SitesBLAST
Comparing WP_011384541.1 NCBI__GCF_000009985.1:WP_011384541.1 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)
28% identity, 92% coverage: 15:252/259 of query aligns to 10:252/259 of 5zaiC
- active site: A65 (= A69), F70 (≠ H74), S82 (≠ L83), R86 (≠ H87), G110 (= G111), E113 (= E114), P132 (= P133), E133 (= E134), I138 (≠ V139), P140 (≠ A141), G141 (≠ P142), A226 (= A225), F236 (≠ M236)
- binding coenzyme a: K24 (= K28), L25 (≠ A29), A63 (≠ F67), G64 (= G68), A65 (= A69), D66 (≠ S70), I67 (≠ V71), P132 (= P133), R166 (≠ S166), F248 (= F248), K251 (= K251)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 92% coverage: 14:252/259 of query aligns to 8:245/250 of 3q0gD
- active site: A64 (= A69), M69 (≠ H74), T75 (≠ A80), F79 (≠ L83), G103 (= G111), E106 (= E114), P125 (= P133), E126 (= E134), V131 (= V139), P133 (vs. gap), G134 (≠ A141), L219 (vs. gap), F229 (≠ M236)
- binding Butyryl Coenzyme A: F225 (≠ L232), F241 (= F248)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
30% identity, 95% coverage: 14:259/259 of query aligns to 8:256/256 of 3h81A
- active site: A64 (= A69), M69 (= M75), T79 (vs. gap), F83 (≠ L83), G107 (= G111), E110 (= E114), P129 (= P133), E130 (= E134), V135 (= V139), P137 (vs. gap), G138 (≠ A141), L223 (vs. gap), F233 (≠ M236)
- binding calcium ion: F233 (≠ M236), Q238 (≠ A241)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
30% identity, 94% coverage: 10:252/259 of query aligns to 5:250/255 of 3q0jC
- active site: A65 (= A69), M70 (= M75), T80 (vs. gap), F84 (≠ L83), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), V136 (= V139), P138 (vs. gap), G139 (≠ A141), L224 (vs. gap), F234 (≠ M236)
- binding acetoacetyl-coenzyme a: Q23 (≠ K28), A24 (= A29), L25 (vs. gap), A27 (≠ I31), A63 (≠ F67), G64 (= G68), A65 (= A69), D66 (≠ S70), I67 (≠ V71), K68 (≠ A72), M70 (= M75), F84 (≠ L83), G107 (= G110), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), P138 (vs. gap), G139 (≠ A141), M140 (≠ P142)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 94% coverage: 10:252/259 of query aligns to 5:250/255 of 3q0gC
- active site: A65 (= A69), M70 (= M75), T80 (vs. gap), F84 (≠ L83), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), V136 (= V139), P138 (vs. gap), G139 (≠ A141), L224 (vs. gap), F234 (≠ M236)
- binding coenzyme a: L25 (vs. gap), A63 (≠ F67), I67 (≠ V71), K68 (≠ A72), Y104 (≠ Q107), P130 (= P133), E131 (= E134), L134 (= L137)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
30% identity, 98% coverage: 7:259/259 of query aligns to 1:257/257 of 6slbAAA
- active site: Q64 (≠ A69), F69 (vs. gap), L80 (= L83), N84 (≠ H87), A108 (≠ G111), S111 (≠ E114), A130 (≠ P133), F131 (≠ E134), L136 (≠ V139), P138 (≠ A141), D139 (≠ P142), A224 (≠ K221), G234 (≠ M236)
- 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 (≠ P63), A62 (≠ F67), Q64 (≠ A69), D65 (≠ S70), L66 (≠ V71), Y76 (≠ C79), A108 (≠ G111), F131 (≠ E134), D139 (≠ P142)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
29% identity, 96% coverage: 11:259/259 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A69), L68 (= L83), N72 (≠ H87), A96 (≠ G111), S99 (≠ E114), A118 (≠ P133), F119 (≠ E134), L124 (≠ V139), P126 (≠ A141), N127 (≠ P142), A212 (≠ K221), G222 (≠ M236)
- 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 (≠ A29), A59 (≠ F67), Q61 (≠ A69), D62 (≠ S70), L63 (≠ V71), L68 (= L83), Y71 (≠ L86), A94 (≠ L109), G95 (= G110), A96 (≠ G111), F119 (≠ E134), I122 (≠ L137), L124 (≠ V139), N127 (≠ P142), F234 (= F248), K237 (= K251)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
28% identity, 90% coverage: 28:259/259 of query aligns to 25:261/261 of 5jbxB
- active site: A67 (= A69), R72 (≠ H74), L84 (= L83), R88 (≠ H87), G112 (= G111), E115 (= E114), T134 (≠ P133), E135 (= E134), I140 (≠ V139), P142 (≠ A141), G143 (≠ P142), A228 (= A229), L238 (≠ M236)
- binding coenzyme a: R25 (≠ K28), R26 (≠ A29), A28 (≠ I31), A65 (≠ F67), D68 (≠ S70), L69 (≠ V71), K70 (≠ A72), L110 (= L109), G111 (= G110), T134 (≠ P133), E135 (= E134), L138 (= L137), R168 (≠ S166)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
27% identity, 92% coverage: 22:258/259 of query aligns to 20:257/258 of 1mj3A
- active site: A68 (= A69), M73 (≠ H74), S83 (≠ A81), L85 (= L83), G109 (= G111), E112 (= E114), P131 (= P133), E132 (= E134), T137 (≠ V139), P139 (≠ A141), G140 (≠ P142), K225 (vs. gap), F235 (≠ M236)
- binding hexanoyl-coenzyme a: K26 (= K28), A27 (= A29), L28 (vs. gap), A30 (≠ I31), A66 (≠ F67), G67 (= G68), A68 (= A69), D69 (≠ S70), I70 (≠ V71), G109 (= G111), P131 (= P133), E132 (= E134), L135 (= L137), G140 (≠ P142)
Q08426 Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens (Human) (see 5 papers)
31% identity, 66% coverage: 22:192/259 of query aligns to 14:184/723 of Q08426
- V40 (≠ H48) to G: in dbSNP:rs1062551
- I41 (≠ E49) to R: in dbSNP:rs1062552
- T75 (≠ S85) to I: in dbSNP:rs1062553
- K165 (≠ R174) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.
- K171 (≠ A180) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.
Sites not aligning to the query:
- 3 E → K: in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells; dbSNP:rs398124646
- 274 A → T: in dbSNP:rs2302819
- 325 A → G: in dbSNP:rs1062555
- 346 modified: N6-acetyllysine; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
- 584 modified: N6-acetyllysine; alternate; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
- 598 K → T: in dbSNP:rs1042437
- 606 T → P: in dbSNP:rs1042438
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)
28% identity, 59% coverage: 30:182/259 of query aligns to 29:188/729 of P21177
- G116 (= G111) 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)
28% identity, 59% coverage: 30:182/259 of query aligns to 29:188/719 of 6tnmA
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
26% identity, 92% coverage: 22:258/259 of query aligns to 19:253/254 of 2dubA
- active site: A67 (= A69), M72 (≠ H74), S82 (≠ A81), G105 (= G111), E108 (= E114), P127 (= P133), E128 (= E134), T133 (≠ V139), P135 (≠ A141), G136 (≠ P142), K221 (vs. gap), F231 (≠ M236)
- binding octanoyl-coenzyme a: K25 (= K28), A26 (= A29), L27 (vs. gap), A29 (≠ I31), A65 (≠ F67), A67 (= A69), D68 (≠ S70), I69 (≠ V71), K70 (≠ A72), G105 (= G111), E108 (= E114), P127 (= P133), E128 (= E134), G136 (≠ P142), A137 (= A143)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
27% identity, 92% coverage: 22:258/259 of query aligns to 20:259/260 of 1dubA
- active site: A68 (= A69), M73 (≠ H74), S83 (≠ A81), L87 (≠ S85), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), T139 (≠ V139), P141 (≠ A141), G142 (≠ P142), K227 (vs. gap), F237 (≠ M236)
- binding acetoacetyl-coenzyme a: K26 (= K28), A27 (= A29), L28 (vs. gap), A30 (≠ I31), A66 (≠ F67), A68 (= A69), D69 (≠ S70), I70 (≠ V71), Y107 (≠ Q107), G110 (= G110), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), L137 (= L137), G142 (≠ P142), F233 (≠ L232), F249 (= F248)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
27% identity, 92% coverage: 22:258/259 of query aligns to 18:257/258 of 1ey3A
- active site: A66 (= A69), M71 (≠ H74), S81 (≠ A81), L85 (≠ S85), G109 (= G111), E112 (= E114), P131 (= P133), E132 (= E134), T137 (≠ V139), P139 (≠ A141), G140 (≠ P142), K225 (vs. gap), F235 (≠ M236)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K28), L26 (vs. gap), A28 (≠ I31), A64 (≠ F67), G65 (= G68), A66 (= A69), D67 (≠ S70), I68 (≠ V71), L85 (≠ S85), W88 (≠ K88), G109 (= G111), P131 (= P133), L135 (= L137), G140 (≠ P142)
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)
27% identity, 92% coverage: 22:258/259 of query aligns to 50:289/290 of P14604
- E144 (= E114) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E134) 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
Q5LLW6 Methylthioacryloyl-CoA hydratase; EC 4.2.1.155 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
28% identity, 93% coverage: 15:254/259 of query aligns to 17:261/267 of Q5LLW6
- K31 (= K28) binding
- R32 (≠ A29) binding
- A69 (≠ F67) binding
- L71 (≠ A69) binding
- L73 (≠ V71) binding
- G118 (= G111) binding
- E121 (= E114) active site, Nucleophile; mutation to A: Abolishes catalytic activity.
- E141 (= E134) active site, Proton acceptor; mutation to A: Abolishes catalytic activity.
- R144 (≠ L137) binding
- G149 (≠ P142) binding
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
25% identity, 92% coverage: 22:259/259 of query aligns to 20:260/260 of 2hw5C
- active site: A68 (= A69), M73 (≠ H74), S83 (≠ A81), L87 (≠ H87), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), T139 (≠ V139), P141 (≠ A141), G142 (≠ P142), K227 (vs. gap), F237 (≠ M236)
- binding crotonyl coenzyme a: K26 (= K28), A27 (= A29), L28 (vs. gap), A30 (≠ I31), K62 (≠ P63), I70 (≠ V71), F109 (≠ L109)
3omeC Crystal structure of a probable enoyl-coa hydratase from mycobacterium smegmatis (see paper)
26% identity, 81% coverage: 22:231/259 of query aligns to 17:228/247 of 3omeC
- active site: H65 (≠ A69), E70 (≠ D77), A82 (vs. gap), L86 (vs. gap), G110 (= G111), L113 (≠ E114), V133 (≠ E134), I138 (≠ V139), G139 (≠ F140), E142 (≠ A143), Q225 (≠ E228)
- binding zinc ion: E81 (≠ K88), E142 (≠ A143)
Sites not aligning to the query:
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
26% identity, 93% coverage: 11:251/259 of query aligns to 4:247/247 of 7borA
- active site: N63 (≠ A69), F68 (≠ H74), D77 (≠ L83), G81 (≠ H87), I105 (≠ G111), T108 (≠ E114), F128 (≠ E134), L133 (≠ V139), P135 (≠ A141), E136 (≠ P142), A222 (= A225), L232 (≠ M236)
- binding coenzyme a: D21 (vs. gap), K22 (= K28), A25 (≠ I31), S61 (≠ F67), I65 (≠ V71), V103 (≠ L109), F128 (≠ E134), L131 (= L137), F244 (= F248), R247 (≠ K251)
Query Sequence
>WP_011384541.1 NCBI__GCF_000009985.1:WP_011384541.1
MAEGISNCLKVWKDREGKLLRLRLSRPKANIVDAEMIAALSAALGDAHEDSALRAVLIDH
EGPHFSFGASVAEHMPDQCAAMLASLHKLVIAMVDFPLPILVAVRGQCLGGGLEVALAGH
MMFVSPDAKLGQPEIVLGVFAPAASCLLPERMPRVAAEDLLYSGRSIDGAEAARLGIANA
VVDDPENAALAWFDNGPAKHSAASLRFAVKAARLGMNERVKAKIAEVEALYLNGLMATHD
AVEGLNAFLEKRPALWEDR
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