SitesBLAST
Comparing GFF55 HP15_55 enoyl-CoA hydratase/isomerase 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, 96% coverage: 8:263/266 of query aligns to 8:254/257 of 6slbAAA
- active site: Q64 (≠ G65), F69 (≠ M70), L80 (≠ R89), N84 (≠ Q93), A108 (= A117), S111 (≠ D120), A130 (≠ S139), F131 (= F140), L136 (≠ I145), P138 (= P147), D139 (≠ G148), A224 (≠ E233), G234 (≠ H243)
- 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 (≠ K59), A62 (= A63), Q64 (≠ G65), D65 (≠ N66), L66 (≠ I67), Y76 (≠ F77), A108 (= A117), F131 (= F140), D139 (≠ G148)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 96% coverage: 8:263/266 of query aligns to 5:242/245 of 6slaAAA
- active site: Q61 (≠ Y82), L68 (≠ R89), N72 (≠ Q93), A96 (= A117), S99 (≠ D120), A118 (≠ S139), F119 (= F140), L124 (≠ I145), P126 (= P147), N127 (≠ G148), A212 (≠ E233), G222 (≠ H243)
- 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 (≠ H24), A59 (= A63), Q61 (≠ Y82), D62 (= D83), L63 (= L84), L68 (≠ R89), Y71 (≠ I92), A94 (≠ I115), G95 (= G116), A96 (= A117), F119 (= F140), I122 (≠ L143), L124 (≠ I145), N127 (≠ G148), F234 (= F255), K237 (= K258)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
37% identity, 96% coverage: 12:266/266 of query aligns to 16:260/260 of 2hw5C
- active site: A68 (≠ G65), M73 (= M70), S83 (≠ R89), L87 (≠ Q93), G111 (≠ A117), E114 (≠ D120), P133 (≠ S139), E134 (≠ F140), T139 (≠ I145), P141 (= P147), G142 (= G148), K227 (≠ L231), F237 (≠ L241)
- binding crotonyl coenzyme a: K26 (≠ E22), A27 (≠ T23), L28 (≠ H24), A30 (= A26), K62 (= K59), I70 (= I67), F109 (≠ I115)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
34% identity, 98% coverage: 5:266/266 of query aligns to 6:259/259 of 5zaiC
- active site: A65 (≠ G65), F70 (≠ M70), S82 (≠ Y88), R86 (≠ Q93), G110 (≠ A117), E113 (≠ D120), P132 (≠ S139), E133 (≠ F140), I138 (= I145), P140 (= P147), G141 (= G148), A226 (≠ E233), F236 (≠ H243)
- binding coenzyme a: K24 (≠ T23), L25 (≠ H24), A63 (= A63), G64 (= G64), A65 (≠ G65), D66 (≠ N66), I67 (= I67), P132 (≠ S139), R166 (≠ T173), F248 (= F255), K251 (= K258)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 97% coverage: 7:263/266 of query aligns to 8:254/255 of 3q0jC
- active site: A65 (≠ G65), M70 (= M70), T80 (≠ R89), F84 (≠ Q93), G108 (≠ A117), E111 (≠ D120), P130 (≠ S139), E131 (≠ F140), V136 (≠ I145), P138 (= P147), G139 (= G148), L224 (≠ A237), F234 (vs. gap)
- binding acetoacetyl-coenzyme a: Q23 (≠ E22), A24 (≠ T23), L25 (≠ H24), A27 (= A26), A63 (= A63), G64 (= G64), A65 (≠ G65), D66 (≠ N66), I67 (= I67), K68 (= K68), M70 (= M70), F84 (≠ Q93), G107 (= G116), G108 (≠ A117), E111 (≠ D120), P130 (≠ S139), E131 (≠ F140), P138 (= P147), G139 (= G148), M140 (≠ D149)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 97% coverage: 7:263/266 of query aligns to 8:254/255 of 3q0gC
- active site: A65 (≠ G65), M70 (= M70), T80 (≠ R89), F84 (≠ Q93), G108 (≠ A117), E111 (≠ D120), P130 (≠ S139), E131 (≠ F140), V136 (≠ I145), P138 (= P147), G139 (= G148), L224 (≠ A237), F234 (vs. gap)
- binding coenzyme a: L25 (≠ H24), A63 (= A63), I67 (= I67), K68 (= K68), Y104 (≠ H113), P130 (≠ S139), E131 (≠ F140), L134 (= L143)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 97% coverage: 7:263/266 of query aligns to 7:253/256 of 3h81A
- active site: A64 (≠ G65), M69 (= M70), T79 (≠ R89), F83 (≠ Q93), G107 (≠ A117), E110 (≠ D120), P129 (≠ S139), E130 (≠ F140), V135 (≠ I145), P137 (= P147), G138 (= G148), L223 (≠ A237), F233 (vs. gap)
- binding calcium ion: F233 (vs. gap), Q238 (≠ H248)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 97% coverage: 7:263/266 of query aligns to 7:249/250 of 3q0gD
- active site: A64 (≠ G65), M69 (= M70), T75 (≠ R89), F79 (≠ Q93), G103 (≠ A117), E106 (≠ D120), P125 (≠ S139), E126 (≠ F140), V131 (≠ I145), P133 (= P147), G134 (= G148), L219 (≠ A237), F229 (vs. gap)
- binding Butyryl Coenzyme A: F225 (≠ H243), F241 (= F255)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 99% coverage: 3:265/266 of query aligns to 2:257/258 of 1ey3A
- active site: A66 (≠ G65), M71 (= M70), S81 (≠ R89), L85 (≠ Q93), G109 (≠ A117), E112 (≠ D120), P131 (≠ S139), E132 (≠ F140), T137 (≠ I145), P139 (= P147), G140 (= G148), K225 (≠ L231), F235 (≠ L241)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E22), L26 (≠ H24), A28 (= A26), A64 (= A63), G65 (= G64), A66 (≠ G65), D67 (≠ N66), I68 (= I67), L85 (≠ Q93), W88 (≠ P96), G109 (≠ A117), P131 (≠ S139), L135 (= L143), G140 (= G148)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 99% coverage: 3:265/266 of query aligns to 4:259/260 of 1dubA
- active site: A68 (≠ G65), M73 (= M70), S83 (≠ R89), L87 (≠ Q93), G111 (≠ A117), E114 (≠ D120), P133 (≠ S139), E134 (≠ F140), T139 (≠ I145), P141 (= P147), G142 (= G148), K227 (≠ L231), F237 (≠ L241)
- binding acetoacetyl-coenzyme a: K26 (≠ E22), A27 (≠ T23), L28 (≠ H24), A30 (= A26), A66 (= A63), A68 (≠ G65), D69 (≠ N66), I70 (= I67), Y107 (≠ H113), G110 (= G116), G111 (≠ A117), E114 (≠ D120), P133 (≠ S139), E134 (≠ F140), L137 (= L143), G142 (= G148), F233 (≠ A237), F249 (= F255)
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, 95% coverage: 12:265/266 of query aligns to 46:289/290 of P14604
- E144 (≠ D120) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F140) 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
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
35% identity, 99% coverage: 3:265/266 of query aligns to 3:253/254 of 2dubA
- active site: A67 (≠ G65), M72 (= M70), S82 (≠ R89), G105 (≠ A117), E108 (≠ D120), P127 (≠ S139), E128 (≠ F140), T133 (≠ I145), P135 (= P147), G136 (= G148), K221 (≠ L231), F231 (≠ L241)
- binding octanoyl-coenzyme a: K25 (≠ E22), A26 (≠ T23), L27 (≠ H24), A29 (= A26), A65 (= A63), A67 (≠ G65), D68 (≠ N66), I69 (= I67), K70 (= K68), G105 (≠ A117), E108 (≠ D120), P127 (≠ S139), E128 (≠ F140), G136 (= G148), A137 (≠ D149)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
35% identity, 99% coverage: 3:265/266 of query aligns to 4:257/258 of 1mj3A
- active site: A68 (≠ G65), M73 (= M70), S83 (≠ A78), L85 (vs. gap), G109 (≠ A117), E112 (≠ D120), P131 (≠ S139), E132 (≠ F140), T137 (≠ I145), P139 (= P147), G140 (= G148), K225 (≠ L231), F235 (≠ L241)
- binding hexanoyl-coenzyme a: K26 (≠ E22), A27 (≠ T23), L28 (≠ H24), A30 (= A26), A66 (= A63), G67 (= G64), A68 (≠ G65), D69 (≠ N66), I70 (= I67), G109 (≠ A117), P131 (≠ S139), E132 (≠ F140), L135 (= L143), G140 (= G148)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 99% coverage: 1:263/266 of query aligns to 4:258/261 of 5jbxB
- active site: A67 (≠ G65), R72 (≠ M70), L84 (≠ R89), R88 (≠ Q93), G112 (≠ A117), E115 (≠ D120), T134 (≠ S139), E135 (≠ F140), I140 (= I145), P142 (= P147), G143 (= G148), A228 (≠ E233), L238 (≠ H243)
- binding coenzyme a: S24 (≠ E22), R25 (≠ T23), R26 (≠ H24), A28 (= A26), A65 (= A63), D68 (≠ N66), L69 (≠ I67), K70 (= K68), L110 (≠ I115), G111 (= G116), T134 (≠ S139), E135 (≠ F140), L138 (= L143), R168 (≠ T173)
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)
33% identity, 95% coverage: 13:265/266 of query aligns to 25:270/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
33% identity, 94% coverage: 13:263/266 of query aligns to 34:278/285 of 4i42A
- active site: G86 (= G65), R91 (≠ Q74), Y97 (≠ S80), H105 (≠ K94), L109 (≠ C98), G133 (≠ A117), V136 (≠ D120), G156 (≠ F140), S161 (≠ I145), D163 (≠ P147), G164 (= G148), A250 (≠ S235), Y258 (≠ H243)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ T23), R45 (≠ H24), S84 (≠ A63), G85 (= G64), G86 (= G65), D87 (≠ N66), Q88 (= Q71), K89 (= K72), Y97 (≠ S80), V108 (≠ L97), Y129 (≠ H113), G133 (≠ A117), T155 (≠ S139), S161 (≠ I145), T254 (≠ Q239), 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)
33% identity, 94% coverage: 13:263/266 of query aligns to 34:278/285 of P0ABU0
- R45 (≠ H24) binding in other chain
- SGGD----QK 84:89 (≠ AGGNIKDMQK 63:72) binding in other chain
- K89 (= K72) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ Q74) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ S80) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ HAIGA 113:117) binding in other chain
- Q154 (≠ E138) 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 (≠ ESF 138:140) binding
- T155 (≠ S139) binding in other chain
- G156 (≠ F140) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ I145) binding in other chain
- W184 (≠ A168) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ H243) 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)
33% identity, 94% coverage: 13:263/266 of query aligns to 30:274/281 of 3t88A
- active site: G82 (= G65), R87 (≠ Q74), Y93 (≠ S80), H101 (≠ K94), L105 (≠ C98), G129 (≠ A117), V132 (≠ D120), G152 (≠ F140), S157 (≠ I145), D159 (≠ P147), G160 (= G148), A246 (≠ S235), Y254 (≠ H243)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E22), V40 (≠ T23), R41 (≠ H24), A43 (= A26), S80 (≠ A63), G81 (= G64), G82 (= G65), D83 (≠ N66), Q84 (= Q71), K85 (= K72), Y93 (≠ S80), V104 (≠ L97), L105 (≠ C98), Y125 (≠ H113), G129 (≠ A117), T151 (≠ S139), V155 (≠ L143), F158 (≠ V146), D159 (≠ P147), T250 (≠ Q239), Y254 (≠ H243), F266 (= F255), K269 (= K258)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
33% identity, 94% coverage: 13:263/266 of query aligns to 34:278/285 of Q7CQ56
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
31% identity, 97% coverage: 5:263/266 of query aligns to 15:266/273 of Q5HH38
- R34 (≠ H24) binding in other chain
- SGG---DQ 73:77 (≠ AGGNIKDM 63:70) binding in other chain
- S149 (≠ I145) binding in other chain
Query Sequence
>GFF55 HP15_55 enoyl-CoA hydratase/isomerase
MTKFLNVERLGNVAVVRMNSPETHNALTTESQINEIVDLCAEVKADKSIRAMVLTGTGKA
FCAGGNIKDMQKRQGIFAGSPYDLRDVYRNGIQKIPLCLYELDIPVIAAVNGHAIGAGLD
LACMCDIRIASNNAKFAESFVKLGIVPGDGGAWLLPRIVGIPKASLMAFTGETIGAEQAL
SWGLVEQVCAPDELDAEALGLAQRIAENPGHALRLCKRLLREGQHMRLDSLLELSAAYQS
LAHHTQDHQEAVDSFVEKRKPNFLDK
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