SitesBLAST
Comparing WP_011952858.1 NCBI__GCF_000016765.1:WP_011952858.1 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)
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)
41% identity, 87% coverage: 14:273/299 of query aligns to 24:269/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
36% identity, 91% coverage: 3:275/299 of query aligns to 2:259/259 of 5zaiC
- active site: A65 (= A67), F70 (≠ R81), S82 (≠ R96), R86 (≠ G100), G110 (≠ A124), E113 (≠ T127), P132 (= P146), E133 (≠ F147), I138 (= I152), P140 (= P154), G141 (≠ E155), A226 (≠ L247), F236 (vs. gap)
- binding coenzyme a: K24 (≠ R25), L25 (≠ M26), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (= I69), P132 (= P146), R166 (≠ L180), F248 (= F264), K251 (= K267)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 88% coverage: 14:275/299 of query aligns to 12:257/257 of 6slbAAA
- active site: Q64 (≠ A67), F69 (≠ Y78), L80 (≠ A89), N84 (≠ G100), A108 (= A124), S111 (≠ T127), A130 (≠ P146), F131 (= F147), L136 (≠ I152), P138 (= P154), D139 (≠ E155), A224 (≠ R242), G234 (= G252)
- 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 (= R61), A62 (= A65), Q64 (≠ A67), D65 (= D68), L66 (≠ I69), Y76 (≠ V85), A108 (= A124), F131 (= F147), D139 (≠ E155)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 88% coverage: 14:275/299 of query aligns to 9:245/245 of 6slaAAA
- active site: Q61 (≠ A67), L68 (≠ S79), N72 (≠ G100), A96 (= A124), S99 (≠ T127), A118 (≠ P146), F119 (= F147), L124 (≠ I152), P126 (= P154), N127 (≠ E155), A212 (≠ R242), G222 (= G252)
- 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 (≠ M26), A59 (= A65), Q61 (≠ A67), D62 (= D68), L63 (≠ I69), L68 (≠ S79), Y71 (≠ D82), A94 (≠ V122), G95 (= G123), A96 (= A124), F119 (= F147), I122 (≠ R150), L124 (≠ I152), N127 (≠ E155), F234 (= F264), K237 (= K267)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 91% coverage: 4:275/299 of query aligns to 2:256/256 of 3h81A
- active site: A64 (= A67), M69 (≠ G72), T79 (≠ R91), F83 (≠ Y95), G107 (≠ A124), E110 (≠ T127), P129 (= P146), E130 (≠ F147), V135 (≠ I152), P137 (= P154), G138 (≠ E155), L223 (≠ R242), F233 (≠ G252)
- binding calcium ion: F233 (≠ G252), Q238 (≠ A257)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 90% coverage: 4:272/299 of query aligns to 3:254/255 of 3q0jC
- active site: A65 (= A67), M70 (≠ G72), T80 (≠ R91), F84 (≠ Y95), G108 (≠ A124), E111 (≠ T127), P130 (= P146), E131 (≠ F147), V136 (≠ I152), P138 (= P154), G139 (≠ E155), L224 (≠ R242), F234 (≠ G252)
- binding acetoacetyl-coenzyme a: Q23 (≠ E24), A24 (≠ R25), L25 (≠ M26), A27 (≠ T28), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (= I69), K68 (≠ S70), M70 (≠ G72), F84 (≠ Y95), G107 (= G123), G108 (≠ A124), E111 (≠ T127), P130 (= P146), E131 (≠ F147), P138 (= P154), G139 (≠ E155), M140 (≠ S156)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 90% coverage: 4:272/299 of query aligns to 3:254/255 of 3q0gC
- active site: A65 (= A67), M70 (≠ G72), T80 (≠ R91), F84 (≠ Y95), G108 (≠ A124), E111 (≠ T127), P130 (= P146), E131 (≠ F147), V136 (≠ I152), P138 (= P154), G139 (≠ E155), L224 (≠ R242), F234 (≠ G252)
- binding coenzyme a: L25 (≠ M26), A63 (= A65), I67 (= I69), K68 (≠ S70), Y104 (≠ A120), P130 (= P146), E131 (≠ F147), L134 (≠ R150)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 90% coverage: 4:272/299 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (= A67), M69 (≠ T75), T75 (≠ R91), F79 (≠ Y95), G103 (≠ A124), E106 (≠ T127), P125 (= P146), E126 (≠ F147), V131 (≠ I152), P133 (= P154), G134 (≠ E155), L219 (≠ R242), F229 (≠ G252)
- binding Butyryl Coenzyme A: F225 (≠ V248), F241 (= F264)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 88% coverage: 12:273/299 of query aligns to 14:256/258 of 1mj3A
- active site: A68 (= A67), M73 (≠ T75), S83 (≠ R91), L85 (≠ G93), G109 (≠ A124), E112 (≠ T127), P131 (= P146), E132 (≠ F147), T137 (≠ I152), P139 (= P154), G140 (≠ E155), K225 (≠ R242), F235 (≠ G252)
- binding hexanoyl-coenzyme a: K26 (≠ E24), A27 (≠ R25), L28 (≠ M26), A30 (≠ T28), A66 (= A65), G67 (= G66), A68 (= A67), D69 (= D68), I70 (= I69), G109 (≠ A124), P131 (= P146), E132 (≠ F147), L135 (≠ R150), G140 (≠ E155)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 88% coverage: 12:273/299 of query aligns to 13:252/254 of 2dubA
- active site: A67 (= A67), M72 (≠ G72), S82 (= S79), G105 (≠ A124), E108 (≠ T127), P127 (= P146), E128 (≠ F147), T133 (≠ I152), P135 (= P154), G136 (≠ E155), K221 (≠ R242), F231 (≠ G252)
- binding octanoyl-coenzyme a: K25 (≠ E24), A26 (≠ R25), L27 (≠ M26), A29 (≠ T28), A65 (= A65), A67 (= A67), D68 (= D68), I69 (= I69), K70 (≠ S70), G105 (≠ A124), E108 (≠ T127), P127 (= P146), E128 (≠ F147), G136 (≠ E155), A137 (≠ S156)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 88% coverage: 12:273/299 of query aligns to 12:256/258 of 1ey3A
- active site: A66 (= A67), M71 (≠ T75), S81 (≠ A89), L85 (≠ G93), G109 (≠ A124), E112 (≠ T127), P131 (= P146), E132 (≠ F147), T137 (≠ I152), P139 (= P154), G140 (≠ E155), K225 (≠ R242), F235 (≠ G252)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E24), L26 (≠ M26), A28 (≠ T28), A64 (= A65), G65 (= G66), A66 (= A67), D67 (= D68), I68 (= I69), L85 (≠ G93), W88 (≠ R96), G109 (≠ A124), P131 (= P146), L135 (≠ R150), G140 (≠ E155)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
31% identity, 88% coverage: 12:273/299 of query aligns to 14:258/260 of 1dubA
- active site: A68 (= A67), M73 (≠ T75), S83 (≠ A89), L87 (≠ G93), G111 (≠ A124), E114 (≠ T127), P133 (= P146), E134 (≠ F147), T139 (≠ I152), P141 (= P154), G142 (≠ E155), K227 (≠ R242), F237 (≠ G252)
- binding acetoacetyl-coenzyme a: K26 (≠ E24), A27 (≠ R25), L28 (≠ M26), A30 (≠ T28), A66 (= A65), A68 (= A67), D69 (= D68), I70 (= I69), Y107 (≠ A120), G110 (= G123), G111 (≠ A124), E114 (≠ T127), P133 (= P146), E134 (≠ F147), L137 (≠ R150), G142 (≠ E155), F233 (≠ V248), F249 (= F264)
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)
31% identity, 88% coverage: 12:273/299 of query aligns to 44:288/290 of P14604
- E144 (≠ T127) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F147) 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
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
35% identity, 89% coverage: 9:275/299 of query aligns to 7:261/261 of 5jbxB
- active site: A67 (= A67), R72 (≠ A83), L84 (≠ R96), R88 (≠ G100), G112 (≠ A124), E115 (≠ T127), T134 (≠ P146), E135 (≠ F147), I140 (= I152), P142 (= P154), G143 (≠ E155), A228 (≠ R242), L238 (≠ G252)
- binding coenzyme a: S24 (≠ E24), R25 (= R25), R26 (≠ M26), A28 (≠ T28), A65 (= A65), D68 (= D68), L69 (≠ I69), K70 (≠ R81), L110 (≠ V122), G111 (= G123), T134 (≠ P146), E135 (≠ F147), L138 (≠ R150), R168 (≠ L180)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 86% coverage: 18:275/299 of query aligns to 21:266/266 of O53561
- K135 (≠ R142) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 142:149, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ R149) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
38% identity, 71% coverage: 5:215/299 of query aligns to 1:183/224 of 3p85A
- active site: L62 (≠ A67), L67 (≠ T75), P68 (≠ F76), G92 (≠ A124), E95 (≠ T127), T114 (≠ P146), H115 (≠ F147), L120 (≠ I152), P122 (= P154), T123 (≠ E155)
- binding calcium ion: D43 (= D47), D45 (= D49)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
30% identity, 88% coverage: 12:273/299 of query aligns to 14:258/260 of 2hw5C
- active site: A68 (= A67), M73 (≠ T75), S83 (≠ R96), L87 (≠ G100), G111 (≠ A124), E114 (≠ T127), P133 (= P146), E134 (≠ F147), T139 (≠ I152), P141 (= P154), G142 (≠ E155), K227 (≠ R242), F237 (≠ G252)
- binding crotonyl coenzyme a: K26 (≠ E24), A27 (≠ R25), L28 (≠ M26), A30 (≠ T28), K62 (≠ R61), I70 (= I69), F109 (≠ V122)
5dufA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk729a (see paper)
32% identity, 87% coverage: 15:274/299 of query aligns to 12:244/245 of 5dufA
- active site: A62 (= A67), D67 (≠ G72), P74 (≠ S79), I78 (≠ L104), A102 (= A124), Q105 (≠ T127), P124 (= P146), T125 (≠ F147), L130 (≠ I152), L132 (≠ P154), D133 (≠ E155), P212 (vs. gap), W222 (≠ G252)
- binding (5R,7S)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxylic acid: L77 (≠ A103), I78 (≠ L104), H81 (≠ F107), D85 (≠ K111), Q105 (≠ T127), D133 (≠ E155), W135 (≠ A157)
5ducA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk951a (see paper)
32% identity, 87% coverage: 15:274/299 of query aligns to 11:243/244 of 5ducA
- active site: A61 (= A67), D66 (≠ G72), P73 (≠ S79), I77 (≠ L104), A101 (= A124), Q104 (≠ T127), P123 (= P146), T124 (≠ F147), L129 (≠ I152), L131 (≠ P154), D132 (≠ E155), P211 (vs. gap), W221 (≠ G252)
- binding (5R,7S)-N-(1,3-benzodioxol-5-ylmethyl)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (≠ A103), H80 (≠ F107), D84 (≠ K111), Q104 (≠ T127), D132 (≠ E155), W134 (≠ A157), F217 (≠ V248)
5du4A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk366a (see paper)
32% identity, 87% coverage: 15:274/299 of query aligns to 11:243/244 of 5du4A
- active site: A61 (= A67), D66 (≠ G72), P73 (≠ S79), I77 (≠ L104), A101 (= A124), Q104 (≠ T127), P123 (= P146), T124 (≠ F147), L129 (≠ I152), L131 (≠ P154), D132 (≠ E155), P211 (vs. gap), W221 (≠ G252)
- binding (5R,7S)-5-(4-ethylphenyl)-N-(4-methoxybenzyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (≠ A103), I77 (≠ L104), H80 (≠ F107), D84 (≠ K111), Q104 (≠ T127), D132 (≠ E155), W134 (≠ A157)
Query Sequence
>WP_011952858.1 NCBI__GCF_000016765.1:WP_011952858.1
MSDFETIRFDVDRGIATITLARPERMNTMNATMTLELIRALDTADADDDVRVVIVTGEGG
RAFCAGADISGGAETFDYSRRDAAVRAEAERGGTYRDSGGRVALRIFNALKPVIGAINGA
AVGAGATISLAMDVRLAAEPARFGFPFVRRGIVPESASSWFLPRIVGISTALEWTLSGRL
VGAAEAKERGLVRSVHAPDELLPAARALAAEIVENAAPVSVALTRQMMWRMLGSDHPMDA
HRLDSRLVQALGSSADAREGVGAFLEKRPARFEGRVSADMPPAFPWWTEPEFQDQKSER
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