SitesBLAST
Comparing WP_011779227.1 NCBI__GCF_000015305.1:WP_011779227.1 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)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
39% identity, 91% coverage: 18:286/294 of query aligns to 4:254/257 of 6slbAAA
- active site: Q64 (≠ A78), F69 (≠ L83), L80 (= L104), N84 (≠ D108), A108 (≠ I139), S111 (≠ T142), A130 (= A161), F131 (= F162), L136 (= L167), P138 (≠ A169), D139 (≠ E170), A224 (= A256), G234 (≠ M266)
- 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 (= R72), A62 (= A76), Q64 (≠ A78), D65 (= D79), L66 (≠ M80), Y76 (≠ G100), A108 (≠ I139), F131 (= F162), D139 (≠ E170)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 91% coverage: 18:286/294 of query aligns to 1:242/245 of 6slaAAA
- active site: Q61 (≠ A78), L68 (≠ Q111), N72 (≠ E115), A96 (≠ I139), S99 (≠ T142), A118 (= A161), F119 (= F162), L124 (= L167), P126 (≠ A169), N127 (≠ E170), A212 (= A256), G222 (≠ M266)
- 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 (≠ M38), A59 (= A76), Q61 (≠ A78), D62 (= D79), L63 (≠ M80), L68 (≠ Q111), Y71 (≠ G114), A94 (= A137), G95 (= G138), A96 (≠ I139), F119 (= F162), I122 (≠ R165), L124 (= L167), N127 (≠ E170), F234 (= F278), K237 (= K281)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
33% identity, 87% coverage: 30:286/294 of query aligns to 17:256/259 of 5zaiC
- active site: A65 (= A78), F70 (≠ L83), S82 (≠ G95), R86 (≠ E115), G110 (≠ I139), E113 (≠ T142), P132 (≠ A161), E133 (≠ F162), I138 (≠ L167), P140 (≠ A169), G141 (≠ E170), A226 (= A256), F236 (≠ M266)
- binding coenzyme a: K24 (≠ R37), L25 (≠ M38), A63 (= A76), G64 (= G77), A65 (= A78), D66 (= D79), I67 (≠ M80), P132 (≠ A161), R166 (≠ T195), F248 (= F278), K251 (= K281)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 90% coverage: 23:286/294 of query aligns to 13:257/260 of 2hw5C
- active site: A68 (= A78), M73 (≠ L83), S83 (≠ V109), L87 (≠ V113), G111 (≠ I139), E114 (≠ T142), P133 (≠ A161), E134 (≠ F162), T139 (≠ L167), P141 (≠ A169), G142 (≠ E170), K227 (≠ A256), F237 (≠ M266)
- binding crotonyl coenzyme a: K26 (≠ E36), A27 (≠ R37), L28 (≠ M38), A30 (≠ S40), K62 (≠ R72), I70 (≠ M80), F109 (≠ A137)
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)
32% identity, 89% coverage: 26:286/294 of query aligns to 24:268/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 90% coverage: 23:287/294 of query aligns to 13:256/258 of 1mj3A
- active site: A68 (= A78), M73 (≠ L83), S83 (= S102), L85 (= L104), G109 (≠ I139), E112 (≠ T142), P131 (≠ A161), E132 (≠ F162), T137 (≠ L167), P139 (≠ A169), G140 (≠ E170), K225 (≠ A256), F235 (≠ M266)
- binding hexanoyl-coenzyme a: K26 (≠ E36), A27 (≠ R37), L28 (≠ M38), A30 (≠ S40), A66 (= A76), G67 (= G77), A68 (= A78), D69 (= D79), I70 (≠ M80), G109 (≠ I139), P131 (≠ A161), E132 (≠ F162), L135 (≠ R165), G140 (≠ E170)
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)
32% identity, 90% coverage: 27:290/294 of query aligns to 21:269/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 92% coverage: 16:286/294 of query aligns to 3:253/256 of 3h81A
- active site: A64 (= A78), M69 (≠ L83), T79 (≠ V109), F83 (≠ V113), G107 (≠ I139), E110 (≠ T142), P129 (≠ A161), E130 (≠ F162), V135 (≠ L167), P137 (≠ A169), G138 (≠ E170), L223 (≠ A256), F233 (≠ M266)
- binding calcium ion: F233 (≠ M266), Q238 (≠ F271)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 92% coverage: 16:286/294 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (= A78), M70 (≠ L83), T80 (≠ V109), F84 (≠ V113), G108 (≠ I139), E111 (≠ T142), P130 (≠ A161), E131 (≠ F162), V136 (≠ L167), P138 (≠ A169), G139 (≠ E170), L224 (≠ A256), F234 (≠ M266)
- binding acetoacetyl-coenzyme a: Q23 (≠ E36), A24 (≠ R37), L25 (≠ M38), A27 (≠ S40), A63 (= A76), G64 (= G77), A65 (= A78), D66 (= D79), I67 (≠ M80), K68 (≠ G81), M70 (≠ L83), F84 (≠ V113), G107 (= G138), G108 (≠ I139), E111 (≠ T142), P130 (≠ A161), E131 (≠ F162), P138 (≠ A169), G139 (≠ E170), M140 (≠ Y171)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 92% coverage: 16:286/294 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (= A78), M70 (≠ L83), T80 (≠ V109), F84 (≠ V113), G108 (≠ I139), E111 (≠ T142), P130 (≠ A161), E131 (≠ F162), V136 (≠ L167), P138 (≠ A169), G139 (≠ E170), L224 (≠ A256), F234 (≠ M266)
- binding coenzyme a: L25 (≠ M38), A63 (= A76), I67 (≠ M80), K68 (≠ G81), Y104 (≠ A135), P130 (≠ A161), E131 (≠ F162), L134 (≠ R165)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
29% identity, 90% coverage: 23:287/294 of query aligns to 13:258/260 of 1dubA
- active site: A68 (= A78), M73 (≠ L83), S83 (≠ V109), L87 (≠ V113), G111 (≠ I139), E114 (≠ T142), P133 (≠ A161), E134 (≠ F162), T139 (≠ L167), P141 (≠ A169), G142 (≠ E170), K227 (≠ A256), F237 (≠ M266)
- binding acetoacetyl-coenzyme a: K26 (≠ E36), A27 (≠ R37), L28 (≠ M38), A30 (≠ S40), A66 (= A76), A68 (= A78), D69 (= D79), I70 (≠ M80), Y107 (≠ A135), G110 (= G138), G111 (≠ I139), E114 (≠ T142), P133 (≠ A161), E134 (≠ F162), L137 (≠ R165), G142 (≠ E170), F233 (≠ M262), F249 (= F278)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
29% identity, 90% coverage: 23:287/294 of query aligns to 11:256/258 of 1ey3A
- active site: A66 (= A78), M71 (≠ L83), S81 (≠ V109), L85 (≠ V113), G109 (≠ I139), E112 (≠ T142), P131 (≠ A161), E132 (≠ F162), T137 (≠ L167), P139 (≠ A169), G140 (≠ E170), K225 (≠ A256), F235 (≠ M266)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E36), L26 (≠ M38), A28 (≠ S40), A64 (= A76), G65 (= G77), A66 (= A78), D67 (= D79), I68 (≠ M80), L85 (≠ V113), W88 (≠ P118), G109 (≠ I139), P131 (≠ A161), L135 (≠ R165), G140 (≠ E170)
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)
30% identity, 90% coverage: 23:286/294 of query aligns to 43:287/290 of P14604
- E144 (≠ T142) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F162) 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
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 92% coverage: 16:286/294 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (= A78), M69 (≠ L83), T75 (≠ S87), F79 (≠ S110), G103 (≠ I139), E106 (≠ T142), P125 (≠ A161), E126 (≠ F162), V131 (≠ L167), P133 (≠ A169), G134 (≠ E170), L219 (≠ A256), F229 (≠ M266)
- binding Butyryl Coenzyme A: F225 (≠ M262), F241 (= F278)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
30% identity, 90% coverage: 23:287/294 of query aligns to 12:252/254 of 2dubA
- active site: A67 (= A78), M72 (≠ L83), S82 (= S102), G105 (≠ I139), E108 (≠ T142), P127 (≠ A161), E128 (≠ F162), T133 (≠ L167), P135 (≠ A169), G136 (≠ E170), K221 (≠ A256), F231 (≠ M266)
- binding octanoyl-coenzyme a: K25 (≠ E36), A26 (≠ R37), L27 (≠ M38), A29 (≠ S40), A65 (= A76), A67 (= A78), D68 (= D79), I69 (≠ M80), K70 (≠ G81), G105 (≠ I139), E108 (≠ T142), P127 (≠ A161), E128 (≠ F162), G136 (≠ E170), A137 (≠ Y171)
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)
31% identity, 89% coverage: 24:286/294 of query aligns to 84:330/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
28% identity, 91% coverage: 24:290/294 of query aligns to 10:264/269 of 1jxzB
- active site: C61 (= C75), F64 (≠ A78), I69 (≠ L83), A86 (≠ Q111), Q90 (≠ E115), G113 (= G138), G114 (≠ I139), G117 (≠ T142), A136 (= A161), W137 (≠ F162), I142 (≠ L167), N144 (≠ A169), D145 (≠ E170), E230 (≠ A256)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E36), H23 (≠ R37), R24 (≠ M38), A62 (= A76), F64 (≠ A78), Y65 (≠ D79), L66 (≠ M80), R67 (≠ G81), W89 (≠ G114), G113 (= G138), A136 (= A161), W137 (≠ F162), I142 (≠ L167), D145 (≠ E170), T146 (≠ Y171), F252 (= F278), R257 (≠ Q283)
- binding calcium ion: G49 (≠ R63), L202 (≠ M227), A203 (= A228), A205 (= A232), T207 (≠ S234), Q210 (≠ A237)
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
28% identity, 91% coverage: 24:290/294 of query aligns to 10:264/269 of 1nzyB
- active site: C61 (= C75), F64 (≠ A78), I69 (≠ L83), A86 (≠ Q111), H90 (≠ E115), G114 (≠ I139), G117 (≠ T142), A136 (= A161), W137 (≠ F162), I142 (≠ L167), N144 (≠ A169), D145 (≠ E170), E230 (≠ A256)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E36), H23 (≠ R37), R24 (≠ M38), A62 (= A76), F64 (≠ A78), Y65 (≠ D79), L66 (≠ M80), R67 (≠ G81), W89 (≠ G114), G113 (= G138), G114 (≠ I139), A136 (= A161), W137 (≠ F162), D145 (≠ E170), T146 (≠ Y171), F252 (= F278), R257 (≠ Q283)
- binding calcium ion: G49 (≠ R63), L202 (≠ M227), A203 (= A228), A205 (= A232), T207 (≠ S234), Q210 (≠ A237)
- binding phosphate ion: E57 (≠ G71), N108 (= N133), K188 (≠ P213), R192 (≠ M217)
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
30% identity, 88% coverage: 24:281/294 of query aligns to 9:247/247 of 7borA
- active site: N63 (≠ A78), F68 (≠ L83), D77 (= D106), G81 (≠ S110), I105 (= I139), T108 (= T142), F128 (= F162), L133 (= L167), P135 (≠ A169), E136 (= E170), A222 (= A256), L232 (≠ M266)
- binding coenzyme a: D21 (≠ E36), K22 (≠ R37), A25 (≠ S40), S61 (≠ A76), I65 (≠ M80), V103 (≠ A137), F128 (= F162), L131 (≠ R165), F244 (= F278), R247 (≠ K281)
A5JTM5 4-chlorobenzoyl coenzyme A dehalogenase; 4-CBA-CoA dehalogenase; 4-CBCoA dehalogenase; 4-chlorobenzoyl-CoA dehalogenase; EC 3.8.1.7 from Pseudomonas sp. (strain CBS-3) (see 7 papers)
28% identity, 91% coverage: 24:290/294 of query aligns to 10:264/269 of A5JTM5
- R24 (≠ M38) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ A48) mutation to T: Forms inclusion bodies.
- E43 (= E57) mutation to A: No effect on catalytic activity.
- D45 (= D59) mutation to A: No effect on catalytic activity.
- D46 (≠ P60) mutation to A: No effect on catalytic activity.
- G63 (= G77) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ A78) mutation to A: 30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.; mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to P: Severely reduces catalytic activity. Arylated intermediate does not accumulate.
- Y65 (≠ D79) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ G81) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ D82) mutation to T: No effect on catalytic activity.
- H81 (≠ T107) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (vs. gap) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ G114) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ E115) active site, Proton acceptor; mutation to Q: Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation.
- H94 (= H119) mutation to Q: No effect on catalytic activity.
- A112 (= A137) mutation to G: Yields insoluble protein.; mutation to S: Protein precipitates upon purification.; mutation to V: Catalytic activity is almost as efficient as wild type.
- G113 (= G138) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.; mutation G->N,S: Strongly reduced catalytic activity. Arylated intermediate does not accumulate.; mutation to V: Protein precipitates upon purification.
- G114 (≠ I139) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G140) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D148) mutation to T: No effect on catalytic activity.
- D129 (≠ A154) mutation to T: No effect on catalytic activity.
- W137 (≠ F162) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (≠ E170) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ D188) mutation to T: No effect on catalytic activity.
- E175 (= E200) mutation to D: No effect on catalytic activity.
- W179 (≠ L204) mutation to F: No effect on catalytic activity.
- H208 (≠ S235) mutation to Q: No effect on catalytic activity.
- R216 (≠ Q242) mutation R->E,K,L: Yields insoluble protein.
- E232 (≠ A258) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.
- R257 (≠ Q283) mutation to K: Retains catalytic activity and substrate CoA binding.; mutation to L: Significantly reduces catalytic activity and substrate CoA binding.
Query Sequence
>WP_011779227.1 NCBI__GCF_000015305.1:WP_011779227.1
MSAVDRAAEPGIADTEPVLFDMHDSGVAVLTLNRPERMNSWGGGLAQAFYRCIDRAEADP
HVRVIVLTGNGRAFCAGADMGDLDSISAAGDTGRGERSDGESGLADTDVSQLVGERHPHF
LTQLRKPLIAAINGACAGIGLTHALMCDVRFAAAGAKFTTAFARRGLIAEYGISWILPRI
VGWSAAQDLLLSGRTFYAEEANELGLVNQVVAPDELMAHTLAYAEDMARNCAPSSLAVIK
RQIYRDALRNLSDASADAEKLMHESMQRPDFIEGITAFFEKRQPSFPPLKEETP
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