SitesBLAST
Comparing WP_011765660.1 NCBI__GCF_000061505.1:WP_011765660.1 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)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
51% identity, 94% coverage: 16:262/264 of query aligns to 10:256/258 of 1ey3A
- active site: A66 (= A72), M71 (= M77), S81 (≠ L87), L85 (≠ P91), G109 (= G115), E112 (= E118), P131 (= P137), E132 (= E138), T137 (≠ I143), P139 (= P145), G140 (= G146), K225 (≠ A231), F235 (≠ A241)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ Q30), L26 (≠ K32), A28 (= A34), A64 (= A70), G65 (= G71), A66 (= A72), D67 (= D73), I68 (≠ L74), L85 (≠ P91), W88 (≠ F94), G109 (= G115), P131 (= P137), L135 (= L141), G140 (= G146)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
51% identity, 94% coverage: 16:262/264 of query aligns to 12:258/260 of 1dubA
- active site: A68 (= A72), M73 (= M77), S83 (≠ L87), L87 (≠ P91), G111 (= G115), E114 (= E118), P133 (= P137), E134 (= E138), T139 (≠ I143), P141 (= P145), G142 (= G146), K227 (≠ A231), F237 (≠ A241)
- binding acetoacetyl-coenzyme a: K26 (≠ Q30), A27 (= A31), L28 (≠ K32), A30 (= A34), A66 (= A70), A68 (= A72), D69 (= D73), I70 (≠ L74), Y107 (= Y111), G110 (= G114), G111 (= G115), E114 (= E118), P133 (= P137), E134 (= E138), L137 (= L141), G142 (= G146), F233 (= F237), F249 (= F253)
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)
51% identity, 94% coverage: 16:262/264 of query aligns to 42:288/290 of P14604
- E144 (= E118) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E138) 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
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
51% identity, 94% coverage: 16:262/264 of query aligns to 11:252/254 of 2dubA
- active site: A67 (= A72), M72 (= M77), S82 (≠ L87), G105 (= G115), E108 (= E118), P127 (= P137), E128 (= E138), T133 (≠ I143), P135 (= P145), G136 (= G146), K221 (≠ A231), F231 (≠ A241)
- binding octanoyl-coenzyme a: K25 (≠ Q30), A26 (= A31), L27 (≠ K32), A29 (= A34), A65 (= A70), A67 (= A72), D68 (= D73), I69 (≠ L74), K70 (≠ A75), G105 (= G115), E108 (= E118), P127 (= P137), E128 (= E138), G136 (= G146), A137 (= A147)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
51% identity, 94% coverage: 16:262/264 of query aligns to 12:256/258 of 1mj3A
- active site: A68 (= A72), M73 (= M77), S83 (≠ E89), L85 (≠ P91), G109 (= G115), E112 (= E118), P131 (= P137), E132 (= E138), T137 (≠ I143), P139 (= P145), G140 (= G146), K225 (≠ A231), F235 (≠ A241)
- binding hexanoyl-coenzyme a: K26 (≠ Q30), A27 (= A31), L28 (≠ K32), A30 (= A34), A66 (= A70), G67 (= G71), A68 (= A72), D69 (= D73), I70 (≠ L74), G109 (= G115), P131 (= P137), E132 (= E138), L135 (= L141), G140 (= G146)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
48% identity, 94% coverage: 16:264/264 of query aligns to 12:260/260 of 2hw5C
- active site: A68 (= A72), M73 (= M77), S83 (≠ L87), L87 (≠ P91), G111 (= G115), E114 (= E118), P133 (= P137), E134 (= E138), T139 (≠ I143), P141 (= P145), G142 (= G146), K227 (≠ A231), F237 (≠ A241)
- binding crotonyl coenzyme a: K26 (≠ Q30), A27 (= A31), L28 (≠ K32), A30 (= A34), K62 (≠ Q66), I70 (≠ L74), F109 (≠ L113)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
44% identity, 91% coverage: 24:264/264 of query aligns to 16:256/256 of 3h81A
- active site: A64 (= A72), M69 (= M77), T79 (≠ L87), F83 (≠ P91), G107 (= G115), E110 (= E118), P129 (= P137), E130 (= E138), V135 (≠ I143), P137 (= P145), G138 (= G146), L223 (≠ A231), F233 (≠ A241)
- binding calcium ion: F233 (≠ A241), Q238 (≠ R246)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
44% identity, 90% coverage: 24:261/264 of query aligns to 17:254/255 of 3q0jC
- active site: A65 (= A72), M70 (= M77), T80 (≠ L87), F84 (≠ P91), G108 (= G115), E111 (= E118), P130 (= P137), E131 (= E138), V136 (≠ I143), P138 (= P145), G139 (= G146), L224 (≠ A231), F234 (≠ A241)
- binding acetoacetyl-coenzyme a: Q23 (= Q30), A24 (= A31), L25 (≠ K32), A27 (= A34), A63 (= A70), G64 (= G71), A65 (= A72), D66 (= D73), I67 (≠ L74), K68 (≠ A75), M70 (= M77), F84 (≠ P91), G107 (= G114), G108 (= G115), E111 (= E118), P130 (= P137), E131 (= E138), P138 (= P145), G139 (= G146), M140 (≠ A147)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
44% identity, 90% coverage: 24:261/264 of query aligns to 17:254/255 of 3q0gC
- active site: A65 (= A72), M70 (= M77), T80 (≠ L87), F84 (≠ P91), G108 (= G115), E111 (= E118), P130 (= P137), E131 (= E138), V136 (≠ I143), P138 (= P145), G139 (= G146), L224 (≠ A231), F234 (≠ A241)
- binding coenzyme a: L25 (≠ K32), A63 (= A70), I67 (≠ L74), K68 (≠ A75), Y104 (= Y111), P130 (= P137), E131 (= E138), L134 (= L141)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
45% identity, 90% coverage: 24:261/264 of query aligns to 16:249/250 of 3q0gD
- active site: A64 (= A72), M69 (= M77), T75 (≠ Q83), F79 (≠ L87), G103 (= G115), E106 (= E118), P125 (= P137), E126 (= E138), V131 (≠ I143), P133 (= P145), G134 (= G146), L219 (≠ A231), F229 (≠ A241)
- binding Butyryl Coenzyme A: F225 (= F237), F241 (= F253)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
43% identity, 94% coverage: 18:264/264 of query aligns to 11:259/259 of 5zaiC
- active site: A65 (= A72), F70 (≠ M77), S82 (≠ E88), R86 (= R92), G110 (= G115), E113 (= E118), P132 (= P137), E133 (= E138), I138 (= I143), P140 (= P145), G141 (= G146), A226 (= A231), F236 (≠ A241)
- binding coenzyme a: K24 (≠ A31), L25 (≠ K32), A63 (= A70), G64 (= G71), A65 (= A72), D66 (= D73), I67 (≠ L74), P132 (= P137), R166 (≠ F171), F248 (= F253), K251 (= K256)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
41% identity, 93% coverage: 20:264/264 of query aligns to 13:261/261 of 5jbxB
- active site: A67 (= A72), R72 (≠ M77), L84 (= L87), R88 (≠ P91), G112 (= G115), E115 (= E118), T134 (≠ P137), E135 (= E138), I140 (= I143), P142 (= P145), G143 (= G146), A228 (= A231), L238 (≠ A241)
- binding coenzyme a: S24 (≠ Q30), R25 (≠ A31), R26 (≠ K32), A28 (= A34), A65 (= A70), D68 (= D73), L69 (= L74), K70 (≠ A75), L110 (= L113), G111 (= G114), T134 (≠ P137), E135 (= E138), L138 (= L141), R168 (≠ F171)
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)
35% identity, 99% coverage: 1:262/264 of query aligns to 1:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
34% identity, 96% coverage: 12:264/264 of query aligns to 3:266/266 of O53561
- K135 (≠ Q133) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 133:140, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ N140) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 96% coverage: 11:264/264 of query aligns to 3:257/257 of 6slbAAA
- active site: Q64 (≠ A72), F69 (≠ M77), L80 (= L86), N84 (≠ P91), A108 (≠ G115), S111 (≠ E118), A130 (≠ P137), F131 (≠ E138), L136 (≠ I143), P138 (= P145), D139 (≠ G146), A224 (= A231), G234 (vs. gap)
- 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 (≠ Q66), A62 (= A70), Q64 (≠ A72), D65 (= D73), L66 (= L74), Y76 (≠ M82), A108 (≠ G115), F131 (≠ E138), D139 (≠ G146)
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)
37% identity, 93% coverage: 18:263/264 of query aligns to 86:338/339 of Q13825
- K105 (≠ T37) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 37:51, 7% identical) RNA-binding
- K109 (≠ R41) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ A45) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G169) 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)
35% identity, 93% coverage: 20:264/264 of query aligns to 9:245/245 of 6slaAAA
- active site: Q61 (≠ A72), L68 (= L87), N72 (≠ P91), A96 (≠ G115), S99 (≠ E118), A118 (≠ P137), F119 (≠ E138), L124 (≠ I143), P126 (= P145), N127 (≠ G146), A212 (= A231), G222 (vs. gap)
- 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 (≠ K32), A59 (= A70), Q61 (≠ A72), D62 (= D73), L63 (= L74), L68 (= L87), Y71 (≠ R90), A94 (≠ L113), G95 (= G114), A96 (≠ G115), F119 (≠ E138), I122 (≠ L141), L124 (≠ I143), N127 (≠ G146), F234 (= F253), K237 (= K256)
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)
36% identity, 94% coverage: 14:262/264 of query aligns to 17:269/296 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)
34% identity, 84% coverage: 12:233/264 of query aligns to 2:210/224 of 3p85A
- active site: L62 (≠ A72), L67 (≠ M77), P68 (= P91), G92 (= G115), E95 (= E118), T114 (≠ P137), H115 (≠ E138), L120 (≠ I143), P122 (= P145), T123 (≠ G146), W208 (≠ A231)
- binding calcium ion: D43 (= D53), D45 (≠ A55)
Sites not aligning to the query:
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
27% identity, 97% coverage: 1:257/264 of query aligns to 49:317/327 of Q62651
- D176 (≠ E118) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E138) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ G146) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
Query Sequence
>WP_011765660.1 NCBI__GCF_000061505.1:WP_011765660.1
MTDKAYLPGEGVIVAGPDAGVLEIRLDRPQAKNALSTPLLRSIVALLEQAEHDDAVRCIV
LTGGDQVFAAGADLAEMAAKDMQAVLLEERPRLFGAIARFPKPIIAAVCGYALGGGCELV
MHADIVIAGESAQFGQPEINLGIIPGAGGTQRLTRAVGKSVAMKLVLAGEFIPAQEARAA
GLVAEVVADEACIARAHELAGKIAKKAPLAVRLAKDSVLQAFETPLAAGLAIERRNFVVL
AGTEDRNEGVKSFLEKRKPVWKGR
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