SitesBLAST
Comparing GFF12 HP15_12 enoyl-CoA hydratase/isomerase 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
42% identity, 96% coverage: 13:270/270 of query aligns to 4:259/259 of 5zaiC
- active site: A65 (= A75), F70 (vs. gap), S82 (≠ R90), R86 (≠ A96), G110 (= G120), E113 (= E123), P132 (= P142), E133 (= E143), I138 (≠ L148), P140 (= P150), G141 (= G151), A226 (≠ D237), F236 (≠ A247)
- binding coenzyme a: K24 (≠ Q33), L25 (≠ I34), A63 (= A73), G64 (= G74), A65 (= A75), D66 (= D76), I67 (= I77), P132 (= P142), R166 (= R176), F248 (= F259), K251 (≠ R262)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
41% identity, 92% coverage: 19:267/270 of query aligns to 12:251/254 of 2dubA
- active site: A67 (= A75), M72 (≠ L87), S82 (≠ R97), G105 (= G120), E108 (= E123), P127 (= P142), E128 (= E143), T133 (≠ L148), P135 (= P150), G136 (= G151), K221 (≠ D237), F231 (≠ A247)
- binding octanoyl-coenzyme a: K25 (= K32), A26 (≠ Q33), L27 (≠ I34), A29 (= A36), A65 (= A73), A67 (= A75), D68 (= D76), I69 (= I77), K70 (= K78), G105 (= G120), E108 (= E123), P127 (= P142), E128 (= E143), G136 (= G151), A137 (≠ G152)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
41% identity, 92% coverage: 19:267/270 of query aligns to 13:255/258 of 1mj3A
- active site: A68 (= A75), M73 (≠ L87), S83 (≠ R97), L85 (≠ I99), G109 (= G120), E112 (= E123), P131 (= P142), E132 (= E143), T137 (≠ L148), P139 (= P150), G140 (= G151), K225 (≠ D237), F235 (≠ A247)
- binding hexanoyl-coenzyme a: K26 (= K32), A27 (≠ Q33), L28 (≠ I34), A30 (= A36), A66 (= A73), G67 (= G74), A68 (= A75), D69 (= D76), I70 (= I77), G109 (= G120), P131 (= P142), E132 (= E143), L135 (= L146), G140 (= G151)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
41% identity, 92% coverage: 19:267/270 of query aligns to 13:257/260 of 1dubA
- active site: A68 (= A75), M73 (≠ L87), S83 (vs. gap), L87 (vs. gap), G111 (= G120), E114 (= E123), P133 (= P142), E134 (= E143), T139 (≠ L148), P141 (= P150), G142 (= G151), K227 (≠ D237), F237 (≠ A247)
- binding acetoacetyl-coenzyme a: K26 (= K32), A27 (≠ Q33), L28 (≠ I34), A30 (= A36), A66 (= A73), A68 (= A75), D69 (= D76), I70 (= I77), Y107 (= Y116), G110 (= G119), G111 (= G120), E114 (= E123), P133 (= P142), E134 (= E143), L137 (= L146), G142 (= G151), F233 (= F243), F249 (= F259)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
41% identity, 92% coverage: 19:267/270 of query aligns to 11:255/258 of 1ey3A
- active site: A66 (= A75), M71 (≠ L87), S81 (vs. gap), L85 (vs. gap), G109 (= G120), E112 (= E123), P131 (= P142), E132 (= E143), T137 (≠ L148), P139 (= P150), G140 (= G151), K225 (≠ D237), F235 (≠ A247)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K32), L26 (≠ I34), A28 (= A36), A64 (= A73), G65 (= G74), A66 (= A75), D67 (= D76), I68 (= I77), L85 (vs. gap), W88 (= W98), G109 (= G120), P131 (= P142), L135 (= L146), G140 (= G151)
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)
41% identity, 92% coverage: 19:267/270 of query aligns to 43:287/290 of P14604
- E144 (= E123) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E143) 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
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
40% identity, 92% coverage: 19:267/270 of query aligns to 13:257/260 of 2hw5C
- active site: A68 (= A75), M73 (≠ R80), S83 (≠ R92), L87 (≠ A96), G111 (= G120), E114 (= E123), P133 (= P142), E134 (= E143), T139 (≠ L148), P141 (= P150), G142 (= G151), K227 (≠ D237), F237 (≠ A247)
- binding crotonyl coenzyme a: K26 (= K32), A27 (≠ Q33), L28 (≠ I34), A30 (= A36), K62 (≠ R69), I70 (= I77), F109 (≠ M118)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
39% identity, 91% coverage: 25:269/270 of query aligns to 18:260/261 of 5jbxB
- active site: A67 (= A75), R72 (= R80), L84 (≠ M93), R88 (≠ A96), G112 (= G120), E115 (= E123), T134 (≠ P142), E135 (= E143), I140 (≠ L148), P142 (= P150), G143 (= G151), A228 (≠ D237), L238 (≠ A247)
- binding coenzyme a: S24 (≠ P31), R25 (≠ K32), R26 (≠ Q33), A28 (= A36), A65 (= A73), D68 (= D76), L69 (≠ I77), K70 (= K78), L110 (≠ M118), G111 (= G119), T134 (≠ P142), E135 (= E143), L138 (= L146), R168 (= R176)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 93% coverage: 17:267/270 of query aligns to 7:249/250 of 3q0gD
- active site: A64 (= A75), M69 (≠ R80), T75 (≠ S86), F79 (≠ C95), G103 (= G120), E106 (= E123), P125 (= P142), E126 (= E143), V131 (≠ L148), P133 (= P150), G134 (= G151), L219 (≠ D237), F229 (≠ A247)
- binding Butyryl Coenzyme A: F225 (= F243), F241 (= F259)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
37% identity, 93% coverage: 17:267/270 of query aligns to 8:254/255 of 3q0jC
- active site: A65 (= A75), M70 (≠ R80), T80 (≠ R90), F84 (≠ C95), G108 (= G120), E111 (= E123), P130 (= P142), E131 (= E143), V136 (≠ L148), P138 (= P150), G139 (= G151), L224 (≠ D237), F234 (≠ A247)
- binding acetoacetyl-coenzyme a: Q23 (≠ K32), A24 (≠ Q33), L25 (≠ I34), A27 (= A36), A63 (= A73), G64 (= G74), A65 (= A75), D66 (= D76), I67 (= I77), K68 (= K78), M70 (≠ R80), F84 (≠ C95), G107 (= G119), G108 (= G120), E111 (= E123), P130 (= P142), E131 (= E143), P138 (= P150), G139 (= G151), M140 (≠ G152)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 93% coverage: 17:267/270 of query aligns to 8:254/255 of 3q0gC
- active site: A65 (= A75), M70 (≠ R80), T80 (≠ R90), F84 (≠ C95), G108 (= G120), E111 (= E123), P130 (= P142), E131 (= E143), V136 (≠ L148), P138 (= P150), G139 (= G151), L224 (≠ D237), F234 (≠ A247)
- binding coenzyme a: L25 (≠ I34), A63 (= A73), I67 (= I77), K68 (= K78), Y104 (= Y116), P130 (= P142), E131 (= E143), L134 (= L146)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
37% identity, 93% coverage: 17:267/270 of query aligns to 7:253/256 of 3h81A
- active site: A64 (= A75), M69 (≠ R80), T79 (≠ R90), F83 (≠ C95), G107 (= G120), E110 (= E123), P129 (= P142), E130 (= E143), V135 (≠ L148), P137 (= P150), G138 (= G151), L223 (≠ D237), F233 (≠ A247)
- binding calcium ion: F233 (≠ A247), Q238 (≠ A252)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 93% coverage: 19:269/270 of query aligns to 9:256/257 of 6slbAAA
- active site: Q64 (≠ A75), F69 (vs. gap), L80 (≠ V89), N84 (≠ A96), A108 (≠ G120), S111 (≠ E123), A130 (≠ P142), F131 (≠ E143), L136 (= L148), P138 (= P150), D139 (≠ G151), A224 (≠ D237), G234 (≠ A247)
- 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 (= R69), A62 (= A73), Q64 (≠ A75), D65 (= D76), L66 (≠ I77), Y76 (≠ N85), A108 (≠ G120), F131 (≠ E143), D139 (≠ G151)
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)
38% identity, 92% coverage: 22:270/270 of query aligns to 86:339/339 of Q13825
- K105 (≠ D39) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 39:53, 7% identical) RNA-binding
- K109 (≠ V43) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ E47) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G174) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 93% coverage: 19:269/270 of query aligns to 6:244/245 of 6slaAAA
- active site: Q61 (≠ A75), L68 (≠ V89), N72 (≠ A96), A96 (≠ G120), S99 (≠ E123), A118 (≠ P142), F119 (≠ E143), L124 (= L148), P126 (= P150), N127 (≠ G151), A212 (≠ D237), G222 (≠ A247)
- 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 (≠ I34), A59 (= A73), Q61 (≠ A75), D62 (= D76), L63 (≠ I77), L68 (≠ V89), Y71 (≠ C95), A94 (≠ M118), G95 (= G119), A96 (≠ G120), F119 (≠ E143), I122 (≠ L146), L124 (= L148), N127 (≠ G151), F234 (= F259), K237 (≠ R262)
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)
32% identity, 87% coverage: 15:248/270 of query aligns to 41:276/763 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
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 97% coverage: 7:267/270 of query aligns to 3:263/266 of O53561
- K135 (≠ V138) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 138:145, 13% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ G145) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
41% identity, 58% coverage: 18:174/270 of query aligns to 6:155/692 of 6iunB
Sites not aligning to the query:
- active site: 248, 407, 428, 440, 478
- binding nicotinamide-adenine-dinucleotide: 300, 301, 302, 321, 322, 365, 377, 378, 380, 384, 388, 405, 407
Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
31% identity, 90% coverage: 26:267/270 of query aligns to 24:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
37% identity, 69% coverage: 22:208/270 of query aligns to 12:201/707 of 6yswA
- active site: A66 (= A75), I71 (vs. gap), A84 (≠ V89), Q88 (≠ M93), G112 (= G120), E115 (= E123), P136 (= P142), E137 (= E143), G145 (= G151)
- binding coenzyme a: E23 (≠ K32), M25 (≠ I34), A66 (= A75), D67 (= D76), I68 (= I77), P136 (= P142), E137 (= E143), L140 (= L146)
Sites not aligning to the query:
Query Sequence
>GFF12 HP15_12 enoyl-CoA hydratase/isomerase
MSLPEKVVESINDAVNVCRDGNVGWVILNRPKQINAINDEIRVGVPEALEQFEKDKEIRV
IVIRGEGERGLCAGADIKERRGPENSLQVRKRMECARWIESIDQTTKPVIVAIHGYCMGG
GLELALACDIRYASPNAVMALPETGLGLIPGGGGTQRLSRVVAPGHALDMLLSGDRLDAA
RARSIGLVTRVAETQESLLQEVSELAQKIAMKPPLATTYVKRAARASLELELKRGLDLEL
DLFALLAPTEDAREAASAFSERRSPNFIGE
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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