SitesBLAST
Comparing AZOBR_RS18155 AZOBR_RS18155 enoyl-CoA hydratase 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
40% identity, 100% coverage: 2:248/248 of query aligns to 11:259/259 of 5zaiC
- active site: A65 (≠ S57), F70 (≠ L62), S82 (≠ R72), R86 (≠ E75), G110 (= G99), E113 (= E102), P132 (= P121), E133 (= E122), I138 (≠ W127), P140 (≠ G129), G141 (= G130), A226 (≠ E215), F236 (= F225)
- binding coenzyme a: K24 (= K15), L25 (= L16), A63 (≠ C55), G64 (= G56), A65 (≠ S57), D66 (= D58), I67 (= I59), P132 (= P121), R166 (≠ P155), F248 (= F237), K251 (= K240)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
41% identity, 100% coverage: 2:248/248 of query aligns to 10:256/256 of 3h81A
- active site: A64 (≠ S57), M69 (≠ L62), T79 (≠ R72), F83 (≠ C78), G107 (= G99), E110 (= E102), P129 (= P121), E130 (= E122), V135 (≠ W127), P137 (≠ G129), G138 (= G130), L223 (≠ E215), F233 (= F225)
- binding calcium ion: F233 (= F225), Q238 (≠ A230)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
41% identity, 98% coverage: 2:245/248 of query aligns to 11:254/255 of 3q0jC
- active site: A65 (≠ S57), M70 (≠ L62), T80 (≠ R72), F84 (≠ C78), G108 (= G99), E111 (= E102), P130 (= P121), E131 (= E122), V136 (≠ W127), P138 (≠ G129), G139 (= G130), L224 (≠ E215), F234 (= F225)
- binding acetoacetyl-coenzyme a: Q23 (= Q14), A24 (≠ K15), L25 (= L16), A27 (= A18), A63 (≠ C55), G64 (= G56), A65 (≠ S57), D66 (= D58), I67 (= I59), K68 (≠ R60), M70 (≠ L62), F84 (≠ C78), G107 (= G98), G108 (= G99), E111 (= E102), P130 (= P121), E131 (= E122), P138 (≠ G129), G139 (= G130), M140 (≠ G131)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
41% identity, 98% coverage: 2:245/248 of query aligns to 11:254/255 of 3q0gC
- active site: A65 (≠ S57), M70 (≠ L62), T80 (≠ R72), F84 (≠ C78), G108 (= G99), E111 (= E102), P130 (= P121), E131 (= E122), V136 (≠ W127), P138 (≠ G129), G139 (= G130), L224 (≠ E215), F234 (= F225)
- binding coenzyme a: L25 (= L16), A63 (≠ C55), I67 (= I59), K68 (≠ R60), Y104 (= Y95), P130 (= P121), E131 (= E122), L134 (= L125)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
42% identity, 98% coverage: 2:245/248 of query aligns to 10:249/250 of 3q0gD
- active site: A64 (≠ S57), M69 (≠ L62), T75 (= T67), F79 (= F71), G103 (= G99), E106 (= E102), P125 (= P121), E126 (= E122), V131 (≠ W127), P133 (≠ G129), G134 (= G130), L219 (≠ E215), F229 (= F225)
- binding Butyryl Coenzyme A: F225 (≠ Q221), F241 (= F237)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
41% identity, 98% coverage: 5:246/248 of query aligns to 16:252/254 of 2dubA
- active site: A67 (≠ S57), M72 (≠ L62), S82 (≠ D76), G105 (= G99), E108 (= E102), P127 (= P121), E128 (= E122), T133 (≠ W127), P135 (≠ G129), G136 (= G130), K221 (≠ E215), F231 (= F225)
- binding octanoyl-coenzyme a: K25 (≠ Q14), A26 (≠ K15), L27 (= L16), A29 (= A18), A65 (≠ C55), A67 (≠ S57), D68 (= D58), I69 (= I59), K70 (≠ R60), G105 (= G99), E108 (= E102), P127 (= P121), E128 (= E122), G136 (= G130), A137 (≠ G131)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
41% identity, 98% coverage: 5:246/248 of query aligns to 17:256/258 of 1mj3A
- active site: A68 (≠ S57), M73 (≠ L62), S83 (≠ N73), L85 (≠ E75), G109 (= G99), E112 (= E102), P131 (= P121), E132 (= E122), T137 (≠ W127), P139 (≠ G129), G140 (= G130), K225 (≠ E215), F235 (= F225)
- binding hexanoyl-coenzyme a: K26 (≠ Q14), A27 (≠ K15), L28 (= L16), A30 (= A18), A66 (≠ C55), G67 (= G56), A68 (≠ S57), D69 (= D58), I70 (= I59), G109 (= G99), P131 (= P121), E132 (= E122), L135 (= L125), G140 (= G130)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
40% identity, 98% coverage: 5:246/248 of query aligns to 15:256/258 of 1ey3A
- active site: A66 (≠ S57), M71 (≠ L62), S81 (≠ R72), L85 (≠ E75), G109 (= G99), E112 (= E102), P131 (= P121), E132 (= E122), T137 (≠ W127), P139 (≠ G129), G140 (= G130), K225 (≠ E215), F235 (= F225)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ Q14), L26 (= L16), A28 (= A18), A64 (≠ C55), G65 (= G56), A66 (≠ S57), D67 (= D58), I68 (= I59), L85 (≠ E75), W88 (≠ C78), G109 (= G99), P131 (= P121), L135 (= L125), G140 (= G130)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
40% identity, 98% coverage: 5:246/248 of query aligns to 17:258/260 of 1dubA
- active site: A68 (≠ S57), M73 (≠ L62), S83 (≠ R72), L87 (≠ E75), G111 (= G99), E114 (= E102), P133 (= P121), E134 (= E122), T139 (≠ W127), P141 (≠ G129), G142 (= G130), K227 (≠ E215), F237 (= F225)
- binding acetoacetyl-coenzyme a: K26 (≠ Q14), A27 (≠ K15), L28 (= L16), A30 (= A18), A66 (≠ C55), A68 (≠ S57), D69 (= D58), I70 (= I59), Y107 (= Y95), G110 (= G98), G111 (= G99), E114 (= E102), P133 (= P121), E134 (= E122), L137 (= L125), G142 (= G130), F233 (≠ Q221), F249 (= F237)
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)
40% identity, 98% coverage: 5:246/248 of query aligns to 47:288/290 of P14604
- E144 (= E102) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E122) 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
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
40% identity, 98% coverage: 5:246/248 of query aligns to 17:258/260 of 2hw5C
- active site: A68 (≠ S57), M73 (≠ L62), S83 (≠ R72), L87 (≠ E75), G111 (= G99), E114 (= E102), P133 (= P121), E134 (= E122), T139 (≠ W127), P141 (≠ G129), G142 (= G130), K227 (≠ E215), F237 (= F225)
- binding crotonyl coenzyme a: K26 (≠ Q14), A27 (≠ K15), L28 (= L16), A30 (= A18), K62 (≠ R51), I70 (= I59), F109 (= F97)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 99% coverage: 2:246/248 of query aligns to 11:255/257 of 6slbAAA
- active site: Q64 (≠ S57), F69 (≠ L62), L80 (≠ F71), N84 (≠ E75), A108 (≠ G99), S111 (≠ E102), A130 (≠ P121), F131 (≠ E122), L136 (≠ W127), P138 (≠ G129), D139 (≠ G130), A224 (≠ E215), G234 (≠ F225)
- 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 (= R51), A62 (≠ C55), Q64 (≠ S57), D65 (= D58), L66 (≠ I59), Y76 (≠ T67), A108 (≠ G99), F131 (≠ E122), D139 (≠ G130)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 99% coverage: 2:246/248 of query aligns to 8:243/245 of 6slaAAA
- active site: Q61 (≠ S57), L68 (≠ F71), N72 (≠ E75), A96 (≠ G99), S99 (≠ E102), A118 (≠ P121), F119 (≠ E122), L124 (≠ W127), P126 (≠ G129), N127 (≠ G130), A212 (≠ E215), G222 (≠ F225)
- 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 (= L16), A59 (≠ C55), Q61 (≠ S57), D62 (= D58), L63 (≠ I59), L68 (≠ F71), Y71 (≠ R74), A94 (≠ F97), G95 (= G98), A96 (≠ G99), F119 (≠ E122), I122 (≠ L125), L124 (≠ W127), N127 (≠ G130), F234 (= F237), K237 (= K240)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
37% identity, 96% coverage: 9:246/248 of query aligns to 19:259/261 of 5jbxB
- active site: A67 (≠ S57), R72 (= R64), L84 (≠ I81), R88 (= R85), G112 (= G99), E115 (= E102), T134 (≠ P121), E135 (= E122), I140 (≠ W127), P142 (≠ G129), G143 (= G130), A228 (≠ E215), L238 (≠ F225)
- binding coenzyme a: S24 (≠ Q14), R25 (≠ K15), R26 (≠ L16), A28 (= A18), A65 (≠ C55), D68 (= D58), L69 (≠ I59), K70 (≠ R60), L110 (≠ F97), G111 (= G98), T134 (≠ P121), E135 (= E122), L138 (= L125), R168 (≠ P155)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
35% identity, 99% coverage: 3:248/248 of query aligns to 16:266/266 of O53561
- K135 (≠ Q117) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 117:124, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K124) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
41% identity, 74% coverage: 5:187/248 of query aligns to 11:180/224 of 3p85A
- active site: L62 (≠ S57), L67 (= L62), P68 (≠ D63), G92 (= G99), E95 (= E102), T114 (≠ P121), H115 (≠ E122), L120 (≠ W127), P122 (≠ G129), T123 (≠ G130)
- binding calcium ion: D43 (= D37), D45 (= D39)
Sites not aligning to the query:
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
32% identity, 98% coverage: 5:247/248 of query aligns to 30:276/281 of 3t88A
- active site: G82 (≠ S57), R87 (≠ L62), Y93 (vs. gap), H101 (≠ F71), L105 (≠ E75), G129 (= G99), V132 (≠ E102), G152 (≠ E122), S157 (≠ W127), D159 (≠ G129), G160 (= G130), A246 (≠ E217), Y254 (≠ F225)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (= Q14), V40 (≠ K15), R41 (≠ L16), A43 (= A18), S80 (≠ C55), G81 (= G56), G82 (≠ S57), D83 (= D58), Q84 (≠ I59), K85 (≠ R60), Y93 (vs. gap), V104 (≠ R74), L105 (≠ E75), Y125 (= Y95), G129 (= G99), T151 (≠ P121), V155 (≠ L125), F158 (≠ I128), D159 (≠ G129), T250 (≠ Q221), Y254 (≠ F225), F266 (= F237), K269 (= K240)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
32% identity, 98% coverage: 5:247/248 of query aligns to 34:280/285 of 4i42A
- active site: G86 (≠ S57), R91 (≠ L62), Y97 (vs. gap), H105 (≠ F71), L109 (≠ E75), G133 (= G99), V136 (≠ E102), G156 (≠ E122), S161 (≠ W127), D163 (≠ G129), G164 (= G130), A250 (≠ E217), Y258 (≠ F225)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K15), R45 (≠ L16), S84 (≠ C55), G85 (= G56), G86 (≠ S57), D87 (= D58), Q88 (≠ I59), K89 (≠ R60), Y97 (vs. gap), V108 (≠ R74), Y129 (= Y95), G133 (= G99), T155 (≠ P121), S161 (≠ W127), T254 (≠ Q221), F270 (= F237), K273 (= K240)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 98% coverage: 5:247/248 of query aligns to 34:280/285 of P0ABU0
- R45 (≠ L16) binding in other chain
- SGGDQK 84:89 (≠ CGSDIR 55:60) binding in other chain
- K89 (≠ R60) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ L62) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (vs. gap) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ YAFGG 95:99) binding in other chain
- Q154 (≠ A120) 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 (≠ APE 120:122) binding
- T155 (≠ P121) binding in other chain
- G156 (≠ E122) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ W127) binding in other chain
- W184 (≠ I150) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ F225) binding
- R267 (= R234) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F237) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K240) binding ; mutation to A: Impairs protein folding.
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
33% identity, 97% coverage: 5:245/248 of query aligns to 18:253/260 of 2uzfA
- active site: G70 (≠ S57), R80 (≠ T67), L84 (≠ E75), G108 (= G99), V111 (≠ E102), T130 (≠ P121), G131 (≠ E122), S136 (≠ W127), D138 (≠ G129), A139 (≠ G130), A225 (≠ E217), Y233 (≠ F225)
- binding acetoacetyl-coenzyme a: V28 (≠ K15), R29 (≠ L16), S68 (≠ C55), G69 (= G56), G70 (≠ S57), D71 (= D58), Y104 (= Y95), G108 (= G99)
Query Sequence
>AZOBR_RS18155 AZOBR_RS18155 enoyl-CoA hydratase
VDGFVATITLDRPQKLNAVTPEMAAQLVAAVARCNADDDIRCVVLTGAGPRAFCCGSDIR
ELDRYDTAWNFRNREDYCDAIRGLRKPSIAAVNGYAFGGGLETAMSCDIRIASENAQFGA
PEIKLGWIGGGGVAAFLSHSIGTSNAAMMILTGDPIPADKALAWGLVSEVVPADRLLARA
QEIAAIVASRAPIAAETAKLNLKAAHTMPVEKAIEYERDLQTICFATADAAEGRAAFKEK
RSPVFRRK
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