SitesBLAST
Comparing Ac3H11_4006 FitnessBrowser__acidovorax_3H11:Ac3H11_4006 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)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
61% identity, 99% coverage: 3:259/259 of query aligns to 2:256/256 of 3h81A
- active site: A64 (= A66), M69 (= M71), T79 (≠ K81), F83 (≠ I85), G107 (= G110), E110 (= E113), P129 (= P132), E130 (= E133), V135 (= V138), P137 (= P140), G138 (= G141), L223 (≠ M226), F233 (= F236)
- binding calcium ion: F233 (= F236), Q238 (= Q241)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
61% identity, 99% coverage: 1:257/259 of query aligns to 1:255/255 of 3q0jC
- active site: A65 (= A66), M70 (= M71), T80 (≠ K81), F84 (≠ I85), G108 (= G110), E111 (= E113), P130 (= P132), E131 (= E133), V136 (= V138), P138 (= P140), G139 (= G141), L224 (≠ M226), F234 (= F236)
- binding acetoacetyl-coenzyme a: Q23 (≠ K24), A24 (≠ Q25), L25 (= L26), A27 (= A28), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (= I68), K68 (≠ G69), M70 (= M71), F84 (≠ I85), G107 (= G109), G108 (= G110), E111 (= E113), P130 (= P132), E131 (= E133), P138 (= P140), G139 (= G141), M140 (≠ A142)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
61% identity, 99% coverage: 1:257/259 of query aligns to 1:255/255 of 3q0gC
- active site: A65 (= A66), M70 (= M71), T80 (≠ K81), F84 (≠ I85), G108 (= G110), E111 (= E113), P130 (= P132), E131 (= E133), V136 (= V138), P138 (= P140), G139 (= G141), L224 (≠ M226), F234 (= F236)
- binding coenzyme a: L25 (= L26), A63 (= A64), I67 (= I68), K68 (≠ G69), Y104 (≠ F106), P130 (= P132), E131 (= E133), L134 (= L136)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
61% identity, 98% coverage: 3:257/259 of query aligns to 2:250/250 of 3q0gD
- active site: A64 (= A66), M69 (= M71), T75 (≠ K81), F79 (≠ I85), G103 (= G110), E106 (= E113), P125 (= P132), E126 (= E133), V131 (= V138), P133 (= P140), G134 (= G141), L219 (≠ M226), F229 (= F236)
- binding Butyryl Coenzyme A: F225 (= F232), F241 (= F248)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
54% identity, 99% coverage: 3:259/259 of query aligns to 5:260/260 of 2hw5C
- active site: A68 (= A66), M73 (= M71), S83 (≠ K81), L87 (≠ I85), G111 (= G110), E114 (= E113), P133 (= P132), E134 (= E133), T139 (≠ V138), P141 (= P140), G142 (= G141), K227 (≠ M226), F237 (= F236)
- binding crotonyl coenzyme a: K26 (= K24), A27 (≠ Q25), L28 (= L26), A30 (= A28), K62 (= K60), I70 (= I68), F109 (≠ L108)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
55% identity, 98% coverage: 3:256/259 of query aligns to 5:257/260 of 1dubA
- active site: A68 (= A66), M73 (= M71), S83 (≠ K81), L87 (≠ I85), G111 (= G110), E114 (= E113), P133 (= P132), E134 (= E133), T139 (≠ V138), P141 (= P140), G142 (= G141), K227 (≠ M226), F237 (= F236)
- binding acetoacetyl-coenzyme a: K26 (= K24), A27 (≠ Q25), L28 (= L26), A30 (= A28), A66 (= A64), A68 (= A66), D69 (= D67), I70 (= I68), Y107 (≠ F106), G110 (= G109), G111 (= G110), E114 (= E113), P133 (= P132), E134 (= E133), L137 (= L136), G142 (= G141), F233 (= F232), F249 (= F248)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
55% identity, 98% coverage: 3:256/259 of query aligns to 3:255/258 of 1ey3A
- active site: A66 (= A66), M71 (= M71), S81 (≠ K81), L85 (≠ I85), G109 (= G110), E112 (= E113), P131 (= P132), E132 (= E133), T137 (≠ V138), P139 (= P140), G140 (= G141), K225 (≠ M226), F235 (= F236)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K24), L26 (= L26), A28 (= A28), A64 (= A64), G65 (= G65), A66 (= A66), D67 (= D67), I68 (= I68), L85 (≠ I85), W88 (= W89), G109 (= G110), P131 (= P132), L135 (= L136), G140 (= G141)
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)
55% identity, 98% coverage: 3:256/259 of query aligns to 35:287/290 of P14604
- E144 (= E113) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E133) 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)
55% identity, 98% coverage: 3:256/259 of query aligns to 5:255/258 of 1mj3A
- active site: A68 (= A66), M73 (= M71), S83 (≠ K81), L85 (≠ T86), G109 (= G110), E112 (= E113), P131 (= P132), E132 (= E133), T137 (≠ V138), P139 (= P140), G140 (= G141), K225 (≠ M226), F235 (= F236)
- binding hexanoyl-coenzyme a: K26 (= K24), A27 (≠ Q25), L28 (= L26), A30 (= A28), A66 (= A64), G67 (= G65), A68 (= A66), D69 (= D67), I70 (= I68), G109 (= G110), P131 (= P132), E132 (= E133), L135 (= L136), G140 (= G141)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
55% identity, 98% coverage: 3:256/259 of query aligns to 4:251/254 of 2dubA
- active site: A67 (= A66), M72 (= M71), S82 (≠ K81), G105 (= G110), E108 (= E113), P127 (= P132), E128 (= E133), T133 (≠ V138), P135 (= P140), G136 (= G141), K221 (≠ M226), F231 (= F236)
- binding octanoyl-coenzyme a: K25 (= K24), A26 (≠ Q25), L27 (= L26), A29 (= A28), A65 (= A64), A67 (= A66), D68 (= D67), I69 (= I68), K70 (≠ G69), G105 (= G110), E108 (= E113), P127 (= P132), E128 (= E133), G136 (= G141), A137 (= A142)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
43% identity, 99% coverage: 1:256/259 of query aligns to 1:256/259 of 5zaiC
- active site: A65 (= A66), F70 (≠ M71), S82 (≠ D83), R86 (= R87), G110 (= G110), E113 (= E113), P132 (= P132), E133 (= E133), I138 (≠ V138), P140 (= P140), G141 (= G141), A226 (≠ M226), F236 (= F236)
- binding coenzyme a: K24 (≠ Q25), L25 (= L26), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (= I68), P132 (= P132), R166 (≠ M166), F248 (= F248), K251 (= K251)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
37% identity, 92% coverage: 15:252/259 of query aligns to 15:254/261 of 5jbxB
- active site: A67 (= A66), R72 (≠ M71), L84 (≠ I85), R88 (≠ W89), G112 (= G110), E115 (= E113), T134 (≠ P132), E135 (= E133), I140 (≠ V138), P142 (= P140), G143 (= G141), A228 (≠ M226), L238 (≠ F236)
- binding coenzyme a: S24 (≠ K24), R25 (≠ Q25), R26 (≠ L26), A28 (= A28), A65 (= A64), D68 (= D67), L69 (≠ I68), K70 (≠ G69), L110 (= L108), G111 (= G109), T134 (≠ P132), E135 (= E133), L138 (= L136), R168 (≠ M166)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 94% coverage: 13:256/259 of query aligns to 11:254/257 of 6slbAAA
- active site: Q64 (≠ A66), F69 (= F76), L80 (vs. gap), N84 (≠ T86), A108 (≠ G110), S111 (≠ E113), A130 (≠ P132), F131 (≠ E133), L136 (≠ V138), P138 (= P140), D139 (≠ G141), A224 (≠ M226), G234 (≠ F236)
- 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 (≠ K60), A62 (= A64), Q64 (≠ A66), D65 (= D67), L66 (≠ I68), Y76 (= Y84), A108 (≠ G110), F131 (≠ E133), D139 (≠ G141)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 94% coverage: 13:256/259 of query aligns to 8:242/245 of 6slaAAA
- active site: Q61 (≠ A66), L68 (≠ K81), N72 (≠ T86), A96 (≠ G110), S99 (≠ E113), A118 (≠ P132), F119 (≠ E133), L124 (≠ V138), P126 (= P140), N127 (≠ G141), A212 (≠ M226), G222 (≠ F236)
- 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 (= L26), A59 (= A64), Q61 (≠ A66), D62 (= D67), L63 (≠ I68), L68 (≠ K81), Y71 (= Y84), A94 (≠ L108), G95 (= G109), A96 (≠ G110), F119 (≠ E133), I122 (≠ L136), L124 (≠ V138), N127 (≠ G141), F234 (= F248), K237 (= K251)
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
37% identity, 83% coverage: 13:228/259 of query aligns to 9:210/224 of 3p85A
- active site: L62 (≠ A66), L67 (≠ M71), P68 (≠ A72), G92 (= G110), E95 (= E113), T114 (≠ P132), H115 (≠ E133), L120 (≠ V138), P122 (= P140), T123 (≠ G141), W208 (≠ M226)
- binding calcium ion: D43 (= D47), D45 (≠ N49)
Sites not aligning to the query:
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
34% identity, 94% coverage: 17:259/259 of query aligns to 20:266/266 of O53561
- K135 (≠ R128) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 128:135, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K135) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
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)
35% identity, 94% coverage: 15:257/259 of query aligns to 87:331/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
34% identity, 98% coverage: 3:257/259 of query aligns to 18:275/281 of 3t88A
- active site: G82 (≠ A66), R87 (≠ M71), Y93 (= Y80), H101 (≠ N88), L105 (vs. gap), G129 (= G110), V132 (≠ E113), G152 (≠ E133), S157 (≠ V138), D159 (≠ P140), G160 (= G141), A246 (≠ V225), Y254 (≠ F236)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ K24), V40 (≠ Q25), R41 (≠ L26), A43 (= A28), S80 (≠ A64), G81 (= G65), G82 (≠ A66), D83 (= D67), Q84 (≠ I68), K85 (≠ G69), Y93 (= Y80), V104 (≠ T91), L105 (vs. gap), Y125 (≠ F106), G129 (= G110), T151 (≠ P132), V155 (≠ L136), F158 (≠ I139), D159 (≠ P140), T250 (≠ R229), Y254 (≠ F236), F266 (= F248), K269 (= K251)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
34% identity, 98% coverage: 3:257/259 of query aligns to 22:279/285 of 4i42A
- active site: G86 (≠ A66), R91 (≠ M71), Y97 (= Y80), H105 (≠ N88), L109 (vs. gap), G133 (= G110), V136 (≠ E113), G156 (≠ E133), S161 (≠ V138), D163 (≠ P140), G164 (= G141), A250 (≠ V225), Y258 (≠ F236)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ Q25), R45 (≠ L26), S84 (≠ A64), G85 (= G65), G86 (≠ A66), D87 (= D67), Q88 (≠ I68), K89 (≠ G69), Y97 (= Y80), V108 (≠ T91), Y129 (≠ F106), G133 (= G110), T155 (≠ P132), S161 (≠ V138), T254 (≠ R229), F270 (= F248), K273 (= K251)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 98% coverage: 3:257/259 of query aligns to 22:279/285 of P0ABU0
- R45 (≠ L26) binding in other chain
- SGGDQK 84:89 (≠ AGADIG 64:69) binding in other chain
- K89 (≠ G69) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ M71) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y80) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ FALGG 106:110) binding in other chain
- Q154 (= Q131) mutation to A: Reduces the specific DHNA-CoA synthase activity by 15-fold, whereas its affinity for hydrogencarbonate is reduced by 36-fold.
- QTG 154:156 (≠ QPE 131:133) binding
- T155 (≠ P132) binding in other chain
- G156 (≠ E133) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ V138) binding in other chain
- W184 (≠ A161) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ F236) binding
- R267 (≠ M245) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F248) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K251) binding ; mutation to A: Impairs protein folding.
Query Sequence
>Ac3H11_4006 FitnessBrowser__acidovorax_3H11:Ac3H11_4006
MAYETIEVRVEADKVGVITLNRPKQLNALNDQLMNELGAALKAFDADENIGCMIVTGSEK
AFAAGADIGAMAKYSFADTYKGDYITRNWETIRSIRKPVIAAVSGFALGGGCELAMMCDF
IIAADNARFGQPEIKLGVIPGAGGTQRLPRAVGKSKAMDMALTGRMMDAAEAERAGLVSR
VVPYDKLMDEALGAAIIVAGFSQLAVMAAKESVNRAFEGTLSDGVMFERRLFHALFATQD
QKEGMDAFMNKRPANFTHQ
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