SitesBLAST
Comparing WP_011911840.1 NCBI__GCF_000013785.1:WP_011911840.1 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
38% identity, 97% coverage: 8:261/261 of query aligns to 3:259/259 of 5zaiC
- active site: A65 (= A65), F70 (≠ V70), S82 (≠ L84), R86 (≠ N88), G110 (= G112), E113 (= E115), P132 (≠ A134), E133 (≠ H135), I138 (≠ V140), P140 (= P142), G141 (= G143), A226 (≠ L228), F236 (≠ L238)
- binding coenzyme a: K24 (≠ A24), L25 (≠ M25), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), P132 (≠ A134), R166 (≠ S168), F248 (= F250), K251 (= K253)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 97% coverage: 5:258/261 of query aligns to 4:249/250 of 3q0gD
- active site: A64 (= A65), M69 (≠ V70), T75 (≠ L76), F79 (≠ L84), G103 (= G112), E106 (= E115), P125 (≠ A134), E126 (≠ H135), V131 (= V140), P133 (= P142), G134 (= G143), L219 (= L228), F229 (≠ L238)
- binding Butyryl Coenzyme A: F225 (≠ L234), F241 (= F250)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
36% identity, 99% coverage: 1:258/261 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (= A65), M70 (≠ V70), T80 (≠ E80), F84 (≠ L84), G108 (= G112), E111 (= E115), P130 (≠ A134), E131 (≠ H135), V136 (= V140), P138 (= P142), G139 (= G143), L224 (= L228), F234 (≠ L238)
- binding acetoacetyl-coenzyme a: Q23 (≠ K23), A24 (= A24), L25 (≠ M25), A27 (≠ S27), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (≠ L67), K68 (= K68), M70 (≠ V70), F84 (≠ L84), G107 (≠ A111), G108 (= G112), E111 (= E115), P130 (≠ A134), E131 (≠ H135), P138 (= P142), G139 (= G143), M140 (≠ A144)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 99% coverage: 1:258/261 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A65), M70 (≠ V70), T80 (≠ E80), F84 (≠ L84), G108 (= G112), E111 (= E115), P130 (≠ A134), E131 (≠ H135), V136 (= V140), P138 (= P142), G139 (= G143), L224 (= L228), F234 (≠ L238)
- binding coenzyme a: L25 (≠ M25), A63 (= A63), I67 (≠ L67), K68 (= K68), Y104 (≠ V108), P130 (≠ A134), E131 (≠ H135), L134 (≠ F138)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
36% identity, 98% coverage: 5:261/261 of query aligns to 4:256/256 of 3h81A
- active site: A64 (= A65), M69 (≠ V70), T79 (≠ E80), F83 (≠ L84), G107 (= G112), E110 (= E115), P129 (≠ A134), E130 (≠ H135), V135 (= V140), P137 (= P142), G138 (= G143), L223 (= L228), F233 (≠ L238)
- binding calcium ion: F233 (≠ L238), Q238 (≠ L243)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 94% coverage: 14:259/261 of query aligns to 17:258/260 of 1dubA
- active site: A68 (= A65), M73 (≠ V70), S83 (≠ E80), L87 (= L84), G111 (= G112), E114 (= E115), P133 (≠ A134), E134 (≠ H135), T139 (≠ V140), P141 (= P142), G142 (= G143), K227 (≠ L228), F237 (≠ L238)
- binding acetoacetyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (≠ M25), A30 (≠ S27), A66 (= A63), A68 (= A65), D69 (= D66), I70 (≠ L67), Y107 (≠ V108), G110 (≠ A111), G111 (= G112), E114 (= E115), P133 (≠ A134), E134 (≠ H135), L137 (≠ F138), G142 (= G143), F233 (≠ L234), F249 (= F250)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
36% identity, 94% coverage: 14:259/261 of query aligns to 17:258/260 of 2hw5C
- active site: A68 (= A65), M73 (≠ V70), S83 (≠ E80), L87 (= L84), G111 (= G112), E114 (= E115), P133 (≠ A134), E134 (≠ H135), T139 (≠ V140), P141 (= P142), G142 (= G143), K227 (≠ L228), F237 (≠ L238)
- binding crotonyl coenzyme a: K26 (= K23), A27 (= A24), L28 (≠ M25), A30 (≠ S27), K62 (≠ P59), I70 (≠ L67), F109 (≠ M110)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 94% coverage: 14:259/261 of query aligns to 15:256/258 of 1ey3A
- active site: A66 (= A65), M71 (≠ V70), S81 (≠ E80), L85 (= L84), G109 (= G112), E112 (= E115), P131 (≠ A134), E132 (≠ H135), T137 (≠ V140), P139 (= P142), G140 (= G143), K225 (≠ L228), F235 (≠ L238)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K23), L26 (≠ M25), A28 (≠ S27), A64 (= A63), G65 (= G64), A66 (= A65), D67 (= D66), I68 (≠ L67), L85 (= L84), W88 (≠ A87), G109 (= G112), P131 (≠ A134), L135 (≠ F138), G140 (= G143)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
36% identity, 96% coverage: 12:261/261 of query aligns to 13:261/261 of 5jbxB
- active site: A67 (= A65), R72 (≠ V70), L84 (= L84), R88 (≠ N88), G112 (= G112), E115 (= E115), T134 (≠ A134), E135 (≠ H135), I140 (≠ V140), P142 (= P142), G143 (= G143), A228 (≠ L228), L238 (= L238)
- binding coenzyme a: S24 (≠ K23), R25 (≠ A24), R26 (≠ M25), A28 (≠ S27), A65 (= A63), D68 (= D66), L69 (= L67), K70 (= K68), L110 (≠ M110), G111 (≠ A111), T134 (≠ A134), E135 (≠ H135), L138 (≠ F138), R168 (≠ S168)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 94% coverage: 17:261/261 of query aligns to 13:245/245 of 6slaAAA
- active site: Q61 (≠ A65), L68 (= L84), N72 (= N88), A96 (≠ G112), S99 (≠ E115), A118 (= A134), F119 (≠ H135), L124 (≠ V140), P126 (= P142), N127 (≠ G143), A212 (≠ L228), G222 (≠ L238)
- 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 (≠ M25), A59 (= A63), Q61 (≠ A65), D62 (= D66), L63 (= L67), L68 (= L84), Y71 (≠ A87), A94 (≠ M110), G95 (≠ A111), A96 (≠ G112), F119 (≠ H135), I122 (≠ F138), L124 (≠ V140), N127 (≠ G143), F234 (= F250), K237 (= K253)
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, 94% coverage: 14:259/261 of query aligns to 47:288/290 of P14604
- E144 (= E115) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ H135) 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)
40% identity, 94% coverage: 17:261/261 of query aligns to 16:257/257 of 6slbAAA
- active site: Q64 (≠ A65), F69 (≠ V70), L80 (= L84), N84 (= N88), A108 (≠ G112), S111 (≠ E115), A130 (= A134), F131 (≠ H135), L136 (≠ V140), P138 (= P142), D139 (≠ G143), A224 (≠ L228), G234 (≠ L238)
- 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 (≠ P59), A62 (= A63), Q64 (≠ A65), D65 (= D66), L66 (= L67), Y76 (≠ G79), A108 (≠ G112), F131 (≠ H135), D139 (≠ G143)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
35% identity, 94% coverage: 14:259/261 of query aligns to 16:252/254 of 2dubA
- active site: A67 (= A65), M72 (≠ V70), S82 (≠ N88), G105 (= G112), E108 (= E115), P127 (≠ A134), E128 (≠ H135), T133 (≠ V140), P135 (= P142), G136 (= G143), K221 (≠ L228), F231 (≠ L238)
- binding octanoyl-coenzyme a: K25 (= K23), A26 (= A24), L27 (≠ M25), A29 (≠ S27), A65 (= A63), A67 (= A65), D68 (= D66), I69 (≠ L67), K70 (= K68), G105 (= G112), E108 (= E115), P127 (≠ A134), E128 (≠ H135), G136 (= G143), A137 (= A144)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
35% identity, 98% coverage: 7:261/261 of query aligns to 11:266/266 of O53561
- K135 (≠ T130) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 130:137, 13% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ N137) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
35% identity, 94% coverage: 14:259/261 of query aligns to 17:256/258 of 1mj3A
- active site: A68 (= A65), M73 (≠ V70), S83 (≠ N88), L85 (≠ V90), G109 (= G112), E112 (= E115), P131 (≠ A134), E132 (≠ H135), T137 (≠ V140), P139 (= P142), G140 (= G143), K225 (≠ L228), F235 (≠ L238)
- binding hexanoyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (≠ M25), A30 (≠ S27), A66 (= A63), G67 (= G64), A68 (= A65), D69 (= D66), I70 (≠ L67), G109 (= G112), P131 (≠ A134), E132 (≠ H135), L135 (≠ F138), G140 (= G143)
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
35% identity, 91% coverage: 5:242/261 of query aligns to 2:222/224 of 3p85A
- active site: L62 (≠ A65), L67 (≠ V70), P68 (≠ N88), G92 (= G112), E95 (= E115), T114 (≠ A134), H115 (= H135), L120 (≠ V140), P122 (= P142), T123 (≠ G143), W208 (≠ L228), T219 (≠ R239)
- binding calcium ion: D43 (≠ N46), D45 (≠ E48)
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)
35% identity, 93% coverage: 17:260/261 of query aligns to 92:338/339 of Q13825
- K105 (≠ L30) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 30:44, 7% identical) RNA-binding
- K109 (≠ A34) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ Q38) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G166) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
31% identity, 94% coverage: 14:258/261 of query aligns to 31:261/268 of 4elxA
- active site: G83 (≠ A65), H88 (≠ V70), L92 (= L84), G116 (= G112), V119 (≠ E115), G139 (≠ H135), S144 (≠ V140), D146 (≠ P142), G147 (= G143), A233 (≠ L228), Y241 (≠ L238)
- binding chloride ion: G115 (≠ A111), G139 (≠ H135), W167 (≠ L163)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
31% identity, 94% coverage: 14:258/261 of query aligns to 31:260/267 of 4elwA
- active site: G83 (≠ A65), L91 (= L84), G115 (= G112), V118 (≠ E115), G138 (≠ H135), S143 (≠ V140), D145 (≠ P142), G146 (= G143), A232 (≠ L228), Y240 (≠ L238)
- binding nitrate ion: G114 (≠ A111), T137 (≠ A134), G138 (≠ H135), F144 (≠ Y141), W166 (≠ L163)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
31% identity, 94% coverage: 14:258/261 of query aligns to 30:274/281 of 3t88A
- active site: G82 (≠ A65), R87 (≠ K68), Y93 (≠ A74), H101 (≠ E80), L105 (= L84), G129 (= G112), V132 (≠ E115), G152 (≠ H135), S157 (≠ V140), D159 (≠ P142), G160 (= G143), A246 (≠ L228), Y254 (≠ L238)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ K23), V40 (≠ A24), R41 (≠ M25), A43 (≠ S27), S80 (≠ A63), G81 (= G64), G82 (≠ A65), D83 (= D66), Q84 (vs. gap), K85 (vs. gap), Y93 (≠ A74), V104 (≠ F83), L105 (= L84), Y125 (≠ V108), G129 (= G112), T151 (≠ A134), V155 (≠ F138), F158 (≠ Y141), D159 (≠ P142), T250 (≠ V232), Y254 (≠ L238), F266 (= F250), K269 (= K253)
Query Sequence
>WP_011911840.1 NCBI__GCF_000013785.1:WP_011911840.1
MSEAVLLFETLGPVARLTLNRPKAMNSLNLAMLAELEQRLAEIAANDELRTVILTGAGPA
FCAGADLKEVLAGASLAAGEADFLDRANQVFGQLRNLPKPVIAALNGVTMAGGLELAMCA
DIVVAADSATIADAHANFGVYPGAGGAAILPRLIPLNMAMYLLLTGKSLSASEMKACGLV
CEVHADAELAEAALSLAKQIAKKSPIALRRMKEVARASADKTRDDALLHEQVMLRQHLRS
ADLQEGLHAFNEKRAPQFKGR
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