SitesBLAST
Comparing WP_058929110.1 NCBI__GCF_001484605.1:WP_058929110.1 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, 95% coverage: 15:258/258 of query aligns to 17:259/259 of 5zaiC
- active site: A65 (= A64), F70 (≠ L69), S82 (≠ Q83), R86 (vs. gap), G110 (= G109), E113 (≠ T112), P132 (≠ S131), E133 (= E132), I138 (≠ V137), P140 (= P139), G141 (= G140), A226 (≠ R225), F236 (≠ Q235)
- binding coenzyme a: K24 (≠ R22), L25 (≠ M23), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), P132 (≠ S131), R166 (≠ P165), F248 (= F247), K251 (≠ R250)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
38% identity, 95% coverage: 15:258/258 of query aligns to 21:266/266 of O53561
- K135 (≠ T127) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 127:134, 63% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K134) 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)
37% identity, 96% coverage: 9:255/258 of query aligns to 14:255/258 of 1mj3A
- active site: A68 (= A64), M73 (≠ L69), S83 (vs. gap), L85 (= L81), G109 (= G109), E112 (≠ T112), P131 (≠ S131), E132 (= E132), T137 (≠ V137), P139 (= P139), G140 (= G140), K225 (≠ R225), F235 (≠ Q235)
- binding hexanoyl-coenzyme a: K26 (≠ E21), A27 (≠ R22), L28 (≠ M23), A30 (= A25), A66 (= A62), G67 (= G63), A68 (= A64), D69 (= D65), I70 (≠ L66), G109 (= G109), P131 (≠ S131), E132 (= E132), L135 (≠ R135), G140 (= G140)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
36% identity, 96% coverage: 9:255/258 of query aligns to 12:255/258 of 1ey3A
- active site: A66 (= A64), M71 (≠ L69), S81 (≠ L81), L85 (≠ D85), G109 (= G109), E112 (≠ T112), P131 (≠ S131), E132 (= E132), T137 (≠ V137), P139 (= P139), G140 (= G140), K225 (≠ R225), F235 (≠ Q235)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E21), L26 (≠ M23), A28 (= A25), A64 (= A62), G65 (= G63), A66 (= A64), D67 (= D65), I68 (≠ L66), L85 (≠ D85), W88 (≠ L88), G109 (= G109), P131 (≠ S131), L135 (≠ R135), G140 (= G140)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
36% identity, 96% coverage: 9:255/258 of query aligns to 14:257/260 of 1dubA
- active site: A68 (= A64), M73 (≠ L69), S83 (≠ L81), L87 (≠ D85), G111 (= G109), E114 (≠ T112), P133 (≠ S131), E134 (= E132), T139 (≠ V137), P141 (= P139), G142 (= G140), K227 (≠ R225), F237 (≠ Q235)
- binding acetoacetyl-coenzyme a: K26 (≠ E21), A27 (≠ R22), L28 (≠ M23), A30 (= A25), A66 (= A62), A68 (= A64), D69 (= D65), I70 (≠ L66), Y107 (= Y105), G110 (= G108), G111 (= G109), E114 (≠ T112), P133 (≠ S131), E134 (= E132), L137 (≠ R135), G142 (= G140), F233 (≠ Q231), F249 (= F247)
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)
36% identity, 96% coverage: 9:255/258 of query aligns to 44:287/290 of P14604
- E144 (≠ T112) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E132) 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)
36% identity, 96% coverage: 9:255/258 of query aligns to 13:251/254 of 2dubA
- active site: A67 (= A64), M72 (≠ L69), S82 (≠ T82), G105 (= G109), E108 (≠ T112), P127 (≠ S131), E128 (= E132), T133 (≠ V137), P135 (= P139), G136 (= G140), K221 (≠ R225), F231 (≠ Q235)
- binding octanoyl-coenzyme a: K25 (≠ E21), A26 (≠ R22), L27 (≠ M23), A29 (= A25), A65 (= A62), A67 (= A64), D68 (= D65), I69 (≠ L66), K70 (= K67), G105 (= G109), E108 (≠ T112), P127 (≠ S131), E128 (= E132), G136 (= G140), A137 (≠ N141)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
38% identity, 92% coverage: 22:258/258 of query aligns to 25:261/261 of 5jbxB
- active site: A67 (= A64), R72 (≠ L69), L84 (= L81), R88 (≠ D85), G112 (= G109), E115 (≠ T112), T134 (≠ S131), E135 (= E132), I140 (≠ V137), P142 (= P139), G143 (= G140), A228 (≠ R225), L238 (= L234)
- binding coenzyme a: R25 (= R22), R26 (≠ M23), A28 (= A25), A65 (= A62), D68 (= D65), L69 (= L66), K70 (= K67), L110 (= L107), G111 (= G108), T134 (≠ S131), E135 (= E132), L138 (≠ R135), R168 (≠ P165)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
34% identity, 96% coverage: 9:255/258 of query aligns to 14:257/260 of 2hw5C
- active site: A68 (= A64), M73 (≠ L69), S83 (≠ L81), L87 (≠ D85), G111 (= G109), E114 (≠ T112), P133 (≠ S131), E134 (= E132), T139 (≠ V137), P141 (= P139), G142 (= G140), K227 (≠ R225), F237 (≠ Q235)
- binding crotonyl coenzyme a: K26 (≠ E21), A27 (≠ R22), L28 (≠ M23), A30 (= A25), K62 (= K58), I70 (≠ L66), F109 (≠ L107)
O69762 Hydroxycinnamoyl-CoA hydratase-lyase; HCHL; P-hydroxycinnamoyl CoA hydratase/lyase; Trans-feruloyl-CoA hydratase/vanillin synthase; EC 4.1.2.61 from Pseudomonas fluorescens (see 2 papers)
36% identity, 93% coverage: 9:247/258 of query aligns to 16:261/276 of O69762
- K29 (≠ R22) binding acetyl-CoA
- A68 (= A62) binding acetyl-CoA
- M70 (≠ A64) binding acetyl-CoA
- L72 (= L66) binding acetyl-CoA
- Y75 (≠ L69) binding vanillin
- G120 (= G109) binding acetyl-CoA
- S123 (≠ T112) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (= S131) binding acetyl-CoA
- E143 (= E132) mutation to A: Abolishes catalytic activity.
- W146 (≠ R135) binding acetyl-CoA
- G151 (= G140) binding vanillin
- Y239 (vs. gap) binding vanillin; mutation to F: Increased KM for feruloyl-CoA but retains a significant amount of catalytic activity with a kcat 10 times less than that of the wild-type.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
38% identity, 81% coverage: 9:218/258 of query aligns to 14:227/246 of 2vssD
- active site: M68 (≠ A64), Y73 (≠ L69), D78 (≠ P71), R90 (≠ T82), Q94 (= Q86), G118 (= G109), S121 (≠ T112), S140 (= S131), E141 (= E132), I146 (≠ V137), P148 (= P139), G149 (= G140)
- binding acetyl coenzyme *a: E26 (= E21), K27 (≠ R22), R28 (≠ M23), A30 (= A25), A66 (= A62), M68 (≠ A64), D69 (= D65), L70 (= L66), F74 (vs. gap), W114 (≠ Y105), F116 (≠ L107), S140 (= S131)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ A64), Y73 (≠ L69), F74 (vs. gap), Q96 (≠ L88), E141 (= E132), G149 (= G140), N150 (= N141)
Sites not aligning to the query:
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
38% identity, 81% coverage: 9:218/258 of query aligns to 13:226/247 of 2vssB
- active site: M67 (≠ A64), Y72 (≠ L69), D77 (≠ P71), R89 (≠ T82), Q93 (= Q86), G117 (= G109), S120 (≠ T112), S139 (= S131), E140 (= E132), I145 (≠ V137), P147 (= P139), G148 (= G140)
- binding acetyl coenzyme *a: E25 (= E21), K26 (≠ R22), R27 (≠ M23), A29 (= A25), A65 (= A62), M67 (≠ A64), D68 (= D65), W113 (≠ Y105), F115 (≠ L107), G117 (= G109), S139 (= S131), E140 (= E132)
Sites not aligning to the query:
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)
36% identity, 93% coverage: 12:251/258 of query aligns to 21:261/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 97% coverage: 9:258/258 of query aligns to 10:257/257 of 6slbAAA
- active site: Q64 (≠ A64), F69 (≠ L69), L80 (= L81), N84 (≠ D85), A108 (≠ G109), S111 (≠ T112), A130 (≠ S131), F131 (≠ E132), L136 (≠ V137), P138 (= P139), D139 (≠ G140), A224 (≠ R225), G234 (≠ Q235)
- 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 (≠ K58), A62 (= A62), Q64 (≠ A64), D65 (= D65), L66 (= L66), Y76 (≠ H77), A108 (≠ G109), F131 (≠ E132), D139 (≠ G140)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 97% coverage: 9:258/258 of query aligns to 10:256/256 of 3h81A
- active site: A64 (= A64), M69 (vs. gap), T79 (≠ L76), F83 (≠ W80), G107 (= G109), E110 (≠ T112), P129 (≠ S131), E130 (= E132), V135 (= V137), P137 (= P139), G138 (= G140), L223 (≠ R225), F233 (≠ Q235)
- binding calcium ion: F233 (≠ Q235), Q238 (≠ A240)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 96% coverage: 9:255/258 of query aligns to 11:254/255 of 3q0jC
- active site: A65 (= A64), M70 (vs. gap), T80 (≠ L76), F84 (≠ W80), G108 (= G109), E111 (≠ T112), P130 (≠ S131), E131 (= E132), V136 (= V137), P138 (= P139), G139 (= G140), L224 (≠ R225), F234 (≠ Q235)
- binding acetoacetyl-coenzyme a: Q23 (≠ E21), A24 (≠ R22), L25 (≠ M23), A27 (= A25), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), K68 (= K67), M70 (vs. gap), F84 (≠ W80), G107 (= G108), G108 (= G109), E111 (≠ T112), P130 (≠ S131), E131 (= E132), P138 (= P139), G139 (= G140), M140 (≠ N141)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 96% coverage: 9:255/258 of query aligns to 11:254/255 of 3q0gC