SitesBLAST
Comparing CA265_RS20005 CA265_RS20005 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)
46% identity, 100% coverage: 1:259/259 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (= A66), F70 (= F71), S82 (≠ A83), R86 (≠ H87), G110 (= G112), E113 (= E115), P132 (= P134), E133 (= E135), I138 (≠ L140), P140 (= P142), G141 (= G143), A226 (= A226), F236 (= F236)
- binding coenzyme a: K24 (≠ A24), L25 (= L25), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (= I68), P132 (= P134), R166 (≠ M168), F248 (= F248), K251 (= K251)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
41% identity, 93% coverage: 18:259/259 of query aligns to 19:261/261 of 5jbxB
- active site: A67 (= A66), R72 (≠ F71), L84 (≠ A83), R88 (≠ E88), G112 (= G112), E115 (= E115), T134 (≠ P134), E135 (= E135), I140 (≠ L140), P142 (= P142), G143 (= G143), A228 (= A226), L238 (≠ F236)
- binding coenzyme a: S24 (≠ K23), R25 (≠ A24), R26 (≠ L25), A28 (= A27), A65 (= A64), D68 (= D67), L69 (≠ I68), K70 (= K69), L110 (= L110), G111 (= G111), T134 (≠ P134), E135 (= E135), L138 (= L138), R168 (≠ M168)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
43% identity, 98% coverage: 3:256/259 of query aligns to 1:255/258 of 1ey3A
- active site: A66 (= A66), M71 (vs. gap), S81 (= S75), L85 (= L82), G109 (= G112), E112 (= E115), P131 (= P134), E132 (= E135), T137 (≠ L140), P139 (= P142), G140 (= G143), K225 (≠ A226), F235 (= F236)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K23), L26 (= L25), A28 (= A27), A64 (= A64), G65 (= G65), A66 (= A66), D67 (= D67), I68 (= I68), L85 (= L82), W88 (≠ R85), G109 (= G112), P131 (= P134), L135 (= L138), G140 (= G143)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
43% identity, 98% coverage: 3:256/259 of query aligns to 3:257/260 of 1dubA
- active site: A68 (= A66), M73 (vs. gap), S83 (= S75), L87 (= L82), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), T139 (≠ L140), P141 (= P142), G142 (= G143), K227 (≠ A226), F237 (= F236)
- binding acetoacetyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (= A27), A66 (= A64), A68 (= A66), D69 (= D67), I70 (= I68), Y107 (≠ F108), G110 (= G111), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), L137 (= L138), G142 (= G143), F233 (= F232), F249 (= F248)
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)
43% identity, 98% coverage: 3:256/259 of query aligns to 33:287/290 of P14604
- E144 (= E115) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E135) 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
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
43% identity, 98% coverage: 3:256/259 of query aligns to 3:255/258 of 1mj3A
- active site: A68 (= A66), M73 (vs. gap), S83 (= S75), L85 (= L82), G109 (= G112), E112 (= E115), P131 (= P134), E132 (= E135), T137 (≠ L140), P139 (= P142), G140 (= G143), K225 (≠ A226), F235 (= F236)
- binding hexanoyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (= A27), A66 (= A64), G67 (= G65), A68 (= A66), D69 (= D67), I70 (= I68), G109 (= G112), P131 (= P134), E132 (= E135), L135 (= L138), G140 (= G143)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
38% identity, 99% coverage: 1:257/259 of query aligns to 1:255/255 of 3q0jC
- active site: A65 (= A66), M70 (≠ F71), T80 (≠ Q78), F84 (≠ L82), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), V136 (≠ L140), P138 (= P142), G139 (= G143), L224 (≠ A226), F234 (= F236)
- binding acetoacetyl-coenzyme a: Q23 (≠ K23), A24 (= A24), L25 (= L25), A27 (= A27), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (= I68), K68 (= K69), M70 (≠ F71), F84 (≠ L82), G107 (= G111), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), P138 (= P142), G139 (= G143), M140 (≠ Y144)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
38% identity, 99% coverage: 1:257/259 of query aligns to 1:255/255 of 3q0gC
- active site: A65 (= A66), M70 (≠ F71), T80 (≠ Q78), F84 (≠ L82), G108 (= G112), E111 (= E115), P130 (= P134), E131 (= E135), V136 (≠ L140), P138 (= P142), G139 (= G143), L224 (≠ A226), F234 (= F236)
- binding coenzyme a: L25 (= L25), A63 (= A64), I67 (= I68), K68 (= K69), Y104 (≠ F108), P130 (= P134), E131 (= E135), L134 (= L138)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
41% identity, 98% coverage: 3:256/259 of query aligns to 2:251/254 of 2dubA
- active site: A67 (= A66), M72 (≠ F71), S82 (≠ G86), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), T133 (≠ L140), P135 (= P142), G136 (= G143), K221 (≠ A226), F231 (= F236)
- binding octanoyl-coenzyme a: K25 (= K23), A26 (= A24), L27 (= L25), A29 (= A27), A65 (= A64), A67 (= A66), D68 (= D67), I69 (= I68), K70 (= K69), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), G136 (= G143), A137 (≠ Y144)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
38% identity, 99% coverage: 3:259/259 of query aligns to 2:256/256 of 3h81A
- active site: A64 (= A66), M69 (≠ F71), T79 (≠ Q78), F83 (≠ L82), G107 (= G112), E110 (= E115), P129 (= P134), E130 (= E135), V135 (≠ L140), P137 (= P142), G138 (= G143), L223 (≠ A226), F233 (= F236)
- binding calcium ion: F233 (= F236), Q238 (≠ F241)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
38% identity, 98% coverage: 3:257/259 of query aligns to 2:250/250 of 3q0gD
- active site: A64 (= A66), M69 (≠ F71), T75 (vs. gap), F79 (≠ S75), G103 (= G112), E106 (= E115), P125 (= P134), E126 (= E135), V131 (≠ L140), P133 (= P142), G134 (= G143), L219 (≠ A226), F229 (= F236)
- binding Butyryl Coenzyme A: F225 (= F232), F241 (= F248)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
41% identity, 93% coverage: 17:256/259 of query aligns to 20:257/260 of 2hw5C
- active site: A68 (= A66), M73 (≠ F71), S83 (≠ E81), L87 (≠ R85), G111 (= G112), E114 (= E115), P133 (= P134), E134 (= E135), T139 (≠ L140), P141 (= P142), G142 (= G143), K227 (≠ E228), F237 (= F236)
- binding crotonyl coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (= A27), K62 (= K60), I70 (= I68), F109 (≠ L110)
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)
33% identity, 97% coverage: 6:256/259 of query aligns to 13:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
42% identity, 71% coverage: 12:196/259 of query aligns to 11:198/707 of 6yswA
- active site: A66 (= A66), I71 (≠ F71), A84 (= A83), Q88 (≠ H87), G112 (= G112), E115 (= E115), P136 (= P134), E137 (= E135), G145 (= G143)
- binding coenzyme a: E23 (≠ K23), M25 (≠ L25), A66 (= A66), D67 (= D67), I68 (= I68), P136 (= P134), E137 (= E135), L140 (= L138)
Sites not aligning to the query:
6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
40% identity, 71% coverage: 5:188/259 of query aligns to 859:1048/1804 of 6eqoA
Sites not aligning to the query:
- binding phosphomethylphosphonic acid adenylate ester: 456, 458, 535, 536, 537, 538, 558, 559, 560, 561, 562, 688, 714
- binding nadp nicotinamide-adenine-dinucleotide phosphate: 1261, 1265, 1379, 1400, 1403, 1404, 1405, 1424, 1425, 1429, 1444, 1492, 1493, 1497, 1514, 1517, 1713, 1730, 1731, 1774
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 98% coverage: 6:259/259 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ A66), F69 (= F71), L80 (≠ K84), N84 (≠ E88), A108 (≠ G112), S111 (≠ E115), A130 (≠ P134), F131 (≠ E135), L136 (= L140), P138 (= P142), D139 (≠ G143), A224 (= A226), G234 (≠ F236)
- 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 (≠ K60), A62 (= A64), Q64 (≠ A66), D65 (= D67), L66 (≠ I68), Y76 (≠ E80), A108 (≠ G112), F131 (≠ E135), D139 (≠ G143)
P40939 Trifunctional enzyme subunit alpha, mitochondrial; 78 kDa gastrin-binding protein; Monolysocardiolipin acyltransferase; TP-alpha; EC 2.3.1.-; EC 4.2.1.17; EC 1.1.1.211 from Homo sapiens (Human) (see 5 papers)
39% identity, 68% coverage: 10:184/259 of query aligns to 45:222/763 of P40939
Sites not aligning to the query:
- 282 V → D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- 305 I → N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- 342 L → P: in LCHAD deficiency; dbSNP:rs137852772
- 510 active site, For hydroxyacyl-coenzyme A dehydrogenase activity; E → Q: in AFLP and LCHAD deficiency; loss of long-chain-3-hydroxyacyl-CoA dehydrogenase activity; dbSNP:rs137852769
Q5LLW6 Methylthioacryloyl-CoA hydratase; EC 4.2.1.155 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
36% identity, 86% coverage: 3:224/259 of query aligns to 9:228/267 of Q5LLW6
- K31 (≠ A24) binding
- R32 (≠ L25) binding
- A69 (= A64) binding
- L71 (≠ A66) binding
- L73 (≠ I68) binding
- G118 (= G112) binding
- E121 (= E115) active site, Nucleophile; mutation to A: Abolishes catalytic activity.
- E141 (= E135) active site, Proton acceptor; mutation to A: Abolishes catalytic activity.
- R144 (≠ L138) binding
- G149 (= G143) binding
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
33% identity, 95% coverage: 12:257/259 of query aligns to 32:279/285 of 4i42A
- active site: G86 (≠ A66), R91 (≠ F71), Y97 (≠ K77), H105 (≠ R85), L109 (= L89), G133 (= G112), V136 (≠ E115), G156 (≠ E135), S161 (≠ L140), D163 (≠ P142), G164 (= G143), A250 (≠ F232), Y258 (≠ F236)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ A24), R45 (≠ L25), S84 (≠ A64), G85 (= G65), G86 (≠ A66), D87 (= D67), Q88 (≠ I68), K89 (= K69), Y97 (≠ K77), V108 (≠ E88), Y129 (≠ F108), G133 (= G112), T155 (≠ P134), S161 (≠ L140), T254 (vs. gap), F270 (= F248), K273 (= K251)
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, 95% coverage: 12:257/259 of query aligns to 32:279/285 of P0ABU0
- R45 (≠ L25) binding in other chain
- SGGDQK 84:89 (≠ AGADIK 64:69) binding in other chain
- K89 (= K69) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ F71) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ K77) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ FALGG 108:112) binding in other chain
- Q154 (≠ L133) 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 133:135) binding
- T155 (≠ P134) binding in other chain
- G156 (≠ E135) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L140) binding in other chain
- W184 (≠ I163) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ F236) binding
- R267 (≠ V245) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F248) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K251) binding ; mutation to A: Impairs protein folding.
Query Sequence
>CA265_RS20005 CA265_RS20005 enoyl-CoA hydratase
MAYQNLISEIKENILYVTINREKALNALNKDTLAELADVIAFAGRTDEVRGVILTGAGEK
AFVAGADIKEFSDYSGKQGEELAKRGHELVFNAIENSSKPFIAAINGFALGGGLELAMAC
HIRIASDNAKLGLPEVTLGLIPGYGGTQRLTQLVGKGKAIEMITTANMITATDAEKIGLV
NVVVPQADLIGKAEEMLNVIKQRAPLAISAAIKSVIASINNTNGYATEIEEFGKCFETAD
FKEGVTAFVEKRKAIFTGK
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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