104), W88 (= W107), G109 (= G129), P131 (= P151), L135 (= L155), G140 (= G160)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
39% identity, 89% coverage: 28:276/279 of query aligns to 13:257/260 of 1dubA
- active site: A68 (= A84), M73 (≠ R89), S83 (≠ R100), L87 (≠ K104), G111 (= G129), E114 (= E132), P133 (= P151), E134 (= E152), T139 (≠ L157), P141 (= P159), G142 (= G160), K227 (≠ D246), F237 (≠ V256)
- binding acetoacetyl-coenzyme a: K26 (≠ D41), A27 (≠ Q42), L28 (≠ I43), A30 (= A45), A66 (= A82), A68 (= A84), D69 (= D85), I70 (= I86), Y107 (= Y125), G110 (= G128), G111 (= G129), E114 (= E132), P133 (= P151), E134 (= E152), L137 (= L155), G142 (= G160), F233 (= F252), F249 (= F268)
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)
39% identity, 89% coverage: 28:276/279 of query aligns to 43:287/290 of P14604
- E144 (= E132) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E152) 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
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 90% coverage: 27:278/279 of query aligns to 8:256/257 of 6slbAAA
- active site: Q64 (≠ A84), F69 (vs. gap), L80 (≠ V98), N84 (≠ S105), A108 (≠ G129), S111 (≠ E132), A130 (≠ P151), F131 (≠ E152), L136 (= L157), P138 (= P159), D139 (≠ G160), A224 (≠ D246), G234 (≠ V256)
- 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 (= R78), A62 (= A82), Q64 (≠ A84), D65 (= D85), L66 (≠ I86), Y76 (≠ T94), A108 (≠ G129), F131 (≠ E152), D139 (≠ G160)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 90% coverage: 27:278/279 of query aligns to 5:244/245 of 6slaAAA
- active site: Q61 (≠ A84), L68 (≠ V98), N72 (≠ S105), A96 (≠ G129), S99 (≠ E132), A118 (≠ P151), F119 (≠ E152), L124 (= L157), P126 (= P159), N127 (≠ G160), A212 (≠ D246), G222 (≠ V256)
- 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 (≠ I43), A59 (= A82), Q61 (≠ A84), D62 (= D85), L63 (≠ I86), L68 (≠ V98), Y71 (≠ K104), A94 (≠ M127), G95 (= G128), A96 (≠ G129), F119 (≠ E152), I122 (≠ L155), L124 (= L157), N127 (≠ G160), F234 (= F268), K237 (= K271)
Q13825 Methylglutaconyl-CoA hydratase, mitochondrial; 3-MG-CoA hydratase; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding protein/enoyl-CoA hydratase; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56 from Homo sapiens (Human) (see 4 papers)
39% identity, 92% coverage: 24:279/279 of query aligns to 82:339/339 of Q13825
- K105 (≠ D48) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 48:62, 13% identical) RNA-binding
- K109 (≠ R52) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ A56) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G183) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
33% identity, 84% coverage: 23:255/279 of query aligns to 9:236/244 of 6l3pA
- active site: M69 (≠ A84), Y74 (≠ R89), R86 (≠ M102), Q90 (≠ R106), G114 (= G129), S117 (≠ E132), S136 (≠ P151), E137 (= E152), I142 (≠ L157), P144 (= P159), G145 (= G160), Y233 (≠ F252)
- binding coenzyme a: K28 (≠ Q42), R29 (≠ I43), A31 (= A45), A67 (= A82), M69 (≠ A84), D70 (= D85), L71 (≠ I86), G113 (= G128)
Sites not aligning to the query:
P40939 Trifunctional enzyme subunit alpha, mitochondrial; 78 kDa gastrin-binding protein; Monolysocardiolipin acyltransferase; TP-alpha; EC 2.3.1.-; EC 4.2.1.17; EC 1.1.1.211 from Homo sapiens (Human) (see 5 papers)
33% identity, 82% coverage: 29:258/279 of query aligns to 46:277/763 of P40939
Sites not aligning to the query:
- 282 V → D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- 305 I → N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- 342 L → P: in LCHAD deficiency; dbSNP:rs137852772
- 510 active site, For hydroxyacyl-coenzyme A dehydrogenase activity; E → Q: in AFLP and LCHAD deficiency; loss of long-chain-3-hydroxyacyl-CoA dehydrogenase activity; dbSNP:rs137852769
3bptA Crystal structure of human beta-hydroxyisobutyryl-coa hydrolase in complex with quercetin
32% identity, 85% coverage: 28:263/279 of query aligns to 11:248/362 of 3bptA
- active site: G67 (≠ A84), P84 (vs. gap), R88 (= R101), G115 (= G129), G118 (≠ E132), E138 (= E152), D146 (≠ G160)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G83), G67 (≠ A84), I69 (= I86), E90 (≠ K104), G114 (= G128), G115 (= G129), E138 (= E152), D146 (≠ G160), V147 (≠ G161)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ Q42), L26 (≠ I43), A28 (= A45), G66 (= G83), G67 (≠ A84), I69 (= I86), P137 (= P151), I141 (≠ L155)
Sites not aligning to the query:
7xwtB Crystal structure of feruoyl-coa hydratase/lyase complexed with coa from sphingomonas paucimobilis (see paper)
32% identity, 82% coverage: 22:251/279 of query aligns to 6:237/277 of 7xwtB
- binding acetyl coenzyme *a: T25 (≠ D41), K26 (≠ Q42), R27 (≠ I43), A29 (= A45), A65 (= A82), G66 (= G83), M67 (≠ A84), D68 (= D85), L69 (≠ I86), F73 (vs. gap), F114 (≠ M127), G116 (= G129), S138 (≠ P151), W142 (≠ L155)
7xwvA Feruloyl-coa hydratase/lyase complexed with vanillin and coenzyme a (see paper)
32% identity, 82% coverage: 22:251/279 of query aligns to 5:236/244 of 7xwvA
- binding coenzyme a: T24 (≠ D41), K25 (≠ Q42), R26 (≠ I43), A64 (= A82), G65 (= G83), M66 (≠ A84), D67 (= D85), L68 (≠ I86), W111 (≠ Y125), F113 (≠ M127), G114 (= G128), G115 (= G129), S137 (≠ P151)
- binding 4-hydroxy-3-methoxybenzaldehyde: M66 (≠ A84), Y71 (vs. gap), F72 (vs. gap), E138 (= E152), G146 (= G160), G147 (= G161)
Query Sequence
>Ac3H11_2775 FitnessBrowser__acidovorax_3H11:Ac3H11_2775
MMETSFHKPATPTRDEAAAPGNAVEVERRGGVGWIVLNRPDQINAINDDIRRGVPAALAE
LDSDPSVRVIVIRGAGARGFCAGADIKERRAAETSVQVRRRMQKSRWIEALDRTEKPVIA
AIHGYCMGGGMELALACDLRFAASDAVFALPETGLGLIPGGGGTQRLGAVVGPGRALDLL
LTGDRVDARRAFDIGLITRMADSADSLLAEVTALAERIAQKPPTATLFAKQAARAACHLD
LKSGLDLELDLFAMLVPMNDVKEAALAFREKRAPCFSGE
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