SitesBLAST
Comparing WP_084517379.1 NCBI__GCF_000422285.1:WP_084517379.1 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)
37% identity, 97% coverage: 8:262/264 of query aligns to 5:255/257 of 6slbAAA
- active site: Q64 (≠ G67), F69 (≠ I72), L80 (≠ F83), N84 (≠ H91), A108 (≠ G115), S111 (= S118), A130 (= A137), F131 (≠ Y138), L136 (= L143), P138 (≠ L145), D139 (= D146), A224 (≠ E231), G234 (= G241)
- 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 (≠ K61), A62 (= A65), Q64 (≠ G67), D65 (= D68), L66 (= L69), Y76 (= Y79), A108 (≠ G115), F131 (≠ Y138), D139 (= D146)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 97% coverage: 8:262/264 of query aligns to 2:243/245 of 6slaAAA
- active site: Q61 (≠ G67), L68 (≠ N76), N72 (≠ G80), A96 (≠ G115), S99 (= S118), A118 (= A137), F119 (≠ Y138), L124 (= L143), P126 (≠ L145), N127 (≠ D146), A212 (≠ E231), G222 (= G241)
- 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 (≠ Y27), A59 (= A65), Q61 (≠ G67), D62 (= D68), L63 (= L69), L68 (≠ N76), Y71 (= Y79), A94 (= A113), G95 (= G114), A96 (≠ G115), F119 (≠ Y138), I122 (≠ N141), L124 (= L143), N127 (≠ D146), F234 (= F253), K237 (= K256)
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)
33% identity, 94% coverage: 14:262/264 of query aligns to 23:269/296 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)
32% identity, 92% coverage: 19:262/264 of query aligns to 17:257/259 of 5zaiC
- active site: A65 (≠ G67), F70 (≠ Y75), S82 (≠ A87), R86 (≠ H91), G110 (= G115), E113 (≠ S118), P132 (≠ A137), E133 (≠ Y138), I138 (≠ L143), P140 (≠ L145), G141 (≠ D146), A226 (≠ E231), F236 (≠ G241)
- binding coenzyme a: K24 (≠ A26), L25 (≠ Y27), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (= I72), P132 (≠ A137), R166 (≠ P171), F248 (= F253), K251 (= K256)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 96% coverage: 8:261/264 of query aligns to 6:254/255 of 3q0jC
- active site: A65 (≠ G67), M70 (≠ I72), T80 (≠ H84), F84 (≠ H91), G108 (= G115), E111 (≠ S118), P130 (≠ A137), E131 (≠ Y138), V136 (≠ L143), P138 (≠ L145), G139 (≠ D146), L224 (≠ E231), F234 (≠ G241)
- binding acetoacetyl-coenzyme a: Q23 (≠ K25), A24 (= A26), L25 (≠ Y27), A27 (= A29), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (≠ L69), K68 (≠ R70), M70 (≠ I72), F84 (≠ H91), G107 (= G114), G108 (= G115), E111 (≠ S118), P130 (≠ A137), E131 (≠ Y138), P138 (≠ L145), G139 (≠ D146), M140 (≠ G147)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 96% coverage: 8:261/264 of query aligns to 6:254/255 of 3q0gC
- active site: A65 (≠ G67), M70 (≠ I72), T80 (≠ H84), F84 (≠ H91), G108 (= G115), E111 (≠ S118), P130 (≠ A137), E131 (≠ Y138), V136 (≠ L143), P138 (≠ L145), G139 (≠ D146), L224 (≠ E231), F234 (≠ G241)
- binding coenzyme a: L25 (≠ Y27), A63 (= A65), I67 (≠ L69), K68 (≠ R70), Y104 (≠ L111), P130 (≠ A137), E131 (≠ Y138), L134 (≠ N141)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 96% coverage: 8:261/264 of query aligns to 5:253/256 of 3h81A
- active site: A64 (≠ G67), M69 (≠ I72), T79 (≠ A87), F83 (≠ H91), G107 (= G115), E110 (≠ S118), P129 (≠ A137), E130 (≠ Y138), V135 (≠ L143), P137 (≠ L145), G138 (≠ D146), L223 (≠ E231), F233 (≠ G241)
- binding calcium ion: F233 (≠ G241), Q238 (≠ G246)
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
30% identity, 92% coverage: 12:255/264 of query aligns to 9:254/269 of 1nzyB
- active site: C61 (= C64), F64 (≠ G67), I69 (= I72), A86 (= A87), H90 (= H91), G114 (= G115), G117 (≠ S118), A136 (= A137), W137 (≠ Y138), I142 (≠ L143), N144 (≠ L145), D145 (= D146), E230 (= E231)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ K25), H23 (≠ A26), R24 (≠ Y27), A62 (= A65), F64 (≠ G67), Y65 (≠ D68), L66 (= L69), R67 (= R70), W89 (≠ F90), G113 (= G114), G114 (= G115), A136 (= A137), W137 (≠ Y138), D145 (= D146), T146 (≠ G147), F252 (= F253)
- binding calcium ion: G49 (≠ R52), L202 (≠ I203), A203 (≠ L204), A205 (≠ R206), T207 (≠ S208), Q210 (≠ F211)
- binding phosphate ion: E57 (≠ G60), N108 (= N109), K188 (≠ Q189), R192 (≠ V193)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 96% coverage: 8:261/264 of query aligns to 5:249/250 of 3q0gD
- active site: A64 (≠ G67), M69 (vs. gap), T75 (≠ N76), F79 (≠ G80), G103 (= G115), E106 (≠ S118), P125 (≠ A137), E126 (≠ Y138), V131 (≠ L143), P133 (≠ L145), G134 (≠ D146), L219 (≠ E231), F229 (≠ G241)
- binding Butyryl Coenzyme A: F225 (≠ L237), F241 (= F253)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
33% identity, 94% coverage: 14:262/264 of query aligns to 15:258/260 of 2hw5C
- active site: A68 (≠ G67), M73 (≠ I72), S83 (≠ A87), L87 (≠ H91), G111 (= G115), E114 (≠ S118), P133 (≠ A137), E134 (≠ Y138), T139 (≠ L143), P141 (≠ L145), G142 (≠ D146), K227 (vs. gap), F237 (≠ G241)
- binding crotonyl coenzyme a: K26 (= K25), A27 (= A26), L28 (≠ Y27), A30 (= A29), K62 (= K61), I70 (≠ L69), F109 (≠ A113)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
33% identity, 95% coverage: 13:262/264 of query aligns to 14:256/258 of 1mj3A
- active site: A68 (≠ G67), M73 (≠ I72), S83 (≠ H84), L85 (= L86), G109 (= G115), E112 (≠ S118), P131 (≠ A137), E132 (≠ Y138), T137 (≠ L143), P139 (≠ L145), G140 (≠ D146), K225 (vs. gap), F235 (≠ G241)
- binding hexanoyl-coenzyme a: K26 (= K25), A27 (= A26), L28 (≠ Y27), A30 (= A29), A66 (= A65), G67 (= G66), A68 (≠ G67), D69 (= D68), I70 (≠ L69), G109 (= G115), P131 (≠ A137), E132 (≠ Y138), L135 (≠ N141), G140 (≠ D146)
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)
30% identity, 94% coverage: 12:258/264 of query aligns to 9:257/269 of A5JTM5
- R24 (≠ Y27) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ R37) mutation to T: Forms inclusion bodies.
- E43 (≠ A46) mutation to A: No effect on catalytic activity.
- D45 (≠ R48) mutation to A: No effect on catalytic activity.
- D46 (≠ E49) mutation to A: No effect on catalytic activity.
- G63 (= G66) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ G67) 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 (≠ D68) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (= R70) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ W71) mutation to T: No effect on catalytic activity.
- H81 (= H84) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ E85) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ F90) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (= H91) 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 (≠ L95) mutation to Q: No effect on catalytic activity.
- A112 (= A113) 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 (= G114) 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 (= G115) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G116) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D124) mutation to T: No effect on catalytic activity.
- D129 (≠ R130) mutation to T: No effect on catalytic activity.
- W137 (≠ Y138) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D146) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (= E164) mutation to T: No effect on catalytic activity.
- E175 (≠ K176) mutation to D: No effect on catalytic activity.
- W179 (= W180) mutation to F: No effect on catalytic activity.
- H208 (≠ S209) mutation to Q: No effect on catalytic activity.
- R216 (≠ L217) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E233) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.
- R257 (≠ K258) mutation to K: Retains catalytic activity and substrate CoA binding.; mutation to L: Significantly reduces catalytic activity and substrate CoA binding.
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, 93% coverage: 18:263/264 of query aligns to 23:267/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
32% identity, 95% coverage: 13:262/264 of query aligns to 12:256/258 of 1ey3A
- active site: A66 (≠ G67), M71 (≠ I72), S81 (≠ N76), L85 (≠ G80), G109 (= G115), E112 (≠ S118), P131 (≠ A137), E132 (≠ Y138), T137 (≠ L143), P139 (≠ L145), G140 (≠ D146), K225 (vs. gap), F235 (≠ G241)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K25), L26 (≠ Y27), A28 (= A29), A64 (= A65), G65 (= G66), A66 (≠ G67), D67 (= D68), I68 (≠ L69), L85 (≠ G80), W88 (≠ F83), G109 (= G115), P131 (≠ A137), L135 (≠ N141), G140 (≠ D146)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
32% identity, 95% coverage: 13:262/264 of query aligns to 14:258/260 of 1dubA
- active site: A68 (≠ G67), M73 (≠ I72), S83 (≠ N76), L87 (≠ G80), G111 (= G115), E114 (≠ S118), P133 (≠ A137), E134 (≠ Y138), T139 (≠ L143), P141 (≠ L145), G142 (≠ D146), K227 (vs. gap), F237 (≠ G241)
- binding acetoacetyl-coenzyme a: K26 (= K25), A27 (= A26), L28 (≠ Y27), A30 (= A29), A66 (= A65), A68 (≠ G67), D69 (= D68), I70 (≠ L69), Y107 (≠ L111), G110 (= G114), G111 (= G115), E114 (≠ S118), P133 (≠ A137), E134 (≠ Y138), L137 (≠ N141), G142 (≠ D146), F233 (≠ L237), F249 (= F253)
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)
32% identity, 95% coverage: 13:262/264 of query aligns to 44:288/290 of P14604
- E144 (≠ S118) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ Y138) 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)
32% identity, 95% coverage: 13:262/264 of query aligns to 13:252/254 of 2dubA
- active site: A67 (≠ G67), M72 (≠ I72), S82 (≠ A88), G105 (= G115), E108 (≠ S118), P127 (≠ A137), E128 (≠ Y138), T133 (≠ L143), P135 (≠ L145), G136 (≠ D146), K221 (vs. gap), F231 (≠ G241)
- binding octanoyl-coenzyme a: K25 (= K25), A26 (= A26), L27 (≠ Y27), A29 (= A29), A65 (= A65), A67 (≠ G67), D68 (= D68), I69 (≠ L69), K70 (≠ R70), G105 (= G115), E108 (≠ S118), P127 (≠ A137), E128 (≠ Y138), G136 (≠ D146), A137 (≠ G147)
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
30% identity, 92% coverage: 12:255/264 of query aligns to 9:254/269 of 1jxzB
- active site: C61 (= C64), F64 (≠ G67), I69 (= I72), A86 (= A87), Q90 (≠ H91), G113 (= G114), G114 (= G115), G117 (≠ S118), A136 (= A137), W137 (≠ Y138), I142 (≠ L143), N144 (≠ L145), D145 (= D146), E230 (= E231)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ K25), H23 (≠ A26), R24 (≠ Y27), A62 (= A65), F64 (≠ G67), Y65 (≠ D68), L66 (= L69), R67 (= R70), W89 (≠ F90), G113 (= G114), A136 (= A137), W137 (≠ Y138), I142 (≠ L143), D145 (= D146), T146 (≠ G147), F252 (= F253)
- binding calcium ion: G49 (≠ R52), L202 (≠ I203), A203 (≠ L204), A205 (≠ R206), T207 (≠ S208), Q210 (≠ F211)
Sites not aligning to the query:
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 89% coverage: 28:262/264 of query aligns to 27:259/261 of 5jbxB
- active site: A67 (≠ G67), R72 (≠ I72), L84 (≠ H84), R88 (≠ A88), G112 (= G115), E115 (≠ S118), T134 (≠ A137), E135 (≠ Y138), I140 (≠ L143), P142 (≠ L145), G143 (≠ D146), A228 (≠ E227), L238 (= L237)
- binding coenzyme a: A28 (= A29), A65 (= A65), D68 (= D68), L69 (= L69), K70 (≠ R70), L110 (≠ A113), G111 (= G114), T134 (≠ A137), E135 (≠ Y138), L138 (≠ N141), R168 (≠ P171)
Sites not aligning to the query:
4izcB Crystal structure of dmdd e121a in complex with mta-coa (see paper)
33% identity, 77% coverage: 2:205/264 of query aligns to 7:206/266 of 4izcB
- active site: L70 (≠ G67), H75 (≠ R70), C89 (≠ A87), H93 (= H91), G117 (= G115), A120 (≠ S118), E140 (≠ Y138), G148 (≠ D146)
- binding methylthioacryloyl-CoA: D29 (≠ K25), K30 (≠ A26), R31 (≠ Y27), A33 (= A29), A68 (= A65), L70 (≠ G67), D71 (= D68), L72 (= L69), W92 (≠ F90), G117 (= G115), P139 (≠ A137), E140 (≠ Y138), R143 (≠ N141), G148 (≠ D146)
Sites not aligning to the query:
Query Sequence
>WP_084517379.1 NCBI__GCF_000422285.1:WP_084517379.1
MGTSAADVMLEVQNGVGILELNRPKAYNAFDLPMVQRLADELVALAGREDVRGLIVTGHG
KAFCAGGDLRWIAGYNGRYGAAFHELAARFHQAILEMRRMPKPVIAALNGLAAGGGFSLA
LACDFRIMDRSAVLRQAYTSNGLSLDGGGTFTLPRIVGLARAMEVVTFDAPIDAAKALEW
GLVTEVVEQGRSVARALEVMEDILSRSSSSFAASKQLLLESFGNPFELQLEREREMLARC
GDHPNGHEGVGAFLEKRKPRFQPV
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