SitesBLAST
Comparing AZOBR_RS24105 AZOBR_RS24105 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)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 90% coverage: 4:234/256 of query aligns to 4:233/257 of 6slbAAA
- active site: Q64 (= Q65), F69 (≠ T70), L80 (≠ V82), N84 (≠ E86), A108 (≠ S110), S111 (≠ Q113), A130 (≠ P132), F131 (≠ E133), L136 (≠ I138), P138 (≠ S140), D139 (≠ T141), A224 (= A225)
- 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 (= R59), A62 (= A63), Q64 (= Q65), D65 (= D66), L66 (= L67), Y76 (≠ R77), A108 (≠ S110), F131 (≠ E133), D139 (≠ T141)
Sites not aligning to the query:
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 90% coverage: 4:234/256 of query aligns to 1:221/245 of 6slaAAA
- active site: Q61 (= Q65), L68 (≠ V82), N72 (≠ E86), A96 (≠ S110), S99 (≠ Q113), A118 (≠ P132), F119 (≠ E133), L124 (≠ I138), P126 (≠ S140), N127 (≠ T141), A212 (= A225)
- 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 (= L24), A59 (= A63), Q61 (= Q65), D62 (= D66), L63 (= L67), L68 (≠ V82), Y71 (≠ W85), A94 (= A108), G95 (= G109), A96 (≠ S110), F119 (≠ E133), I122 (≠ S136), L124 (≠ I138), N127 (≠ T141)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 100% coverage: 1:256/256 of query aligns to 2:255/255 of 3q0jC
- active site: A65 (≠ Q65), M70 (≠ T70), T80 (≠ V82), F84 (≠ E86), G108 (≠ S110), E111 (≠ Q113), P130 (= P132), E131 (= E133), V136 (≠ I138), P138 (≠ A139), G139 (≠ S140), L224 (≠ A225), F234 (≠ Y235)
- binding acetoacetyl-coenzyme a: Q23 (≠ E22), A24 (≠ I23), L25 (= L24), A27 (= A26), A63 (= A63), G64 (= G64), A65 (≠ Q65), D66 (= D66), I67 (≠ L67), K68 (≠ N68), M70 (≠ T70), F84 (≠ E86), G107 (= G109), G108 (≠ S110), E111 (≠ Q113), P130 (= P132), E131 (= E133), P138 (≠ A139), G139 (≠ S140), M140 (≠ T141)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 100% coverage: 1:256/256 of query aligns to 2:255/255 of 3q0gC
- active site: A65 (≠ Q65), M70 (≠ T70), T80 (≠ V82), F84 (≠ E86), G108 (≠ S110), E111 (≠ Q113), P130 (= P132), E131 (= E133), V136 (≠ I138), P138 (≠ A139), G139 (≠ S140), L224 (≠ A225), F234 (≠ Y235)
- binding coenzyme a: L25 (= L24), A63 (= A63), I67 (≠ L67), K68 (≠ N68), Y104 (≠ V106), P130 (= P132), E131 (= E133), L134 (≠ S136)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 100% coverage: 1:256/256 of query aligns to 1:254/256 of 3h81A
- active site: A64 (≠ Q65), M69 (≠ T70), T79 (≠ V82), F83 (≠ E86), G107 (≠ S110), E110 (≠ Q113), P129 (= P132), E130 (= E133), V135 (≠ I138), P137 (≠ A139), G138 (≠ S140), L223 (≠ A225), F233 (≠ Y235)
- binding calcium ion: F233 (≠ Y235), Q238 (≠ P240)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 100% coverage: 1:256/256 of query aligns to 1:250/250 of 3q0gD
- active site: A64 (≠ Q65), M69 (vs. gap), T75 (≠ N74), F79 (≠ V82), G103 (≠ S110), E106 (≠ Q113), P125 (= P132), E126 (= E133), V131 (≠ I138), P133 (≠ A139), G134 (≠ S140), L219 (≠ A225), F229 (≠ Y235)
- binding Butyryl Coenzyme A: F225 (≠ Q231), F241 (= F247)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
31% identity, 98% coverage: 2:251/256 of query aligns to 3:252/259 of 5zaiC
- active site: A65 (≠ Q65), F70 (≠ T70), S82 (≠ V82), R86 (≠ E86), G110 (≠ S110), E113 (≠ Q113), P132 (= P132), E133 (= E133), I138 (= I138), P140 (≠ A139), G141 (≠ S140), A226 (≠ R229), F236 (≠ Y235)
- binding coenzyme a: K24 (≠ I23), L25 (= L24), A63 (= A63), G64 (= G64), A65 (≠ Q65), D66 (= D66), I67 (≠ L67), P132 (= P132), R166 (≠ L165), F248 (= F247), K251 (= K250)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 98% coverage: 2:253/256 of query aligns to 3:255/260 of 2hw5C
- active site: A68 (≠ Q65), M73 (≠ T70), S83 (≠ A78), L87 (≠ V82), G111 (≠ S110), E114 (≠ Q113), P133 (= P132), E134 (= E133), T139 (vs. gap), P141 (≠ A139), G142 (≠ S140), K227 (≠ R229), F237 (≠ Y235)
- binding crotonyl coenzyme a: K26 (≠ E22), A27 (≠ I23), L28 (= L24), A30 (= A26), K62 (≠ R59), I70 (≠ L67), F109 (≠ A108)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
30% identity, 98% coverage: 2:253/256 of query aligns to 1:253/258 of 1ey3A
- active site: A66 (≠ Q65), M71 (vs. gap), S81 (≠ A78), L85 (≠ V82), G109 (≠ S110), E112 (≠ Q113), P131 (= P132), E132 (= E133), T137 (vs. gap), P139 (≠ A139), G140 (≠ S140), K225 (≠ R229), F235 (≠ Y235)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E22), L26 (= L24), A28 (= A26), A64 (= A63), G65 (= G64), A66 (≠ Q65), D67 (= D66), I68 (≠ L67), L85 (≠ V82), W88 (= W85), G109 (≠ S110), P131 (= P132), L135 (≠ S136), G140 (≠ S140)
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)
30% identity, 98% coverage: 2:253/256 of query aligns to 33:285/290 of P14604
- E144 (≠ Q113) 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
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
30% identity, 98% coverage: 2:253/256 of query aligns to 3:255/260 of 1dubA
- active site: A68 (≠ Q65), M73 (vs. gap), S83 (≠ A78), L87 (≠ V82), G111 (≠ S110), E114 (≠ Q113), P133 (= P132), E134 (= E133), T139 (vs. gap), P141 (≠ A139), G142 (≠ S140), K227 (≠ R229), F237 (≠ Y235)
- binding acetoacetyl-coenzyme a: K26 (≠ E22), A27 (≠ I23), L28 (= L24), A30 (= A26), A66 (= A63), A68 (≠ Q65), D69 (= D66), I70 (≠ L67), Y107 (≠ V106), G110 (= G109), G111 (≠ S110), E114 (≠ Q113), P133 (= P132), E134 (= E133), L137 (≠ S136), G142 (≠ S140), F233 (vs. gap), F249 (= F247)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
30% identity, 98% coverage: 2:253/256 of query aligns to 3:253/258 of 1mj3A
- active site: A68 (≠ Q65), M73 (≠ T70), S83 (≠ E80), L85 (≠ V82), G109 (≠ S110), E112 (≠ Q113), P131 (= P132), E132 (= E133), T137 (vs. gap), P139 (≠ A139), G140 (≠ S140), K225 (≠ R229), F235 (≠ Y235)
- binding hexanoyl-coenzyme a: K26 (≠ E22), A27 (≠ I23), L28 (= L24), A30 (= A26), A66 (= A63), G67 (= G64), A68 (≠ Q65), D69 (= D66), I70 (≠ L67), G109 (≠ S110), P131 (= P132), E132 (= E133), L135 (≠ S136), G140 (≠ S140)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
30% identity, 98% coverage: 2:253/256 of query aligns to 2:249/254 of 2dubA
- active site: A67 (≠ Q65), M72 (vs. gap), S82 (≠ A83), G105 (≠ S110), E108 (≠ Q113), P127 (= P132), E128 (= E133), T133 (vs. gap), P135 (≠ A139), G136 (≠ S140), K221 (≠ R229), F231 (≠ Y235)
- binding octanoyl-coenzyme a: K25 (≠ E22), A26 (≠ I23), L27 (= L24), A29 (= A26), A65 (= A63), A67 (≠ Q65), D68 (= D66), I69 (≠ L67), K70 (≠ N68), G105 (≠ S110), E108 (≠ Q113), P127 (= P132), E128 (= E133), G136 (≠ S140), A137 (≠ T141)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
31% identity, 96% coverage: 7:252/256 of query aligns to 9:255/261 of 5jbxB
- active site: A67 (≠ Q65), R72 (≠ T70), L84 (≠ V82), R88 (≠ E86), G112 (≠ S110), E115 (≠ Q113), T134 (≠ P132), E135 (= E133), I140 (vs. gap), P142 (≠ A139), G143 (≠ S140), A228 (= A225), L238 (≠ Y235)
- binding coenzyme a: S24 (≠ E22), R25 (≠ I23), R26 (≠ L24), A28 (= A26), A65 (= A63), D68 (= D66), L69 (= L67), K70 (≠ N68), L110 (≠ A108), G111 (= G109), T134 (≠ P132), E135 (= E133), L138 (≠ S136), R168 (≠ L165)
Q9XB60 Carboxymethylproline synthase; Carbapenem biosynthesis protein B; EC 2.3.1.226 from Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) (see 3 papers)
27% identity, 79% coverage: 5:205/256 of query aligns to 2:203/250 of Q9XB60
- AGGDF 60:64 (≠ AGQDL 63:67) binding
- W79 (= W81) mutation to A: Forms the C6 epimers of 6-methyl-t-CMP in 16:84 ratio of (6R):(6S) epimers.; mutation to F: Forms the C6 epimers of 6-methyl-t-CMP in 17:83 ratio of (6R):(6S) epimers.
- M108 (≠ S110) mutation to A: Forms the C6 epimers of 6-methyl-t-CMP in 45:55 ratio of (6R):(6S) epimers.; mutation to I: Forms the C6 epimers of 6-methyl-t-CMP in 92:8 ratio of (6R):(6S) epimers.; mutation to L: Forms the C6 epimers of 6-methyl-t-CMP in 47:53 ratio of (6R):(6S) epimers.; mutation to V: Forms the C6 epimers of 6-methyl-t-CMP in 95:5 ratio of (6R):(6S) epimers.
- Q111 (= Q113) mutation to N: Forms the C6 epimers of 6-methyl-t-CMP in 75:25 ratio of (6R):(6S) epimers.
- E131 (= E133) Important for catalytic activity; mutation E->A,Q: Does not catalyze production of (2S,5S)-5-carboxymethylproline but catalyzes decarboxylation of malonyl-CoA to methylmalonyl-CoA.; mutation to D: Catalyzes production of (2S,5S)-5-carboxymethylproline and decarboxylation of malonyl-CoA to methylmalonyl-CoA, but with much lower specific activity for decarboxylation.
Sites not aligning to the query:
- 229 H→A: Forms the C6 epimers of 6-methyl-t-CMP in 70:30 ratio of (6R):(6S) epimers.
2a81A Carboxymethylproline synthase (carb) from pectobacterium carotovora, complexed with acetyl coa and bicine (see paper)
27% identity, 79% coverage: 5:205/256 of query aligns to 2:203/235 of 2a81A
- active site: G62 (≠ Q65), V67 (≠ T70), I80 (≠ V82), I84 (≠ E86), M108 (≠ S110), Q111 (= Q113), E131 (= E133), G137 (≠ A139), C138 (≠ S140), S139 (≠ T141)
- binding acetyl coenzyme *a: N19 (≠ E22), P23 (≠ A26), G62 (≠ Q65), D63 (= D66), F64 (≠ L67)
Sites not aligning to the query:
Q5LLW6 Methylthioacryloyl-CoA hydratase; EC 4.2.1.155 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
30% identity, 90% coverage: 13:243/256 of query aligns to 21:263/267 of Q5LLW6
- K31 (≠ I23) binding
- R32 (≠ L24) binding
- A69 (= A63) binding
- L71 (≠ Q65) binding
- L73 (= L67) binding
- G118 (≠ S110) binding
- E121 (≠ Q113) active site, Nucleophile; mutation to A: Abolishes catalytic activity.
- E141 (= E133) active site, Proton acceptor; mutation to A: Abolishes catalytic activity.
- R144 (≠ S136) binding
- G149 (≠ T141) binding
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
29% identity, 96% coverage: 6:252/256 of query aligns to 11:260/266 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, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ N135) 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)
32% identity, 84% coverage: 3:218/256 of query aligns to 1:201/224 of 3p85A
- active site: L62 (≠ Q65), L67 (≠ T70), P68 (≠ K71), G92 (≠ S110), E95 (≠ Q113), T114 (≠ P132), H115 (≠ E133), L120 (≠ I138), P122 (≠ S140), T123 (= T141)
- binding calcium ion: D43 (≠ Q45), D45 (≠ G47)
Sites not aligning to the query:
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)
32% identity, 75% coverage: 15:207/256 of query aligns to 23:215/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
Query Sequence
>AZOBR_RS24105 AZOBR_RS24105 enoyl-CoA hydratase
VFKFILTEVRGPVGIITLNRPEILNAWNAAMRDELVVAFDQFENQDGVRAIILTGAGDRA
FGAGQDLNETKTFNADRAEEWVAEWERLYHRMRTLSKPLIIALNGVAAGSAFQVALLGDF
RIGHAGVRMGQPEINSGIASTTGPWIMKEMIGLARTMDLTLSGRLMDAEESHRIGLINRI
VPQDRVMAESLALAEELAAKPPVAMRLDKQRFREMTEAGFRDALAAGVRIQREAYASGEP
ARMMEEFLAKRAAKRT
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