SitesBLAST
Comparing CCNA_01794 CCNA_01794 enoyl-CoA hydratase/isomerase family 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)
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
44% identity, 91% coverage: 1:234/256 of query aligns to 2:223/224 of 3p85A
- active site: L62 (= L62), L67 (= L67), P68 (≠ N78), G92 (= G108), E95 (= E111), T114 (= T130), H115 (= H131), L120 (≠ I136), P122 (= P138), T123 (≠ G139), W208 (≠ F219), T219 (≠ S230)
- binding calcium ion: D43 (= D42), D45 (= D44)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
37% identity, 95% coverage: 2:243/256 of query aligns to 6:241/255 of 3q0jC
- active site: A65 (≠ L62), M70 (≠ L67), T80 (≠ A77), F84 (≠ D81), G108 (= G108), E111 (= E111), P130 (≠ T130), E131 (≠ H131), V136 (≠ I136), P138 (= P138), G139 (= G139), L224 (≠ A224), F234 (≠ T236)
- binding acetoacetyl-coenzyme a: Q23 (≠ E19), A24 (= A20), L25 (≠ M21), A27 (= A23), A63 (= A60), G64 (= G61), A65 (≠ L62), D66 (= D63), I67 (≠ L64), K68 (= K65), M70 (≠ L67), F84 (≠ D81), G107 (≠ T107), G108 (= G108), E111 (= E111), P130 (≠ T130), E131 (≠ H131), P138 (= P138), G139 (= G139), M140 (≠ W140)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 95% coverage: 2:243/256 of query aligns to 6:241/255 of 3q0gC
- active site: A65 (≠ L62), M70 (≠ L67), T80 (≠ A77), F84 (≠ D81), G108 (= G108), E111 (= E111), P130 (≠ T130), E131 (≠ H131), V136 (≠ I136), P138 (= P138), G139 (= G139), L224 (≠ A224), F234 (≠ T236)
- binding coenzyme a: L25 (≠ M21), A63 (= A60), I67 (≠ L64), K68 (= K65), Y104 (≠ V104), P130 (≠ T130), E131 (≠ H131), L134 (≠ V134)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
37% identity, 95% coverage: 2:243/256 of query aligns to 5:240/256 of 3h81A
- active site: A64 (≠ L62), M69 (≠ L67), T79 (≠ A77), F83 (≠ D81), G107 (= G108), E110 (= E111), P129 (≠ T130), E130 (≠ H131), V135 (≠ I136), P137 (= P138), G138 (= G139), L223 (≠ A224), F233 (≠ T236)
- binding calcium ion: F233 (≠ T236), Q238 (≠ R241)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 95% coverage: 2:243/256 of query aligns to 5:236/250 of 3q0gD
- active site: A64 (≠ L62), M69 (≠ L67), T75 (≠ A77), F79 (≠ D81), G103 (= G108), E106 (= E111), P125 (≠ T130), E126 (≠ H131), V131 (≠ I136), P133 (= P138), G134 (= G139), L219 (≠ A224), F229 (≠ T236)
- binding Butyryl Coenzyme A: F225 (≠ A232)
Sites not aligning to the query:
3pe8A Crystal structure of enoyl-coa hydratase from mycobacterium smegmatis (see paper)
44% identity, 91% coverage: 1:234/256 of query aligns to 3:214/219 of 3pe8A
- active site: L63 (= L62), L68 (= L67), G90 (= G108), E93 (= E111), T112 (= T130), H113 (= H131), L118 (≠ I136), P120 (= P138), T121 (≠ G139), W206 (≠ E226)
- binding zinc ion: E93 (= E111), H113 (= H131)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
36% identity, 87% coverage: 5:227/256 of query aligns to 9:229/259 of 5zaiC
- active site: A65 (≠ L62), F70 (≠ L67), S82 (≠ D79), R86 (= R83), G110 (= G108), E113 (= E111), P132 (≠ T130), E133 (≠ H131), I138 (= I136), P140 (= P138), G141 (= G139), A226 (= A224)
- binding coenzyme a: K24 (≠ A20), L25 (≠ M21), A63 (= A60), G64 (= G61), A65 (≠ L62), D66 (= D63), I67 (≠ L64), P132 (≠ T130), R166 (≠ F164)
Sites not aligning to the query:
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
40% identity, 88% coverage: 1:226/256 of query aligns to 4:226/257 of 6slbAAA
- active site: Q64 (≠ L62), F69 (≠ L67), L80 (≠ N78), N84 (≠ A82), A108 (≠ G108), S111 (≠ E111), A130 (≠ T130), F131 (≠ H131), L136 (≠ I136), P138 (= P138), D139 (≠ G139), A224 (= A224)
- 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 (= R56), A62 (= A60), Q64 (≠ L62), D65 (= D63), L66 (= L64), Y76 (≠ M74), A108 (≠ G108), F131 (≠ H131), D139 (≠ G139)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 89% coverage: 2:228/256 of query aligns to 6:231/260 of 2hw5C
- active site: A68 (≠ L62), M73 (= M74), S83 (= S84), L87 (≠ R88), G111 (= G108), E114 (= E111), P133 (≠ T130), E134 (≠ H131), T139 (≠ I136), P141 (= P138), G142 (= G139), K227 (≠ A224)
- binding crotonyl coenzyme a: K26 (≠ E19), A27 (= A20), L28 (≠ M21), A30 (= A23), K62 (≠ R56), I70 (≠ L64), F109 (≠ I106)
Sites not aligning to the query:
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
39% identity, 88% coverage: 1:226/256 of query aligns to 1:214/245 of 6slaAAA
- active site: Q61 (≠ L62), L68 (≠ M74), N72 (= N78), A96 (≠ G108), S99 (≠ E111), A118 (≠ T130), F119 (≠ H131), L124 (≠ I136), P126 (= P138), N127 (≠ G139), A212 (= A224)
- 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 (≠ M21), A59 (= A60), Q61 (≠ L62), D62 (= D63), L63 (= L64), L68 (≠ M74), Y71 (≠ A77), A94 (≠ I106), G95 (≠ T107), A96 (≠ G108), F119 (≠ H131), I122 (≠ V134), L124 (≠ I136), N127 (≠ G139)
Sites not aligning to the query:
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
36% identity, 98% coverage: 4:254/256 of query aligns to 9:261/261 of 5jbxB
- active site: A67 (≠ L62), R72 (≠ P71), L84 (vs. gap), R88 (≠ S84), G112 (= G108), E115 (= E111), T134 (= T130), E135 (≠ H131), I140 (= I136), P142 (= P138), G143 (= G139), A228 (= A224), L238 (≠ N234)
- binding coenzyme a: S24 (≠ E19), R25 (≠ A20), R26 (≠ M21), A28 (= A23), A65 (= A60), D68 (= D63), L69 (= L64), K70 (= K65), L110 (≠ I106), G111 (≠ T107), T134 (= T130), E135 (≠ H131), L138 (≠ V134), R168 (≠ F164)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 89% coverage: 2:228/256 of query aligns to 5:225/254 of 2dubA
- active site: A67 (≠ L62), M72 (= M74), S82 (= S84), G105 (= G108), E108 (= E111), P127 (≠ T130), E128 (≠ H131), T133 (≠ I136), P135 (= P138), G136 (= G139), K221 (≠ A224)
- binding octanoyl-coenzyme a: K25 (≠ E19), A26 (= A20), L27 (≠ M21), A29 (= A23), A65 (= A60), A67 (≠ L62), D68 (= D63), I69 (≠ L64), K70 (= K65), G105 (= G108), E108 (= E111), P127 (≠ T130), E128 (≠ H131), G136 (= G139), A137 (≠ W140)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
33% identity, 89% coverage: 2:228/256 of query aligns to 6:231/260 of 1dubA
- active site: A68 (≠ L62), M73 (= M74), S83 (= S84), L87 (≠ R88), G111 (= G108), E114 (= E111), P133 (≠ T130), E134 (≠ H131), T139 (≠ I136), P141 (= P138), G142 (= G139), K227 (≠ A224)
- binding acetoacetyl-coenzyme a: K26 (≠ E19), A27 (= A20), L28 (≠ M21), A30 (= A23), A66 (= A60), A68 (≠ L62), D69 (= D63), I70 (≠ L64), Y107 (≠ V104), G110 (≠ T107), G111 (= G108), E114 (= E111), P133 (≠ T130), E134 (≠ H131), L137 (≠ V134), G142 (= G139)
Sites not aligning to the query:
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)
33% identity, 89% coverage: 2:228/256 of query aligns to 36:261/290 of P14604
- E144 (= E111) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ H131) 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
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
33% identity, 89% coverage: 2:228/256 of query aligns to 4:229/258 of 1ey3A
- active site: A66 (≠ L62), M71 (= M74), S81 (= S84), L85 (≠ R88), G109 (= G108), E112 (= E111), P131 (≠ T130), E132 (≠ H131), T137 (≠ I136), P139 (= P138), G140 (= G139), K225 (≠ A224)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E19), L26 (≠ M21), A28 (= A23), A64 (= A60), G65 (= G61), A66 (≠ L62), D67 (= D63), I68 (≠ L64), L85 (≠ R88), W88 (vs. gap), G109 (= G108), P131 (≠ T130), L135 (≠ V134), G140 (= G139)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
33% identity, 89% coverage: 2:228/256 of query aligns to 6:229/258 of 1mj3A
- active site: A68 (≠ L62), M73 (= M74), S83 (= S84), L85 (≠ P86), G109 (= G108), E112 (= E111), P131 (≠ T130), E132 (≠ H131), T137 (≠ I136), P139 (= P138), G140 (= G139), K225 (≠ A224)
- binding hexanoyl-coenzyme a: K26 (≠ E19), A27 (= A20), L28 (≠ M21), A30 (= A23), A66 (= A60), G67 (= G61), A68 (≠ L62), D69 (= D63), I70 (≠ L64), G109 (= G108), P131 (≠ T130), E132 (≠ H131), L135 (≠ V134), G140 (= G139)
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)
35% identity, 81% coverage: 10:216/256 of query aligns to 21:242/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
35% identity, 80% coverage: 9:212/256 of query aligns to 33:237/285 of Q7CQ56
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
34% identity, 80% coverage: 9:212/256 of query aligns to 33:237/285 of 4i42A
- active site: G86 (≠ L62), R91 (vs. gap), Y97 (vs. gap), H105 (≠ A76), L109 (≠ Q80), G133 (= G108), V136 (≠ E111), G156 (≠ H131), S161 (≠ I136), D163 (≠ P138), G164 (vs. gap)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ A20), R45 (≠ M21), S84 (≠ A60), G85 (= G61), G86 (≠ L62), D87 (= D63), Q88 (≠ L64), K89 (= K65), Y97 (vs. gap), V108 (≠ D79), Y129 (≠ V104), G133 (= G108), T155 (= T130), S161 (≠ I136)
Sites not aligning to the query:
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 80% coverage: 9:212/256 of query aligns to 33:237/285 of P0ABU0
- R45 (≠ M21) binding in other chain
- SGGDQK 84:89 (≠ AGLDLK 60:65) binding in other chain
- K89 (= K65) 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 (vs. gap) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ VAITG 104:108) binding in other chain
- Q154 (≠ D129) 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 (≠ DTH 129:131) binding
- T155 (= T130) binding in other chain
- G156 (≠ H131) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ I136) binding in other chain
- W184 (≠ S159) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
Sites not aligning to the query:
- 258 binding
- 267 R→A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- 270 F→A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- 273 binding ; K→A: Impairs protein folding.
Query Sequence
>CCNA_01794 CCNA_01794 enoyl-CoA hydratase/isomerase family
MLLIERRGAIAIVTLNRPEAMNALSKALRLALHDAIVQLDQDPDVSVVILTGAGDRAFTA
GLDLKELGGDPAAMGAANDQDARSNPVRAVETCRKPVIGAINGVAITGGFELALACDVLL
ASENARFADTHARVGIMPGWGLSQKLSRLIGPYRAKELSLTGNFLDARTAADWGLVNRVT
TASELLPTALRMAQDMASIPVEALSFYKSLIDDGYAVAFGEGLALEHERSSAHNRTVTPE
RVEAQRRQVMERGRGQ
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