SitesBLAST
Comparing WP_004314659.1 NCBI__GCF_000310185.1:WP_004314659.1 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)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
37% identity, 97% coverage: 10:260/260 of query aligns to 10:256/256 of 3h81A
- active site: A64 (≠ G65), M69 (≠ F70), T79 (≠ H84), F83 (≠ V88), G107 (= G113), E110 (= E116), P129 (= P135), E130 (≠ I136), V135 (≠ M143), P137 (= P145), G138 (= G146), L223 (≠ A224), F233 (≠ L237)
- binding calcium ion: F233 (≠ L237), Q238 (≠ Y242)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
37% identity, 95% coverage: 10:257/260 of query aligns to 11:254/255 of 3q0jC
- active site: A65 (≠ G65), M70 (≠ F70), T80 (≠ H84), F84 (≠ V88), G108 (= G113), E111 (= E116), P130 (= P135), E131 (≠ I136), V136 (≠ M143), P138 (= P145), G139 (= G146), L224 (≠ A224), F234 (≠ L237)
- binding acetoacetyl-coenzyme a: Q23 (≠ T22), A24 (≠ K23), L25 (= L24), A27 (= A26), A63 (= A63), G64 (= G64), A65 (≠ G65), D66 (= D66), I67 (= I67), K68 (≠ E68), M70 (≠ F70), F84 (≠ V88), G107 (= G112), G108 (= G113), E111 (= E116), P130 (= P135), E131 (≠ I136), P138 (= P145), G139 (= G146), M140 (= M148)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 95% coverage: 10:257/260 of query aligns to 11:254/255 of 3q0gC
- active site: A65 (≠ G65), M70 (≠ F70), T80 (≠ H84), F84 (≠ V88), G108 (= G113), E111 (= E116), P130 (= P135), E131 (≠ I136), V136 (≠ M143), P138 (= P145), G139 (= G146), L224 (≠ A224), F234 (≠ L237)
- binding coenzyme a: L25 (= L24), A63 (= A63), I67 (= I67), K68 (≠ E68), Y104 (≠ A109), P130 (= P135), E131 (≠ I136), L134 (= L139)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 94% coverage: 16:260/260 of query aligns to 17:259/259 of 5zaiC
- active site: A65 (≠ G65), F70 (= F70), S82 (≠ H84), R86 (≠ A89), G110 (= G113), E113 (= E116), P132 (= P135), E133 (≠ I136), I138 (≠ M143), P140 (= P145), G141 (= G146), A226 (= A224), F236 (= F234)
- binding coenzyme a: K24 (= K23), L25 (= L24), A63 (= A63), G64 (= G64), A65 (≠ G65), D66 (= D66), I67 (= I67), P132 (= P135), R166 (≠ I169), F248 (= F249), K251 (= K252)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 95% coverage: 10:257/260 of query aligns to 10:249/250 of 3q0gD
- active site: A64 (≠ G65), M69 (≠ F70), T75 (≠ H84), F79 (≠ V88), G103 (= G113), E106 (= E116), P125 (= P135), E126 (≠ I136), V131 (≠ M143), P133 (= P145), G134 (= G146), L219 (≠ A224), F229 (≠ L237)
- binding Butyryl Coenzyme A: F225 (≠ A233), F241 (= F249)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
35% identity, 94% coverage: 17:260/260 of query aligns to 19:261/261 of 5jbxB
- active site: A67 (≠ G65), R72 (= R74), L84 (≠ E85), R88 (≠ A89), G112 (= G113), E115 (= E116), T134 (≠ P135), E135 (≠ I136), I140 (≠ F141), P142 (≠ M143), G143 (≠ Y144), A228 (vs. gap), L238 (= L237)
- binding coenzyme a: S24 (≠ T22), R25 (≠ K23), R26 (≠ L24), A28 (= A26), A65 (= A63), D68 (= D66), L69 (≠ I67), K70 (≠ E68), L110 (≠ V111), G111 (= G112), T134 (≠ P135), E135 (≠ I136), L138 (= L139), R168 (≠ I169)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 96% coverage: 10:258/260 of query aligns to 13:252/254 of 2dubA
- active site: A67 (≠ G65), M72 (≠ F70), S82 (≠ L81), G105 (= G113), E108 (= E116), P127 (= P135), E128 (≠ I136), T133 (≠ F141), P135 (≠ M143), G136 (≠ Y144), K221 (≠ A224), F231 (≠ L237)
- binding octanoyl-coenzyme a: K25 (≠ T22), A26 (≠ K23), L27 (= L24), A29 (= A26), A65 (= A63), A67 (≠ G65), D68 (= D66), I69 (= I67), K70 (≠ E68), G105 (= G113), E108 (= E116), P127 (= P135), E128 (≠ I136), G136 (≠ Y144), A137 (≠ P145)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
33% identity, 96% coverage: 10:258/260 of query aligns to 14:258/260 of 1dubA
- active site: A68 (≠ G65), M73 (≠ F70), S83 (≠ E85), L87 (≠ A89), G111 (= G113), E114 (= E116), P133 (= P135), E134 (≠ I136), T139 (≠ F141), P141 (≠ M143), G142 (≠ Y144), K227 (≠ A224), F237 (≠ L237)
- binding acetoacetyl-coenzyme a: K26 (≠ T22), A27 (≠ K23), L28 (= L24), A30 (= A26), A66 (= A63), A68 (≠ G65), D69 (= D66), I70 (= I67), Y107 (≠ A109), G110 (= G112), G111 (= G113), E114 (= E116), P133 (= P135), E134 (≠ I136), L137 (= L139), G142 (≠ Y144), F233 (≠ A233), F249 (= F249)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
33% identity, 96% coverage: 10:258/260 of query aligns to 12:256/258 of 1ey3A
- active site: A66 (≠ G65), M71 (≠ F70), S81 (≠ E85), L85 (≠ A89), G109 (= G113), E112 (= E116), P131 (= P135), E132 (≠ I136), T137 (≠ F141), P139 (≠ M143), G140 (≠ Y144), K225 (≠ A224), F235 (≠ L237)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ T22), L26 (= L24), A28 (= A26), A64 (= A63), G65 (= G64), A66 (≠ G65), D67 (= D66), I68 (= I67), L85 (≠ A89), W88 (≠ L92), G109 (= G113), P131 (= P135), L135 (= L139), G140 (≠ Y144)
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)
33% identity, 96% coverage: 10:258/260 of query aligns to 44:288/290 of P14604
- E144 (= E116) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ I136) 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
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
32% identity, 96% coverage: 10:258/260 of query aligns to 14:256/258 of 1mj3A
- active site: A68 (≠ G65), M73 (≠ F70), S83 (≠ D78), L85 (≠ A80), G109 (= G113), E112 (= E116), P131 (= P135), E132 (≠ I136), T137 (≠ F141), P139 (≠ M143), G140 (≠ Y144), K225 (≠ A224), F235 (≠ L237)
- binding hexanoyl-coenzyme a: K26 (≠ T22), A27 (≠ K23), L28 (= L24), A30 (= A26), A66 (= A63), G67 (= G64), A68 (≠ G65), D69 (= D66), I70 (= I67), G109 (= G113), P131 (= P135), E132 (≠ I136), L135 (= L139), G140 (≠ Y144)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
30% identity, 97% coverage: 10:260/260 of query aligns to 14:260/260 of 2hw5C
- active site: A68 (≠ G65), M73 (≠ F70), S83 (≠ A89), L87 (vs. gap), G111 (= G113), E114 (= E116), P133 (= P135), E134 (≠ I136), T139 (≠ F141), P141 (≠ M143), G142 (≠ Y144), K227 (≠ A224), F237 (≠ L237)
- binding crotonyl coenzyme a: K26 (≠ T22), A27 (≠ K23), L28 (= L24), A30 (= A26), K62 (≠ N59), I70 (= I67), F109 (≠ V111)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 96% coverage: 12:260/260 of query aligns to 12:257/257 of 6slbAAA
- active site: Q64 (≠ G65), F69 (= F70), L80 (= L81), N84 (≠ E85), A108 (≠ G113), S111 (≠ E116), A130 (≠ P135), F131 (≠ I136), L136 (≠ F141), P138 (≠ M143), D139 (≠ Y144), A224 (= A224), G234 (≠ F234)
- 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 (≠ N59), A62 (= A63), Q64 (≠ G65), D65 (= D66), L66 (≠ I67), Y76 (≠ V77), A108 (≠ G113), F131 (≠ I136), D139 (≠ Y144)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 94% coverage: 16:260/260 of query aligns to 21:266/266 of O53561
- K135 (≠ R131) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 131:140, 30% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ G140) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 96% coverage: 12:260/260 of query aligns to 9:245/245 of 6slaAAA
- active site: Q61 (≠ G65), L68 (≠ S72), N72 (≠ H84), A96 (≠ G113), S99 (≠ E116), A118 (≠ P135), F119 (≠ I136), L124 (≠ F141), P126 (≠ M143), N127 (≠ Y144), A212 (= A224), G222 (≠ F234)
- 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 (= L24), A59 (= A63), Q61 (≠ G65), D62 (= D66), L63 (≠ I67), L68 (≠ S72), Y71 (= Y83), A94 (≠ V111), G95 (= G112), A96 (≠ G113), F119 (≠ I136), I122 (≠ L139), L124 (≠ F141), N127 (≠ Y144), F234 (= F249), K237 (= K252)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
33% identity, 76% coverage: 16:213/260 of query aligns to 69:275/327 of Q62651
- D176 (≠ E116) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (≠ I136) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ Y144) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
Q5LLW6 Methylthioacryloyl-CoA hydratase; EC 4.2.1.155 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
32% identity, 79% coverage: 3:208/260 of query aligns to 10:212/267 of Q5LLW6
- K31 (= K23) binding 3-(methylsulfanyl)acryloyl-CoA
- R32 (≠ L24) binding 3-(methylsulfanyl)acryloyl-CoA
- A69 (= A63) binding 3-(methylsulfanyl)acryloyl-CoA
- L71 (≠ G65) binding 3-(methylsulfanyl)acryloyl-CoA
- L73 (≠ I67) binding 3-(methylsulfanyl)acryloyl-CoA
- G118 (= G113) binding 3-(methylsulfanyl)acryloyl-CoA
- E121 (= E116) active site, Nucleophile; mutation to A: Abolishes catalytic activity.
- E141 (≠ I136) active site, Proton acceptor; mutation to A: Abolishes catalytic activity.
- R144 (≠ L139) binding 3-(methylsulfanyl)acryloyl-CoA
- G149 (≠ Y144) binding 3-(methylsulfanyl)acryloyl-CoA
3t3wF Crystal structure of probable enoyl-coa hydratase from mycobacterium thermoresistibile (see paper)
32% identity, 82% coverage: 5:218/260 of query aligns to 6:214/248 of 3t3wF
- active site: H65 (≠ G65), D71 (≠ R74), S83 (≠ D86), L87 (≠ V88), G111 (= G113), L114 (≠ E116), V134 (≠ I136), I139 (≠ F141), G140 (≠ S142), E143 (= E147)
- binding zinc ion: E82 (= E85), E143 (= E147)
Sites not aligning to the query:
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
32% identity, 95% coverage: 12:257/260 of query aligns to 33:278/285 of Q7CQ56
3omeC Crystal structure of a probable enoyl-coa hydratase from mycobacterium smegmatis (see paper)
31% identity, 82% coverage: 5:218/260 of query aligns to 6:213/247 of 3omeC
- active site: H65 (≠ G65), E70 (≠ V73), A82 (≠ E85), L86 (≠ A89), G110 (= G113), L113 (≠ E116), V133 (≠ I136), I138 (≠ F141), G139 (≠ S142), E142 (= E147)
- binding zinc ion: E81 (≠ H84), E142 (= E147)
Sites not aligning to the query:
Query Sequence
>WP_004314659.1 NCBI__GCF_000310185.1:WP_004314659.1
MNTRIDLDIDQGIATVTLHNPTKLNAVNAAMWRGLSAAMARIAADDSVRCVIVRGAGENA
FAAGGDIEEFRSVRATVDDALHYHEDLVASALNAIRDCAVPTVAAIRGACVGGGLEIAGC
CDIRIAGESARFGAPINRLGFSMYPGEMAGLLALVGPAVVLEILLEGRILDAREALQKGL
LTRVVDDERVFEEAAVSAERIRAGAPLVARWHKQWVRRLTTGVALDEEEKRRAFDFLATA
DYREGLAAFSEKRAPVFRGR
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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