SitesBLAST
Comparing WP_011881868.1 NCBI__GCF_000016205.1:WP_011881868.1 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)
45% identity, 99% coverage: 4:261/261 of query aligns to 3:259/259 of 5zaiC
- active site: A65 (= A67), F70 (≠ I72), S82 (≠ A84), R86 (≠ H88), G110 (= G112), E113 (= E115), P132 (= P134), E133 (= E135), I138 (= I140), P140 (= P142), G141 (= G143), A226 (≠ S228), F236 (≠ A238)
- binding coenzyme a: K24 (≠ S25), L25 (= L26), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (= I69), P132 (= P134), R166 (≠ L168), F248 (= F250), K251 (= K253)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
47% identity, 99% coverage: 3:261/261 of query aligns to 1:256/256 of 3h81A
- active site: A64 (= A67), M69 (≠ I72), T79 (≠ A84), F83 (≠ H88), G107 (= G112), E110 (= E115), P129 (= P134), E130 (= E135), V135 (≠ I140), P137 (= P142), G138 (= G143), L223 (≠ S228), F233 (≠ A238)
- binding calcium ion: F233 (≠ A238), Q238 (≠ K243)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
48% identity, 98% coverage: 3:258/261 of query aligns to 2:254/255 of 3q0jC
- active site: A65 (= A67), M70 (≠ I72), T80 (≠ A84), F84 (≠ H88), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), V136 (≠ I140), P138 (= P142), G139 (= G143), L224 (≠ S228), F234 (≠ A238)
- binding acetoacetyl-coenzyme a: Q23 (≠ K24), A24 (≠ S25), L25 (= L26), A27 (= A28), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (= I69), K68 (≠ S70), M70 (≠ I72), F84 (≠ H88), G107 (= G111), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), P138 (= P142), G139 (= G143), M140 (≠ F144)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
48% identity, 98% coverage: 3:258/261 of query aligns to 2:254/255 of 3q0gC
- active site: A65 (= A67), M70 (≠ I72), T80 (≠ A84), F84 (≠ H88), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), V136 (≠ I140), P138 (= P142), G139 (= G143), L224 (≠ S228), F234 (≠ A238)
- binding coenzyme a: L25 (= L26), A63 (= A65), I67 (= I69), K68 (≠ S70), Y104 (≠ F108), P130 (= P134), E131 (= E135), L134 (= L138)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
48% identity, 98% coverage: 3:258/261 of query aligns to 1:249/250 of 3q0gD
- active site: A64 (= A67), M69 (≠ I72), T75 (≠ A79), F79 (= F83), G103 (= G112), E106 (= E115), P125 (= P134), E126 (= E135), V131 (≠ I140), P133 (= P142), G134 (= G143), L219 (≠ S228), F229 (≠ A238)
- binding Butyryl Coenzyme A: F225 (= F234), F241 (= F250)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
44% identity, 99% coverage: 2:259/261 of query aligns to 1:256/258 of 1mj3A
- active site: A68 (= A67), M73 (≠ I72), S83 (≠ A84), L85 (= L86), G109 (= G112), E112 (= E115), P131 (= P134), E132 (= E135), T137 (≠ I140), P139 (= P142), G140 (= G143), K225 (≠ S228), F235 (≠ A238)
- binding hexanoyl-coenzyme a: K26 (= K24), A27 (≠ S25), L28 (= L26), A30 (= A28), A66 (= A65), G67 (= G66), A68 (= A67), D69 (= D68), I70 (= I69), G109 (= G112), P131 (= P134), E132 (= E135), L135 (= L138), G140 (= G143)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
44% identity, 99% coverage: 2:259/261 of query aligns to 1:258/260 of 1dubA
- active site: A68 (= A67), M73 (≠ I72), S83 (≠ A84), L87 (≠ H88), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), T139 (≠ I140), P141 (= P142), G142 (= G143), K227 (≠ S228), F237 (≠ A238)
- binding acetoacetyl-coenzyme a: K26 (= K24), A27 (≠ S25), L28 (= L26), A30 (= A28), A66 (= A65), A68 (= A67), D69 (= D68), I70 (= I69), Y107 (≠ F108), G110 (= G111), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), L137 (= L138), G142 (= G143), F233 (= F234), F249 (= F250)
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)
44% identity, 99% coverage: 2:259/261 of query aligns to 31:288/290 of P14604
- E144 (= E115) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E135) 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
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
44% identity, 98% coverage: 4:259/261 of query aligns to 1:256/258 of 1ey3A
- active site: A66 (= A67), M71 (≠ I72), S81 (≠ A84), L85 (≠ H88), G109 (= G112), E112 (= E115), P131 (= P134), E132 (= E135), T137 (≠ I140), P139 (= P142), G140 (= G143), K225 (≠ S228), F235 (≠ A238)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K24), L26 (= L26), A28 (= A28), A64 (= A65), G65 (= G66), A66 (= A67), D67 (= D68), I68 (= I69), L85 (≠ H88), W88 (≠ M91), G109 (= G112), P131 (= P134), L135 (= L138), G140 (= G143)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
44% identity, 99% coverage: 3:260/261 of query aligns to 1:253/254 of 2dubA
- active site: A67 (= A67), M72 (≠ I72), S82 (= S89), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), T133 (≠ I140), P135 (= P142), G136 (= G143), K221 (≠ S228), F231 (≠ A238)
- binding octanoyl-coenzyme a: K25 (= K24), A26 (≠ S25), L27 (= L26), A29 (= A28), A65 (= A65), A67 (= A67), D68 (= D68), I69 (= I69), K70 (≠ S70), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), G136 (= G143), A137 (≠ F144)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
41% identity, 100% coverage: 2:261/261 of query aligns to 1:260/260 of 2hw5C
- active site: A68 (= A67), M73 (≠ I72), S83 (≠ K82), L87 (= L86), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), T139 (≠ I140), P141 (= P142), G142 (= G143), K227 (≠ S228), F237 (≠ A238)
- binding crotonyl coenzyme a: K26 (= K24), A27 (≠ S25), L28 (= L26), A30 (= A28), K62 (= K61), I70 (= I69), F109 (≠ L110)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
40% identity, 99% coverage: 3:261/261 of query aligns to 3:261/261 of 5jbxB
- active site: A67 (= A67), R72 (≠ I72), L84 (≠ A84), R88 (≠ H88), G112 (= G112), E115 (= E115), T134 (≠ P134), E135 (= E135), I140 (= I140), P142 (= P142), G143 (= G143), A228 (≠ S228), L238 (≠ A238)
- binding coenzyme a: S24 (≠ K24), R25 (≠ S25), R26 (≠ L26), A28 (= A28), A65 (= A65), D68 (= D68), L69 (≠ I69), K70 (≠ S70), L110 (= L110), G111 (= G111), T134 (≠ P134), E135 (= E135), L138 (= L138), R168 (≠ L168)
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, 96% coverage: 10:259/261 of query aligns to 84:337/339 of Q13825
- K105 (≠ F31) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 31:45, 7% identical) RNA-binding
- K109 (≠ T35) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ A39) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (= A166) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
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)
37% identity, 94% coverage: 15:259/261 of query aligns to 21:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
Q8GYN9 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; DHNS; Enoyl-CoA hydratase/isomerase D; ECHID; Naphthoate synthase; EC 4.1.3.36 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 98% coverage: 4:258/261 of query aligns to 74:330/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
P21177 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Escherichia coli (strain K12) (see 2 papers)
40% identity, 72% coverage: 12:199/261 of query aligns to 14:203/729 of P21177
- G116 (= G112) mutation to F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected.
Sites not aligning to the query:
- 322 G→A: 10-fold increase in KM for NADH.
- 450 active site, For 3-hydroxyacyl-CoA dehydrogenase activity; mutation H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
40% identity, 72% coverage: 12:199/261 of query aligns to 14:203/719 of 6tnmA