SitesBLAST
Comparing AZOBR_RS15730 AZOBR_RS15730 enoyl-CoA hydratase to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
32% identity, 91% coverage: 22:264/266 of query aligns to 20:258/260 of 2hw5C
- active site: A68 (≠ G70), M73 (≠ L75), S83 (= S85), L87 (≠ H94), G111 (≠ A118), E114 (≠ P121), P133 (≠ S140), E134 (≠ Y141), T139 (≠ L146), P141 (≠ S148), G142 (≠ D149), K227 (≠ D233), F237 (≠ L243)
- binding crotonyl coenzyme a: K26 (≠ A28), A27 (≠ T29), L28 (≠ R30), A30 (≠ S32), K62 (≠ G64), I70 (≠ L72), F109 (≠ G116)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 94% coverage: 13:263/266 of query aligns to 12:263/266 of O53561
- K135 (≠ V136) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 136:143, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K143) 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)
31% identity, 93% coverage: 19:265/266 of query aligns to 34:280/285 of 4i42A
- active site: G86 (= G70), R91 (≠ K76), Y97 (≠ D82), H105 (≠ S92), L109 (≠ M96), G133 (≠ A118), V136 (≠ P121), G156 (≠ Y141), S161 (≠ L146), D163 (≠ S148), G164 (≠ D149), A250 (≠ E235), Y258 (≠ L243)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ T29), R45 (= R30), S84 (= S68), G85 (= G69), G86 (= G70), D87 (≠ N71), Q88 (≠ L72), K89 (= K73), Y97 (≠ D82), V108 (≠ A95), Y129 (≠ P114), G133 (≠ A118), T155 (≠ S140), S161 (≠ L146), T254 (≠ F239), F270 (= F255), K273 (= K258)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 93% coverage: 19:265/266 of query aligns to 34:280/285 of P0ABU0
- R45 (= R30) binding in other chain
- SGGDQK 84:89 (≠ SGGNLK 68:73) binding in other chain
- K89 (= K73) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ K76) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ D82) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ PAGGA 114:118) binding in other chain
- Q154 (≠ L139) 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 (≠ LSY 139:141) binding
- T155 (≠ S140) binding in other chain
- G156 (≠ Y141) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L146) binding in other chain
- W184 (≠ L169) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ L243) binding
- R267 (≠ V252) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F255) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K258) binding ; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
31% identity, 93% coverage: 19:265/266 of query aligns to 30:276/281 of 3t88A
- active site: G82 (= G70), R87 (≠ K76), Y93 (≠ D82), H101 (≠ S92), L105 (≠ M96), G129 (≠ A118), V132 (≠ P121), G152 (≠ Y141), S157 (≠ L146), D159 (≠ S148), G160 (≠ D149), A246 (≠ E235), Y254 (≠ L243)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ A28), V40 (≠ T29), R41 (= R30), A43 (≠ S32), S80 (= S68), G81 (= G69), G82 (= G70), D83 (≠ N71), Q84 (≠ L72), K85 (= K73), Y93 (≠ D82), V104 (≠ A95), L105 (≠ M96), Y125 (≠ P114), G129 (≠ A118), T151 (≠ S140), V155 (= V144), F158 (≠ T147), D159 (≠ S148), T250 (≠ F239), Y254 (≠ L243), F266 (= F255), K269 (= K258)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
32% identity, 91% coverage: 22:264/266 of query aligns to 20:256/258 of 1mj3A
- active site: A68 (≠ G70), M73 (≠ A78), S83 (≠ A88), L85 (≠ V90), G109 (≠ A118), E112 (≠ P121), P131 (≠ S140), E132 (≠ Y141), T137 (≠ L146), P139 (≠ S148), G140 (≠ D149), K225 (≠ D233), F235 (≠ L243)
- binding hexanoyl-coenzyme a: K26 (≠ A28), A27 (≠ T29), L28 (≠ R30), A30 (≠ S32), A66 (≠ S68), G67 (= G69), A68 (≠ G70), D69 (≠ N71), I70 (≠ L72), G109 (≠ A118), P131 (≠ S140), E132 (≠ Y141), L135 (≠ V144), G140 (≠ D149)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
32% identity, 91% coverage: 22:264/266 of query aligns to 20:258/260 of 1dubA
- active site: A68 (≠ G70), M73 (≠ L75), S83 (= S85), L87 (≠ H94), G111 (≠ A118), E114 (≠ P121), P133 (≠ S140), E134 (≠ Y141), T139 (≠ L146), P141 (≠ S148), G142 (≠ D149), K227 (≠ D233), F237 (≠ L243)
- binding acetoacetyl-coenzyme a: K26 (≠ A28), A27 (≠ T29), L28 (≠ R30), A30 (≠ S32), A66 (≠ S68), A68 (≠ G70), D69 (≠ N71), I70 (≠ L72), Y107 (≠ P114), G110 (= G117), G111 (≠ A118), E114 (≠ P121), P133 (≠ S140), E134 (≠ Y141), L137 (≠ V144), G142 (≠ D149), F233 (= F239), F249 (= F255)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
31% identity, 93% coverage: 19:265/266 of query aligns to 34:280/285 of Q7CQ56
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
32% identity, 91% coverage: 22:264/266 of query aligns to 18:256/258 of 1ey3A
- active site: A66 (≠ G70), M71 (≠ L75), S81 (= S85), L85 (≠ H94), G109 (≠ A118), E112 (≠ P121), P131 (≠ S140), E132 (≠ Y141), T137 (≠ L146), P139 (≠ S148), G140 (≠ D149), K225 (≠ D233), F235 (≠ L243)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A28), L26 (≠ R30), A28 (≠ S32), A64 (≠ S68), G65 (= G69), A66 (≠ G70), D67 (≠ N71), I68 (≠ L72), L85 (≠ H94), W88 (≠ I97), G109 (≠ A118), P131 (≠ S140), L135 (≠ V144), G140 (≠ D149)
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, 91% coverage: 22:263/266 of query aligns to 50:287/290 of P14604
- E144 (≠ P121) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ Y141) 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
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 94% coverage: 15:263/266 of query aligns to 10:254/257 of 6slbAAA
- active site: Q64 (≠ G70), F69 (≠ L75), L80 (≠ V90), N84 (≠ H94), A108 (= A118), S111 (≠ P121), A130 (≠ S140), F131 (≠ Y141), L136 (= L146), P138 (≠ S148), D139 (= D149), A224 (≠ F239), G234 (= G249)
- 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 (≠ G64), A62 (≠ S68), Q64 (≠ G70), D65 (≠ N71), L66 (= L72), Y76 (≠ V86), A108 (= A118), F131 (≠ Y141), D139 (= D149)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 91% coverage: 22:264/266 of query aligns to 19:252/254 of 2dubA
- active site: A67 (≠ G70), M72 (≠ L75), S82 (≠ A95), G105 (≠ A118), E108 (≠ P121), P127 (≠ S140), E128 (≠ Y141), T133 (≠ L146), P135 (≠ S148), G136 (≠ D149), K221 (≠ D233), F231 (≠ L243)
- binding octanoyl-coenzyme a: K25 (≠ A28), A26 (≠ T29), L27 (≠ R30), A29 (≠ S32), A65 (≠ S68), A67 (≠ G70), D68 (≠ N71), I69 (≠ L72), K70 (= K73), G105 (≠ A118), E108 (≠ P121), P127 (≠ S140), E128 (≠ Y141), G136 (≠ D149), A137 (≠ G150)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
34% identity, 93% coverage: 19:265/266 of query aligns to 23:268/273 of Q5HH38
- R34 (= R30) binding in other chain
- SGGDQ 73:77 (≠ SGGNL 68:72) binding in other chain
- S149 (≠ L146) binding in other chain
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
31% identity, 93% coverage: 19:265/266 of query aligns to 31:262/267 of 4elwA
- active site: G83 (= G70), L91 (≠ E91), G115 (≠ A118), V118 (≠ P121), G138 (≠ Y141), S143 (≠ L146), D145 (≠ S148), G146 (≠ D149), A232 (≠ E235), Y240 (≠ L243)
- binding nitrate ion: G114 (= G117), T137 (≠ S140), G138 (≠ Y141), F144 (≠ T147), W166 (≠ L169)
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
34% identity, 93% coverage: 19:265/266 of query aligns to 18:255/260 of 2uzfA
- active site: G70 (= G70), R80 (= R87), L84 (≠ E91), G108 (≠ A118), V111 (≠ P121), T130 (≠ S140), G131 (≠ Y141), S136 (≠ L146), D138 (≠ S148), A139 (≠ D149), A225 (≠ E235), Y233 (≠ L243)
- binding acetoacetyl-coenzyme a: V28 (≠ T29), R29 (= R30), S68 (= S68), G69 (= G69), G70 (= G70), D71 (≠ N71), Y104 (≠ P114), G108 (≠ A118)
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)
32% identity, 98% coverage: 6:265/266 of query aligns to 70:332/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
31% identity, 93% coverage: 19:265/266 of query aligns to 31:263/268 of 4elxA
- active site: G83 (= G70), H88 (≠ R87), L92 (≠ E91), G116 (≠ A118), V119 (≠ P121), G139 (≠ Y141), S144 (≠ L146), D146 (≠ S148), G147 (≠ D149), A233 (≠ E235), Y241 (≠ L243)
- binding chloride ion: G115 (= G117), G139 (≠ Y141), W167 (≠ L169)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
31% identity, 93% coverage: 19:265/266 of query aligns to 30:261/266 of 3h02A
- active site: G82 (= G70), H86 (≠ W74), L90 (≠ E91), G114 (≠ A118), V117 (≠ P121), G137 (≠ Y141), S142 (≠ L146), D144 (≠ S148), G145 (≠ D149), A231 (≠ E235), Y239 (≠ L243)
- binding bicarbonate ion: G113 (= G117), Q135 (≠ L139), G137 (≠ Y141), W165 (≠ L169)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 95% coverage: 13:265/266 of query aligns to 7:255/256 of 3h81A
- active site: A64 (≠ G70), M69 (≠ L75), T79 (≠ V90), F83 (≠ H94), G107 (≠ A118), E110 (≠ P121), P129 (≠ S140), E130 (≠ Y141), V135 (≠ L146), P137 (≠ S148), G138 (≠ D149), L223 (≠ D233), F233 (≠ L243)
- binding calcium ion: F233 (≠ L243), Q238 (≠ A248)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 94% coverage: 13:263/266 of query aligns to 8:254/255 of 3q0jC
- active site: A65 (≠ G70), M70 (≠ L75), T80 (≠ V90), F84 (≠ H94), G108 (≠ A118), E111 (≠ P121), P130 (≠ S140), E131 (≠ Y141), V136 (≠ L146), P138 (≠ S148), G139 (≠ D149), L224 (≠ D233), F234 (≠ L243)
- binding acetoacetyl-coenzyme a: Q23 (≠ A28), A24 (≠ T29), L25 (≠ R30), A27 (≠ S32), A63 (≠ S68), G64 (= G69), A65 (≠ G70), D66 (≠ N71), I67 (≠ L72), K68 (= K73), M70 (≠ L75), F84 (≠ H94), G107 (= G117), G108 (≠ A118), E111 (≠ P121), P130 (≠ S140), E131 (≠ Y141), P138 (≠ S148), G139 (≠ D149), M140 (≠ G150)
Query Sequence
>AZOBR_RS15730 AZOBR_RS15730 enoyl-CoA hydratase
MTDTNDKKTGLDIAQDGRVLRLTINDPATRNSIGPALMEAARAAFDAAAADPGVGAVVLT
GAEGAFCSGGNLKWLKEARGGDRESVRAGVESFHAMIRSLRACPKPVIAAVEGPAGGAGF
PLALACDLIVAAEDAVFTLSYIKVALTSDGGGTASLARALPPQLAAEILFEGGRVGAPRL
AQLGMINRLTAPGGALAEATAWAERLAAGPTAALGRAKGLLEVAYGGLADQLDRERDAFV
ESLFNDEAGEGVTAFFEKRAPVFPKG
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