SitesBLAST
Comparing 3610342 Dshi_3723 Enoyl-CoA hydratase/isomerase (RefSeq) 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)
33% identity, 93% coverage: 19:267/267 of query aligns to 6:259/259 of 5zaiC
- active site: A65 (≠ G77), F70 (= F82), S82 (vs. gap), R86 (≠ S91), G110 (≠ V118), E113 (= E121), P132 (= P140), E133 (= E141), I138 (≠ Q146), P140 (= P148), G141 (= G149), A226 (≠ E234), F236 (≠ R244)
- binding coenzyme a: K24 (≠ P36), L25 (≠ M37), A63 (≠ S75), G64 (= G76), A65 (≠ G77), D66 (≠ Y78), I67 (= I79), P132 (= P140), R166 (= R174), F248 (= F256), K251 (= K259)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 87% coverage: 37:267/267 of query aligns to 24:257/257 of 6slbAAA
- active site: Q64 (≠ G77), F69 (= F82), L80 (= L93), N84 (vs. gap), A108 (≠ V118), S111 (≠ E121), A130 (≠ P140), F131 (≠ E141), L136 (≠ Q146), P138 (= P148), D139 (≠ G149), A224 (≠ E234), G234 (≠ R244)
- 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 (≠ E71), A62 (≠ S75), Q64 (≠ G77), D65 (≠ Y78), L66 (≠ I79), Y76 (≠ H89), A108 (≠ V118), F131 (≠ E141), D139 (≠ G149)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
31% identity, 86% coverage: 38:267/267 of query aligns to 27:261/261 of 5jbxB
- active site: A67 (≠ G77), R72 (≠ F82), L84 (≠ A94), R88 (≠ A98), G112 (≠ V118), E115 (= E121), T134 (≠ P140), E135 (= E141), I140 (≠ Q146), P142 (= P148), G143 (= G149), A228 (≠ E234), L238 (≠ R244)
- binding coenzyme a: A28 (≠ V39), A65 (≠ S75), D68 (≠ Y78), L69 (≠ I79), K70 (≠ H80), L110 (≠ F116), G111 (= G117), T134 (≠ P140), E135 (= E141), L138 (= L144), R168 (= R174)
Sites not aligning to the query:
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
31% identity, 87% coverage: 37:267/267 of query aligns to 21:245/245 of 6slaAAA
- active site: Q61 (≠ G77), L68 (≠ V90), N72 (≠ A94), A96 (≠ V118), S99 (≠ E121), A118 (≠ P140), F119 (≠ E141), L124 (≠ Q146), P126 (= P148), N127 (≠ G149), A212 (≠ E234), G222 (≠ R244)
- 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 (≠ M37), A59 (≠ S75), Q61 (≠ G77), D62 (= D84), L63 (≠ A85), L68 (≠ V90), Y71 (≠ L93), A94 (≠ F116), G95 (= G117), A96 (≠ V118), F119 (≠ E141), I122 (≠ L144), L124 (≠ Q146), N127 (≠ G149), F234 (= F256), K237 (= K259)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 93% coverage: 19:267/267 of query aligns to 5:256/256 of 3h81A
- active site: A64 (≠ G77), M69 (≠ F82), T79 (≠ L93), F83 (≠ V97), G107 (≠ V118), E110 (= E121), P129 (= P140), E130 (= E141), V135 (≠ Q146), P137 (= P148), G138 (= G149), L223 (≠ E234), F233 (≠ R244)
- binding calcium ion: F233 (≠ R244), Q238 (≠ F249)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 93% coverage: 19:265/267 of query aligns to 6:255/255 of 3q0jC
- active site: A65 (≠ G77), M70 (≠ F82), T80 (≠ L93), F84 (≠ V97), G108 (≠ V118), E111 (= E121), P130 (= P140), E131 (= E141), V136 (≠ Q146), P138 (= P148), G139 (= G149), L224 (≠ E234), F234 (≠ R244)
- binding acetoacetyl-coenzyme a: Q23 (≠ A35), A24 (≠ P36), L25 (≠ M37), A27 (≠ V39), A63 (≠ S75), G64 (= G76), A65 (≠ G77), D66 (≠ Y78), I67 (= I79), K68 (≠ H80), M70 (≠ F82), F84 (≠ V97), G107 (= G117), G108 (≠ V118), E111 (= E121), P130 (= P140), E131 (= E141), P138 (= P148), G139 (= G149), M140 (≠ S150)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 93% coverage: 19:265/267 of query aligns to 6:255/255 of 3q0gC
- active site: A65 (≠ G77), M70 (≠ F82), T80 (≠ L93), F84 (≠ V97), G108 (≠ V118), E111 (= E121), P130 (= P140), E131 (= E141), V136 (≠ Q146), P138 (= P148), G139 (= G149), L224 (≠ E234), F234 (≠ R244)
- binding coenzyme a: L25 (≠ M37), A63 (≠ S75), I67 (= I79), K68 (≠ H80), Y104 (= Y114), P130 (= P140), E131 (= E141), L134 (= L144)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 93% coverage: 19:265/267 of query aligns to 5:250/250 of 3q0gD
- active site: A64 (≠ G77), M69 (≠ G81), T75 (≠ L93), F79 (≠ V97), G103 (≠ V118), E106 (= E121), P125 (= P140), E126 (= E141), V131 (≠ Q146), P133 (= P148), G134 (= G149), L219 (≠ E234), F229 (≠ R244)
- binding Butyryl Coenzyme A: F225 (≠ Y240), F241 (= F256)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 89% coverage: 28:264/267 of query aligns to 18:257/260 of 2hw5C
- active site: A68 (≠ G77), M73 (≠ F82), S83 (vs. gap), L87 (vs. gap), G111 (≠ V118), E114 (= E121), P133 (= P140), E134 (= E141), T139 (≠ Q146), P141 (= P148), G142 (= G149), K227 (≠ E234), F237 (≠ R244)
- binding crotonyl coenzyme a: K26 (≠ A35), A27 (≠ P36), L28 (≠ M37), A30 (≠ V39), K62 (≠ E71), I70 (= I79), F109 (= F116)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
30% identity, 82% coverage: 45:264/267 of query aligns to 41:278/285 of Q7CQ56
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
30% identity, 89% coverage: 28:264/267 of query aligns to 17:251/254 of 2dubA
- active site: A67 (≠ G77), M72 (≠ F82), S82 (≠ H92), G105 (≠ V118), E108 (= E121), P127 (= P140), E128 (= E141), T133 (≠ Q146), P135 (= P148), G136 (= G149), K221 (≠ E234), F231 (≠ R244)
- binding octanoyl-coenzyme a: K25 (≠ A35), A26 (≠ P36), L27 (≠ M37), A29 (≠ V39), A65 (≠ S75), A67 (≠ G77), D68 (≠ Y78), I69 (= I79), K70 (≠ H80), G105 (≠ V118), E108 (= E121), P127 (= P140), E128 (= E141), G136 (= G149), A137 (≠ S150)
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, 89% coverage: 28:264/267 of query aligns to 48:287/290 of P14604
- E144 (= E121) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E141) 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)
32% identity, 89% coverage: 28:264/267 of query aligns to 18:257/260 of 1dubA
- active site: A68 (≠ G77), M73 (vs. gap), S83 (= S86), L87 (≠ V90), G111 (≠ V118), E114 (= E121), P133 (= P140), E134 (= E141), T139 (≠ Q146), P141 (= P148), G142 (= G149), K227 (≠ E234), F237 (≠ R244)
- binding acetoacetyl-coenzyme a: K26 (≠ A35), A27 (≠ P36), L28 (≠ M37), A30 (≠ V39), A66 (≠ S75), A68 (≠ G77), D69 (≠ Y78), I70 (= I79), Y107 (= Y114), G110 (= G117), G111 (≠ V118), E114 (= E121), P133 (= P140), E134 (= E141), L137 (= L144), G142 (= G149), F233 (≠ Y240), F249 (= F256)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
32% identity, 89% coverage: 28:264/267 of query aligns to 16:255/258 of 1ey3A
- active site: A66 (≠ G77), M71 (vs. gap), S81 (= S86), L85 (≠ V90), G109 (≠ V118), E112 (= E121), P131 (= P140), E132 (= E141), T137 (≠ Q146), P139 (= P148), G140 (= G149), K225 (≠ E234), F235 (≠ R244)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A35), L26 (≠ M37), A28 (≠ V39), A64 (≠ S75), G65 (= G76), A66 (≠ G77), D67 (≠ Y78), I68 (= I79), L85 (≠ V90), W88 (≠ L93), G109 (≠ V118), P131 (= P140), L135 (= L144), G140 (= G149)
Q13825 Methylglutaconyl-CoA hydratase, mitochondrial; 3-MG-CoA hydratase; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding protein/enoyl-CoA hydratase; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56 from Homo sapiens (Human) (see 4 papers)
32% identity, 94% coverage: 15:266/267 of query aligns to 75:338/339 of Q13825
- K105 (≠ M42) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 42:56, 27% identical) RNA-binding
- K109 (≠ D46) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ A50) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ S172) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 89% coverage: 28:264/267 of query aligns to 18:255/258 of 1mj3A
- active site: A68 (≠ G77), M73 (vs. gap), S83 (≠ P87), L85 (vs. gap), G109 (≠ V118), E112 (= E121), P131 (= P140), E132 (= E141), T137 (≠ Q146), P139 (= P148), G140 (= G149), K225 (≠ E234), F235 (≠ R244)
- binding hexanoyl-coenzyme a: K26 (≠ A35), A27 (≠ P36), L28 (≠ M37), A30 (≠ V39), A66 (≠ S75), G67 (= G76), A68 (≠ G77), D69 (≠ Y78), I70 (= I79), G109 (≠ V118), P131 (= P140), E132 (= E141), L135 (= L144), G140 (= G149)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
30% identity, 82% coverage: 45:264/267 of query aligns to 37:259/266 of 3h02A
- active site: G82 (= G77), H86 (≠ V90), L90 (≠ A94), G114 (≠ V118), V117 (≠ E121), G137 (≠ E141), S142 (≠ Q146), D144 (≠ P148), G145 (= G149), A231 (≠ E236), Y239 (≠ R244)
- binding bicarbonate ion: G113 (= G117), Q135 (≠ L139), G137 (≠ E141), W165 (≠ V169)
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)
29% identity, 85% coverage: 38:264/267 of query aligns to 33:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
29% identity, 83% coverage: 44:264/267 of query aligns to 40:278/285 of 4i42A
- active site: G86 (= G77), R91 (vs. gap), Y97 (≠ F82), H105 (≠ V90), L109 (≠ A94), G133 (≠ V118), V136 (≠ E121), G156 (≠ E141), S161 (≠ Q146), D163 (≠ P148), G164 (= G149), A250 (≠ E236), Y258 (≠ R244)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ L48), R45 (= R49), S84 (= S75), G85 (= G76), G86 (= G77), D87 (≠ Y78), Q88 (vs. gap), K89 (vs. gap), Y97 (≠ F82), V108 (≠ L93), Y129 (= Y114), G133 (≠ V118), T155 (≠ P140), S161 (≠ Q146), T254 (≠ Y240), F270 (= F256), K273 (= K259)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
29% identity, 83% coverage: 44:264/267 of query aligns to 40:278/285 of P0ABU0
- R45 (= R49) binding in other chain
- SGGDQK 84:89 (≠ SGGY-- 75:78) binding in other chain
- K89 (vs. gap) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (vs. gap) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ F82) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ YTFGV 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 (≠ LPE 139:141) binding
- T155 (≠ P140) binding in other chain
- G156 (≠ E141) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ Q146) binding in other chain
- W184 (≠ V169) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ R244) binding
- R267 (≠ V253) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F256) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K259) binding ; mutation to A: Impairs protein folding.
Query Sequence
>3610342 Dshi_3723 Enoyl-CoA hydratase/isomerase (RefSeq)
MTNPYSDRPLLSKLDGFRIEVDAEAERGDIVLERAPMNVISMDQRDQLRAAFEALDADDA
VRVIVLRAEGEHFSSGGYIHGFLDASPEHVSHLADNVAAPWRCAKPVIAANKGYTFGVGF
EISLACDFRIAAKSTFYALPEQKLGQIPGSGGSARLQALIGLARTKDVVMRSRRISGQQA
FDWGIAVELVEDDKLEEATAKLVNELRSFSPMAQRTAKKLLNDSENATVATGIELEGHCY
SRLRQSEDFAEGVKAFHEKRKPTFVGR
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