SitesBLAST
Comparing H281DRAFT_04594 FitnessBrowser__Burk376:H281DRAFT_04594 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)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 94% coverage: 16:262/262 of query aligns to 18:264/266 of O53561
- K135 (= K133) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 133:140, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ R140) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
32% identity, 98% coverage: 5:262/262 of query aligns to 4:256/258 of 1ey3A
- active site: A66 (≠ G67), M71 (≠ L72), S81 (= S86), L85 (= L90), G109 (≠ A115), E112 (≠ S118), P131 (≠ S137), E132 (≠ Y138), T137 (≠ L143), P139 (= P145), G140 (≠ D146), K225 (≠ V231), F235 (≠ L241)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ G25), L26 (≠ R27), A28 (= A29), A64 (= A65), G65 (= G66), A66 (≠ G67), D67 (≠ N68), I68 (≠ L69), L85 (= L90), W88 (= W93), G109 (≠ A115), P131 (≠ S137), L135 (≠ V141), G140 (≠ D146)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
32% identity, 98% coverage: 5:262/262 of query aligns to 6:258/260 of 1dubA
- active site: A68 (≠ G67), M73 (≠ L72), S83 (= S86), L87 (= L90), G111 (≠ A115), E114 (≠ S118), P133 (≠ S137), E134 (≠ Y138), T139 (≠ L143), P141 (= P145), G142 (≠ D146), K227 (≠ V231), F237 (≠ L241)
- binding acetoacetyl-coenzyme a: K26 (≠ G25), A27 (= A26), L28 (≠ R27), A30 (= A29), A66 (= A65), A68 (≠ G67), D69 (≠ N68), I70 (≠ L69), Y107 (≠ A111), G110 (= G114), G111 (≠ A115), E114 (≠ S118), P133 (≠ S137), E134 (≠ Y138), L137 (≠ V141), G142 (≠ D146), F233 (= F237), 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, 98% coverage: 5:262/262 of query aligns to 36:288/290 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, 98% coverage: 5:262/262 of query aligns to 5:252/254 of 2dubA
- active site: A67 (≠ G67), M72 (≠ L72), S82 (≠ A91), G105 (≠ A115), E108 (≠ S118), P127 (≠ S137), E128 (≠ Y138), T133 (≠ L143), P135 (= P145), G136 (≠ D146), K221 (≠ V231), F231 (≠ L241)
- binding octanoyl-coenzyme a: K25 (≠ G25), A26 (= A26), L27 (≠ R27), A29 (= A29), A65 (= A65), A67 (≠ G67), D68 (≠ N68), I69 (≠ L69), K70 (≠ N70), G105 (≠ A115), E108 (≠ S118), P127 (≠ S137), E128 (≠ Y138), G136 (≠ D146), A137 (≠ G147)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
32% identity, 98% coverage: 5:262/262 of query aligns to 6:256/258 of 1mj3A
- active site: A68 (≠ G67), M73 (≠ L72), S83 (≠ Q83), L85 (= L90), G109 (≠ A115), E112 (≠ S118), P131 (≠ S137), E132 (≠ Y138), T137 (≠ L143), P139 (= P145), G140 (≠ D146), K225 (≠ V231), F235 (≠ L241)
- binding hexanoyl-coenzyme a: K26 (≠ G25), A27 (= A26), L28 (≠ R27), A30 (= A29), A66 (= A65), G67 (= G66), A68 (≠ G67), D69 (≠ N68), I70 (≠ L69), G109 (≠ A115), P131 (≠ S137), E132 (≠ Y138), L135 (≠ V141), G140 (≠ D146)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
33% identity, 96% coverage: 11:262/262 of query aligns to 8:257/259 of 5zaiC
- active site: A65 (≠ G67), F70 (vs. gap), S82 (= S81), R86 (≠ Q85), G110 (≠ A115), E113 (≠ S118), P132 (≠ S137), E133 (≠ Y138), I138 (≠ L143), P140 (= P145), G141 (≠ D146), A226 (≠ V231), F236 (≠ L241)
- binding coenzyme a: K24 (≠ A26), L25 (≠ R27), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (≠ N68), I67 (≠ L69), P132 (≠ S137), R166 (≠ P171), F248 (= F253), K251 (= K256)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 98% coverage: 5:262/262 of query aligns to 6:258/260 of 2hw5C
- active site: A68 (≠ G67), M73 (≠ L72), S83 (= S86), L87 (= L90), G111 (≠ A115), E114 (≠ S118), P133 (≠ S137), E134 (≠ Y138), T139 (≠ L143), P141 (= P145), G142 (≠ D146), K227 (≠ V231), F237 (≠ L241)
- binding crotonyl coenzyme a: K26 (≠ G25), A27 (= A26), L28 (≠ R27), A30 (= A29), K62 (≠ N61), I70 (≠ L69), F109 (≠ A113)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 93% coverage: 18:261/262 of query aligns to 16:254/255 of 3q0jC
- active site: A65 (≠ G67), M70 (≠ L72), T80 (≠ S86), F84 (≠ L90), G108 (≠ A115), E111 (≠ S118), P130 (≠ S137), E131 (≠ Y138), V136 (≠ L143), P138 (= P145), G139 (≠ D146), L224 (≠ V231), F234 (≠ L241)
- binding acetoacetyl-coenzyme a: Q23 (≠ G25), A24 (= A26), L25 (≠ R27), A27 (= A29), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (≠ N68), I67 (≠ L69), K68 (≠ N70), M70 (≠ L72), F84 (≠ L90), G107 (= G114), G108 (≠ A115), E111 (≠ S118), P130 (≠ S137), E131 (≠ Y138), P138 (= P145), G139 (≠ D146), M140 (≠ G147)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 93% coverage: 18:261/262 of query aligns to 16:254/255 of 3q0gC
- active site: A65 (≠ G67), M70 (≠ L72), T80 (≠ S86), F84 (≠ L90), G108 (≠ A115), E111 (≠ S118), P130 (≠ S137), E131 (≠ Y138), V136 (≠ L143), P138 (= P145), G139 (≠ D146), L224 (≠ V231), F234 (≠ L241)
- binding coenzyme a: L25 (≠ R27), A63 (= A65), I67 (≠ L69), K68 (≠ N70), Y104 (≠ A111), P130 (≠ S137), E131 (≠ Y138), L134 (≠ V141)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 93% coverage: 18:261/262 of query aligns to 15:249/250 of 3q0gD
- active site: A64 (≠ G67), M69 (≠ L72), T75 (≠ S86), F79 (≠ L90), G103 (≠ A115), E106 (≠ S118), P125 (≠ S137), E126 (≠ Y138), V131 (≠ L143), P133 (= P145), G134 (≠ D146), L219 (≠ V231), F229 (≠ L241)
- binding Butyryl Coenzyme A: F225 (= F237), F241 (= F253)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 93% coverage: 18:261/262 of query aligns to 15:253/256 of 3h81A
- active site: A64 (≠ G67), M69 (≠ L72), T79 (≠ S86), F83 (≠ L90), G107 (≠ A115), E110 (≠ S118), P129 (≠ S137), E130 (≠ Y138), V135 (≠ L143), P137 (= P145), G138 (≠ D146), L223 (≠ V231), F233 (≠ L241)
- binding calcium ion: F233 (≠ L241), Q238 (≠ G246)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
34% identity, 94% coverage: 18:262/262 of query aligns to 17:259/261 of 5jbxB
- active site: A67 (≠ G67), R72 (= R76), L84 (≠ I87), R88 (≠ A91), G112 (≠ A115), E115 (≠ S118), T134 (≠ S137), E135 (≠ Y138), I140 (≠ L143), P142 (= P145), G143 (≠ D146), A228 (≠ V231), L238 (= L241)
- binding coenzyme a: S24 (≠ G25), R25 (≠ A26), R26 (= R27), A28 (= A29), A65 (= A65), D68 (≠ N68), L69 (= L69), K70 (≠ E74), L110 (≠ A113), G111 (= G114), T134 (≠ S137), E135 (≠ Y138), L138 (≠ V141), R168 (≠ P171)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 95% coverage: 13:262/262 of query aligns to 10:255/257 of 6slbAAA
- active site: Q64 (≠ G67), F69 (≠ L72), L80 (≠ A84), N84 (≠ D88), A108 (= A115), S111 (= S118), A130 (≠ S137), F131 (≠ Y138), L136 (= L143), P138 (= P145), D139 (= D146), A224 (≠ V231), G234 (≠ L241)
- 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 (≠ N61), A62 (= A65), Q64 (≠ G67), D65 (≠ N68), L66 (= L69), Y76 (≠ P80), A108 (= A115), F131 (≠ Y138), D139 (= D146)
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
33% identity, 92% coverage: 17:256/262 of query aligns to 13:247/247 of 7borA
- active site: N63 (≠ G67), F68 (≠ L72), D77 (≠ A84), G81 (≠ A91), I105 (≠ A115), T108 (≠ S118), F128 (≠ Y138), L133 (= L143), P135 (= P145), E136 (≠ D146), A222 (≠ V231), L232 (= L241)
- binding coenzyme a: D21 (≠ G25), K22 (≠ A26), A25 (= A29), S61 (≠ A65), I65 (≠ L69), V103 (≠ A113), F128 (≠ Y138), L131 (≠ V141), F244 (= F253), R247 (≠ K256)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
31% identity, 95% coverage: 13:262/262 of query aligns to 7:243/245 of 6slaAAA
- active site: Q61 (≠ G67), L68 (≠ A84), N72 (≠ D88), A96 (= A115), S99 (= S118), A118 (≠ S137), F119 (≠ Y138), L124 (= L143), P126 (= P145), N127 (≠ D146), A212 (≠ V231), G222 (≠ L241)
- 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 (≠ R27), A59 (= A65), Q61 (≠ G67), D62 (≠ N68), L63 (= L69), L68 (≠ A84), Y71 (≠ I87), A94 (= A113), G95 (= G114), A96 (= A115), F119 (≠ Y138), I122 (≠ V141), L124 (= L143), N127 (≠ D146), F234 (= F253), K237 (= K256)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
30% identity, 93% coverage: 19:261/262 of query aligns to 21:253/260 of 2uzfA
- active site: G70 (= G67), R80 (≠ Q83), L84 (≠ I87), G108 (≠ A115), V111 (≠ S118), T130 (≠ S137), G131 (≠ Y138), S136 (≠ L143), D138 (≠ P145), A139 (≠ D146), A225 (≠ S227), Y233 (≠ L241)
- binding acetoacetyl-coenzyme a: V28 (≠ A26), R29 (= R27), S68 (≠ A65), G69 (= G66), G70 (= G67), D71 (≠ N68), Y104 (≠ A111), G108 (≠ A115)
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)
29% identity, 98% coverage: 6:262/262 of query aligns to 13:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
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)
29% identity, 90% coverage: 19:255/262 of query aligns to 16:254/269 of A5JTM5
- R24 (= R27) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ A37) mutation to T: Forms inclusion bodies.
- E43 (= E46) mutation to A: No effect on catalytic activity.
- D45 (= D48) mutation to A: No effect on catalytic activity.
- D46 (≠ P49) 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 (≠ N68) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ N70) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ R71) mutation to T: No effect on catalytic activity.
- H81 (≠ A84) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ Q85) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (vs. gap) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ A91) 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 (≠ S95) 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 (≠ A115) 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 (= D130) 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 (≠ R176) mutation to D: No effect on catalytic activity.
- W179 (≠ L180) mutation to F: No effect on catalytic activity.
- H208 (≠ N209) 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.
Sites not aligning to the query:
- 257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
29% identity, 90% coverage: 19:255/262 of query aligns to 16:254/269 of 1jxzB
- active site: C61 (= C64), F64 (≠ G67), I69 (≠ L72), A86 (= A91), Q90 (vs. gap), G113 (= G114), G114 (≠ A115), G117 (≠ S118), A136 (≠ S137), W137 (≠ Y138), I142 (≠ L143), N144 (≠ P145), D145 (= D146), E230 (≠ V231)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ G25), H23 (≠ A26), R24 (= R27), A62 (= A65), F64 (≠ G67), Y65 (≠ N68), L66 (= L69), R67 (≠ N70), W89 (vs. gap), G113 (= G114), A136 (≠ S137), W137 (≠ Y138), I142 (≠ L143), D145 (= D146), T146 (≠ G147), F252 (= F253)
- binding calcium ion: G49 (≠ R52), L202 (= L203), A203 (≠ G204), A205 (≠ I206), T207 (≠ P208), Q210 (≠ V211)
Sites not aligning to the query:
Query Sequence
>H281DRAFT_04594 FitnessBrowser__Burk376:H281DRAFT_04594
MSAELLTSRPTESESTLVLTLSNPGARNALHPDMYAAGIEALDSVERDPSIRAVVITGAD
NFFCAGGNLNRLLENRAKDPSVQAQSIDLLAEWISALRLSSKPVIAAVDGAAAGAGFSLA
LACDLIVAADDAKFVMSYARVGLTPDGGGSWFLAQALPRQLATEVLIEGKPIGAARLHEL
GVVNKLTKPGTARDAAIAWADELGKISPNSVARIKTLVCAAGTQPLSEHLVAERDNFVAS
LHHREGLEGISAFLEKRAPVYK
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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