SitesBLAST
Comparing CCNA_02658 CCNA_02658 3-hydroxybutyryl-CoA dehydratase 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)
38% identity, 100% coverage: 1:264/265 of query aligns to 2:256/257 of 6slbAAA
- active site: Q64 (≠ G64), F69 (≠ M69), L80 (≠ R88), N84 (≠ H92), A108 (≠ L116), S111 (≠ D119), A130 (≠ T138), F131 (= F139), L136 (= L144), P138 (= P146), D139 (≠ G147), A224 (≠ E232), G234 (≠ H242)
- 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 (≠ K58), A62 (= A62), Q64 (≠ G64), D65 (= D65), L66 (≠ V66), Y76 (≠ F76), A108 (≠ L116), F131 (= F139), D139 (≠ G147)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 99% coverage: 3:264/265 of query aligns to 1:244/245 of 6slaAAA
- active site: Q61 (≠ G64), L68 (≠ R88), N72 (≠ H92), A96 (≠ L116), S99 (≠ D119), A118 (≠ T138), F119 (= F139), L124 (= L144), P126 (= P146), N127 (≠ G147), A212 (≠ E232), G222 (≠ H242)
- 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 (≠ M23), A59 (= A62), Q61 (≠ G64), D62 (= D65), L63 (≠ V66), L68 (≠ R88), Y71 (≠ I91), A94 (≠ I114), G95 (= G115), A96 (≠ L116), F119 (= F139), I122 (≠ L142), L124 (= L144), N127 (≠ G147), F234 (≠ I254), K237 (= K257)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
40% identity, 98% coverage: 4:262/265 of query aligns to 5:249/250 of 3q0gD
- active site: A64 (≠ G64), M69 (= M69), T75 (≠ R88), F79 (≠ H92), G103 (≠ L116), E106 (≠ D119), P125 (≠ T138), E126 (≠ F139), V131 (≠ L144), P133 (= P146), G134 (= G147), L219 (≠ E232), F229 (≠ H242)
- binding Butyryl Coenzyme A: F225 (≠ Q238), F241 (≠ I254)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
40% identity, 98% coverage: 4:262/265 of query aligns to 6:254/255 of 3q0jC
- active site: A65 (≠ G64), M70 (= M69), T80 (≠ R88), F84 (≠ H92), G108 (≠ L116), E111 (≠ D119), P130 (≠ T138), E131 (≠ F139), V136 (≠ L144), P138 (= P146), G139 (= G147), L224 (≠ E232), F234 (≠ H242)
- binding acetoacetyl-coenzyme a: Q23 (≠ D21), A24 (= A22), L25 (≠ M23), A27 (= A25), A63 (= A62), G64 (= G63), A65 (≠ G64), D66 (= D65), I67 (≠ V66), K68 (= K67), M70 (= M69), F84 (≠ H92), G107 (= G115), G108 (≠ L116), E111 (≠ D119), P130 (≠ T138), E131 (≠ F139), P138 (= P146), G139 (= G147), M140 (≠ D148)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
40% identity, 98% coverage: 4:262/265 of query aligns to 6:254/255 of 3q0gC
- active site: A65 (≠ G64), M70 (= M69), T80 (≠ R88), F84 (≠ H92), G108 (≠ L116), E111 (≠ D119), P130 (≠ T138), E131 (≠ F139), V136 (≠ L144), P138 (= P146), G139 (= G147), L224 (≠ E232), F234 (≠ H242)
- binding coenzyme a: L25 (≠ M23), A63 (= A62), I67 (≠ V66), K68 (= K67), Y104 (≠ A112), P130 (≠ T138), E131 (≠ F139), L134 (= L142)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
40% identity, 98% coverage: 4:262/265 of query aligns to 5:253/256 of 3h81A
- active site: A64 (≠ G64), M69 (= M69), T79 (≠ R88), F83 (≠ H92), G107 (≠ L116), E110 (≠ D119), P129 (≠ T138), E130 (≠ F139), V135 (≠ L144), P137 (= P146), G138 (= G147), L223 (≠ E232), F233 (≠ H242)
- binding calcium ion: F233 (≠ H242), Q238 (≠ H247)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
37% identity, 98% coverage: 4:264/265 of query aligns to 6:258/259 of 5zaiC
- active site: A65 (≠ G64), F70 (≠ M69), S82 (≠ R88), R86 (≠ H92), G110 (≠ L116), E113 (≠ D119), P132 (≠ T138), E133 (≠ F139), I138 (≠ L144), P140 (= P146), G141 (= G147), A226 (≠ E232), F236 (≠ H242)
- binding coenzyme a: K24 (≠ A22), L25 (≠ M23), A63 (= A62), G64 (= G63), A65 (≠ G64), D66 (= D65), I67 (≠ V66), P132 (≠ T138), R166 (≠ V172), F248 (≠ I254), K251 (= K257)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
36% identity, 99% coverage: 1:263/265 of query aligns to 1:256/258 of 1ey3A
- active site: A66 (≠ G64), M71 (= M69), S81 (≠ R88), L85 (≠ H92), G109 (≠ L116), E112 (≠ D119), P131 (≠ T138), E132 (≠ F139), T137 (≠ L144), P139 (= P146), G140 (= G147), K225 (≠ A235), F235 (vs. gap)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D21), L26 (≠ M23), A28 (= A25), A64 (= A62), G65 (= G63), A66 (≠ G64), D67 (= D65), I68 (≠ V66), L85 (≠ H92), W88 (≠ V95), G109 (≠ L116), P131 (≠ T138), L135 (= L142), G140 (= G147)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
36% identity, 99% coverage: 1:263/265 of query aligns to 3:258/260 of 1dubA
- active site: A68 (≠ G64), M73 (= M69), S83 (≠ R88), L87 (≠ H92), G111 (≠ L116), E114 (≠ D119), P133 (≠ T138), E134 (≠ F139), T139 (≠ L144), P141 (= P146), G142 (= G147), K227 (≠ A235), F237 (vs. gap)
- binding acetoacetyl-coenzyme a: K26 (≠ D21), A27 (= A22), L28 (≠ M23), A30 (= A25), A66 (= A62), A68 (≠ G64), D69 (= D65), I70 (≠ V66), Y107 (≠ A112), G110 (= G115), G111 (≠ L116), E114 (≠ D119), P133 (≠ T138), E134 (≠ F139), L137 (= L142), G142 (= G147), F233 (≠ A241), F249 (≠ I254)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
37% identity, 99% coverage: 1:263/265 of query aligns to 2:252/254 of 2dubA
- active site: A67 (≠ G64), M72 (= M69), S82 (≠ R88), G105 (≠ L116), E108 (≠ D119), P127 (≠ T138), E128 (≠ F139), T133 (≠ L144), P135 (= P146), G136 (= G147), K221 (≠ A235), F231 (vs. gap)
- binding octanoyl-coenzyme a: K25 (≠ D21), A26 (= A22), L27 (≠ M23), A29 (= A25), A65 (= A62), A67 (≠ G64), D68 (= D65), I69 (≠ V66), K70 (= K67), G105 (≠ L116), E108 (≠ D119), P127 (≠ T138), E128 (≠ F139), G136 (= G147), A137 (≠ D148)
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)
36% identity, 99% coverage: 1:263/265 of query aligns to 33:288/290 of P14604
- E144 (≠ D119) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F139) 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)
37% identity, 99% coverage: 1:263/265 of query aligns to 3:256/258 of 1mj3A
- active site: A68 (≠ G64), M73 (= M69), S83 (≠ N79), L85 (≠ V81), G109 (≠ L116), E112 (≠ D119), P131 (≠ T138), E132 (≠ F139), T137 (≠ L144), P139 (= P146), G140 (= G147), K225 (≠ A235), F235 (vs. gap)
- binding hexanoyl-coenzyme a: K26 (≠ D21), A27 (= A22), L28 (≠ M23), A30 (= A25), A66 (= A62), G67 (= G63), A68 (≠ G64), D69 (= D65), I70 (≠ V66), G109 (≠ L116), P131 (≠ T138), E132 (≠ F139), L135 (= L142), G140 (= G147)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 99% coverage: 1:263/265 of query aligns to 3:258/260 of 2hw5C
- active site: A68 (≠ G64), M73 (= M69), S83 (≠ R88), L87 (≠ H92), G111 (≠ L116), E114 (≠ D119), P133 (≠ T138), E134 (≠ F139), T139 (≠ L144), P141 (= P146), G142 (= G147), K227 (≠ A235), F237 (vs. gap)
- binding crotonyl coenzyme a: K26 (≠ D21), A27 (= A22), L28 (≠ M23), A30 (= A25), K62 (= K58), I70 (≠ V66), F109 (≠ I114)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
34% identity, 100% coverage: 1:264/265 of query aligns to 4:260/261 of 5jbxB
- active site: A67 (≠ G64), R72 (≠ E73), L84 (≠ R88), R88 (≠ H92), G112 (≠ L116), E115 (≠ D119), T134 (= T138), E135 (≠ F139), I140 (≠ L144), P142 (= P146), G143 (= G147), A228 (≠ E232), L238 (≠ H242)
- binding coenzyme a: S24 (≠ D21), R25 (≠ A22), R26 (≠ M23), A28 (= A25), A65 (= A62), D68 (= D65), L69 (≠ V66), K70 (= K67), L110 (≠ I114), G111 (= G115), T134 (= T138), E135 (≠ F139), L138 (= L142), R168 (≠ V172)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
37% identity, 98% coverage: 5:263/265 of query aligns to 11:264/266 of O53561
- K135 (≠ R134) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 134:141, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K141) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
36% identity, 95% coverage: 12:262/265 of query aligns to 34:278/285 of 4i42A
- active site: G86 (= G64), R91 (≠ M69), Y97 (≠ A75), H105 (≠ R88), L109 (≠ H92), G133 (≠ L116), V136 (≠ D119), G156 (≠ F139), S161 (≠ L144), D163 (≠ P146), G164 (= G147), A250 (≠ S234), Y258 (≠ H242)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ A22), R45 (≠ M23), S84 (≠ A62), G85 (= G63), G86 (= G64), D87 (= D65), Q88 (≠ V66), K89 (= K67), Y97 (≠ A75), V108 (≠ I91), Y129 (≠ A112), G133 (≠ L116), T155 (= T138), S161 (≠ L144), T254 (≠ Q238), F270 (≠ I254), K273 (= K257)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
36% identity, 95% coverage: 12:262/265 of query aligns to 34:278/285 of P0ABU0
- R45 (≠ M23) binding in other chain
- SGGDQK 84:89 (≠ AGGDVK 62:67) binding in other chain
- K89 (= K67) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ M69) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ A75) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAIGL 112:116) binding in other chain
- Q154 (≠ V137) 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 (≠ VTF 137:139) binding
- T155 (= T138) binding in other chain
- G156 (≠ F139) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L144) binding in other chain
- W184 (≠ L167) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ H242) binding
- R267 (≠ V251) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (≠ I254) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K257) binding ; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
36% identity, 95% coverage: 12:262/265 of query aligns to 30:274/281 of 3t88A
- active site: G82 (= G64), R87 (≠ M69), Y93 (≠ A75), H101 (≠ R88), L105 (≠ H92), G129 (≠ L116), V132 (≠ D119), G152 (≠ F139), S157 (≠ L144), D159 (≠ P146), G160 (= G147), A246 (≠ S234), Y254 (≠ H242)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D21), V40 (≠ A22), R41 (≠ M23), A43 (= A25), S80 (≠ A62), G81 (= G63), G82 (= G64), D83 (= D65), Q84 (≠ V66), K85 (= K67), Y93 (≠ A75), V104 (≠ I91), L105 (≠ H92), Y125 (≠ A112), G129 (≠ L116), T151 (= T138), V155 (≠ L142), F158 (≠ I145), D159 (≠ P146), T250 (≠ Q238), Y254 (≠ H242), F266 (≠ I254), K269 (= K257)
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, 95% coverage: 12:263/265 of query aligns to 25:269/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
3rrvB Crystal structure of an enoyl-coa hydratase/isomerase from mycobacterium paratuberculosis (see paper)
33% identity, 94% coverage: 10:257/265 of query aligns to 14:253/254 of 3rrvB
Query Sequence
>CCNA_02658 CCNA_02658 3-hydroxybutyryl-CoA dehydratase
MSLILTEKRGHIAILTLNRPDAMNALGAPGDGDQVAAACEAINDDQDIRCVILTGAGKAF
SAGGDVKAMKAREGAFGGNGVKVRDGYRKNIHRIVRAIYGLEVPSIAAVNGAAIGLGCDV
ACMTDIRIAADTARFGVTFLKLGLIPGDGGAWLMPRTIGMSRAAELLFTGDVIDAAKAAE
WGLISKAVPAGDLMGEALALAERIAQQPPHALRMAKSLLKHGQTASYDTLMEMSAAAQAI
AHHTEDHMEGVDAILEKRSPVFKGA
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