SitesBLAST
Comparing 3607639 Dshi_1048 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)
37% identity, 95% coverage: 14:265/265 of query aligns to 10:259/259 of 5zaiC
- active site: A65 (= A69), F70 (= F74), S82 (≠ N88), R86 (≠ A92), G110 (= G116), E113 (= E119), P132 (≠ T138), E133 (≠ P139), I138 (≠ L144), P140 (≠ I146), G141 (= G147), A226 (= A228), F236 (= F242)
- binding coenzyme a: K24 (≠ R28), L25 (= L29), A63 (= A67), G64 (= G68), A65 (= A69), D66 (= D70), I67 (= I71), P132 (≠ T138), R166 (≠ P172), F248 (= F254), K251 (= K257)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
37% identity, 96% coverage: 12:265/265 of query aligns to 9:261/261 of 5jbxB
- active site: A67 (= A69), R72 (= R78), L84 (≠ N88), R88 (≠ A92), G112 (= G116), E115 (= E119), T134 (= T138), E135 (≠ P139), I140 (≠ L144), P142 (≠ I146), G143 (= G147), A228 (vs. gap), L238 (≠ F242)
- binding coenzyme a: S24 (≠ D27), R25 (= R28), R26 (≠ L29), A28 (= A31), A65 (= A67), D68 (= D70), L69 (≠ I71), K70 (≠ S72), L110 (≠ I114), G111 (= G115), T134 (= T138), E135 (≠ P139), L138 (= L142), R168 (≠ P172)
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)
34% identity, 92% coverage: 21:263/265 of query aligns to 24:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 95% coverage: 10:262/265 of query aligns to 6:254/255 of 3q0jC
- active site: A65 (= A69), M70 (≠ F74), T80 (≠ V84), F84 (≠ N88), G108 (= G116), E111 (= E119), P130 (≠ T138), E131 (≠ P139), V136 (≠ L144), P138 (≠ I146), G139 (= G147), L224 (≠ S232), F234 (= F242)
- binding acetoacetyl-coenzyme a: Q23 (≠ D27), A24 (≠ R28), L25 (= L29), A27 (= A31), A63 (= A67), G64 (= G68), A65 (= A69), D66 (= D70), I67 (= I71), K68 (≠ S72), M70 (≠ F74), F84 (≠ N88), G107 (= G115), G108 (= G116), E111 (= E119), P130 (≠ T138), E131 (≠ P139), P138 (≠ I146), G139 (= G147), M140 (≠ A148)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 95% coverage: 10:262/265 of query aligns to 6:254/255 of 3q0gC
- active site: A65 (= A69), M70 (≠ F74), T80 (≠ V84), F84 (≠ N88), G108 (= G116), E111 (= E119), P130 (≠ T138), E131 (≠ P139), V136 (≠ L144), P138 (≠ I146), G139 (= G147), L224 (≠ S232), F234 (= F242)
- binding coenzyme a: L25 (= L29), A63 (= A67), I67 (= I71), K68 (≠ S72), Y104 (≠ H112), P130 (≠ T138), E131 (≠ P139), L134 (= L142)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
35% identity, 95% coverage: 10:262/265 of query aligns to 5:253/256 of 3h81A
- active site: A64 (= A69), M69 (≠ F74), T79 (≠ V84), F83 (≠ N88), G107 (= G116), E110 (= E119), P129 (≠ T138), E130 (≠ P139), V135 (≠ L144), P137 (≠ I146), G138 (= G147), L223 (≠ S232), F233 (= F242)
- binding calcium ion: F233 (= F242), Q238 (≠ Y247)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 95% coverage: 10:262/265 of query aligns to 5:249/250 of 3q0gD
- active site: A64 (= A69), M69 (≠ F74), T75 (= T80), F79 (≠ V84), G103 (= G116), E106 (= E119), P125 (≠ T138), E126 (≠ P139), V131 (≠ L144), P133 (≠ I146), G134 (= G147), L219 (≠ S232), F229 (= F242)
- binding Butyryl Coenzyme A: F225 (≠ V238), F241 (= F254)
1ef9A The crystal structure of methylmalonyl coa decarboxylase complexed with 2s-carboxypropyl coa (see paper)
30% identity, 94% coverage: 18:265/265 of query aligns to 14:261/261 of 1ef9A
- active site: H66 (≠ A69), L71 (≠ F74), D82 (≠ N88), R86 (≠ A92), G110 (= G116), E113 (= E119), P133 (= P139), V138 (≠ L144), Y140 (≠ I146), N141 (≠ G147), E228 (≠ S232), Y238 (≠ F242)
- binding 2-carboxypropyl-coenzyme a: A64 (= A67), H66 (≠ A69), D67 (= D70), I68 (= I71), H69 (≠ S72), W108 (≠ I114), G110 (= G116), T132 (= T138), P133 (= P139), K253 (= K257)
P52045 Methylmalonyl-CoA decarboxylase; MMCD; Transcarboxylase; EC 4.1.1.- from Escherichia coli (strain K12) (see paper)
30% identity, 94% coverage: 18:265/265 of query aligns to 14:261/261 of P52045
- G110 (= G116) binding
- T132 (= T138) binding
- K253 (= K257) binding
6n97A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- amino(dethia)-coa (see paper)
30% identity, 94% coverage: 18:265/265 of query aligns to 13:260/260 of 6n97A
- active site: H65 (≠ A69), L70 (≠ F74), G109 (= G116), E112 (= E119), P132 (= P139), V137 (≠ L144), Y139 (≠ I146), E227 (≠ S232), Y237 (≠ F242)
- binding (2R)-sulfonatepropionyl-amino(dethia)-CoA: L24 (= L29), K59 (≠ R63), A63 (= A67), H65 (≠ A69), D66 (= D70), I67 (= I71), W107 (≠ I114), G108 (= G115), G109 (= G116), T131 (= T138), P132 (= P139), L135 (= L142), Y139 (≠ I146), F249 (= F254), K252 (= K257)
- binding (2S)-sulfonatepropionyl-amino(dethia)-CoA: L24 (= L29), K59 (≠ R63), A63 (= A67), H65 (≠ A69), D66 (= D70), I67 (= I71), W107 (≠ I114), G108 (= G115), G109 (= G116), T131 (= T138), P132 (= P139), L135 (= L142), Y139 (≠ I146), F249 (= F254), K252 (= K257)
6n96A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- oxa(dethia)-coa (see paper)
30% identity, 94% coverage: 18:265/265 of query aligns to 13:260/260 of 6n96A
- active site: H65 (≠ A69), L70 (≠ F74), G109 (= G116), E112 (= E119), P132 (= P139), V137 (≠ L144), Y139 (≠ I146), E227 (≠ S232), Y237 (≠ F242)
- binding (2~{S})-1-[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]ethoxy]-1-oxidanylidene-propane-2-sulfonic acid: K59 (≠ R63), A63 (= A67), H65 (≠ A69), D66 (= D70), I67 (= I71), H68 (≠ S72), W107 (≠ I114), G108 (= G115), G109 (= G116), T131 (= T138), P132 (= P139), L135 (= L142), V137 (≠ L144), Y139 (≠ I146), F249 (= F254), K252 (= K257)
- binding (2~{R})-1-[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]ethoxy]-1-oxidanylidene-propane-2-sulfonic acid: K59 (≠ R63), A63 (= A67), H65 (≠ A69), D66 (= D70), I67 (= I71), H68 (≠ S72), W107 (≠ I114), G108 (= G115), G109 (= G116), T131 (= T138), P132 (= P139), L135 (= L142), V137 (≠ L144), Y139 (≠ I146), F249 (= F254), K252 (= K257)
6n95A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- coa (see paper)
30% identity, 94% coverage: 18:265/265 of query aligns to 13:260/260 of 6n95A
- active site: H65 (≠ A69), L70 (≠ F74), G109 (= G116), E112 (= E119), P132 (= P139), V137 (≠ L144), Y139 (≠ I146), E227 (≠ S232), Y237 (≠ F242)
- binding (2R)-sulfonatepropionyl-CoA: K23 (≠ R28), L24 (= L29), K59 (≠ R63), A63 (= A67), H65 (≠ A69), D66 (= D70), I67 (= I71), H68 (≠ S72), W107 (≠ I114), G108 (= G115), G109 (= G116), T131 (= T138), P132 (= P139), L135 (= L142), Y139 (≠ I146), F249 (= F254), K252 (= K257)
- binding (2S)-sulfonatepropionyl-CoA: K23 (≠ R28), L24 (= L29), K59 (≠ R63), A63 (= A67), H65 (≠ A69), D66 (= D70), I67 (= I71), H68 (≠ S72), W107 (≠ I114), G108 (= G115), G109 (= G116), T131 (= T138), P132 (= P139), L135 (= L142), V137 (≠ L144), Y139 (≠ I146), F249 (= F254), K252 (= K257)
6n94A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- amino(dethia)-coa (see paper)
30% identity, 94% coverage: 18:265/265 of query aligns to 13:260/260 of 6n94A
- active site: H65 (≠ A69), L70 (≠ F74), G109 (= G116), E112 (= E119), P132 (= P139), V137 (≠ L144), Y139 (≠ I146), E227 (≠ S232), Y237 (≠ F242)
- binding [1-[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]ethylamino]-1-oxidanylidene-propan-2-ylidene]-bis(oxidanidyl)azanium: K23 (≠ R28), L24 (= L29), A63 (= A67), H65 (≠ A69), D66 (= D70), I67 (= I71), H68 (≠ S72), W107 (≠ I114), G108 (= G115), G109 (= G116), T131 (= T138), P132 (= P139), Y139 (≠ I146)
6n93A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- oxa(dethia)-coa (see paper)
30% identity, 94% coverage: 18:265/265 of query aligns to 13:260/260 of 6n93A
- active site: H65 (≠ A69), L70 (≠ F74), G109 (= G116), E112 (= E119), P132 (= P139), V137 (≠ L144), Y139 (≠ I146), E227 (≠ S232), Y237 (≠ F242)
- binding [1-[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]ethoxy]-1-oxidanylidene-propan-2-ylidene]-bis(oxidanidyl)azanium: L24 (= L29), A63 (= A67), H65 (≠ A69), D66 (= D70), I67 (= I71), H68 (≠ S72), W107 (≠ I114), T131 (= T138), L135 (= L142), F249 (= F254), K252 (= K257)
6n92F Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- coa (see paper)
30% identity, 94% coverage: 18:265/265 of query aligns to 13:260/260 of 6n92F
- active site: H65 (≠ A69), L70 (≠ F74), G109 (= G116), E112 (= E119), P132 (= P139), V137 (≠ L144), Y139 (≠ I146), E227 (≠ S232), Y237 (≠ F242)
- binding [1-[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]-1-oxidanylidene-propan-2-ylidene]-bis(oxidanidyl)azanium: R22 (≠ D27), K23 (≠ R28), L24 (= L29), A63 (= A67), H65 (≠ A69), D66 (= D70), S105 (≠ H112), W107 (≠ I114), W107 (≠ I114), G108 (= G115), G109 (= G116), T127 (≠ R134), F128 (≠ I135), S129 (≠ A136), T131 (= T138), P132 (= P139), Y139 (≠ I146), S164 (≠ Q171), P165 (= P172), F249 (= F254)
- binding (2E)-2-(hydroxyimino)propanoic acid: E240 (≠ A245), H260 (≠ Q265)
6n92A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- coa (see paper)
30% identity, 94% coverage: 18:265/265 of query aligns to 13:260/260 of 6n92A
- active site: H65 (≠ A69), L70 (≠ F74), G109 (= G116), E112 (= E119), P132 (= P139), V137 (≠ L144), Y139 (≠ I146), E227 (≠ S232), Y237 (≠ F242)
- binding [1-[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]-1-oxidanylidene-propan-2-ylidene]-bis(oxidanidyl)azanium: L24 (= L29), A63 (= A67), H65 (≠ A69), D66 (= D70), I67 (= I71), H68 (≠ S72), W107 (≠ I114), G108 (= G115), G109 (= G116), T131 (= T138), P132 (= P139), Y139 (≠ I146), F249 (= F254), K252 (= K257)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
32% identity, 92% coverage: 18:262/265 of query aligns to 34:278/285 of Q7CQ56
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 95% coverage: 14:265/265 of query aligns to 13:260/260 of 2hw5C
- active site: A68 (= A69), M73 (≠ F74), S83 (≠ N88), L87 (≠ A92), G111 (= G116), E114 (= E119), P133 (≠ T138), E134 (≠ P139), T139 (≠ L144), P141 (≠ I146), G142 (= G147), K227 (≠ S232), F237 (= F242)
- binding crotonyl coenzyme a: K26 (≠ D27), A27 (≠ R28), L28 (= L29), A30 (= A31), K62 (≠ R63), I70 (= I71), F109 (≠ I114)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
32% identity, 92% coverage: 18:262/265 of query aligns to 34:278/285 of 4i42A
- active site: G86 (≠ A69), R91 (≠ F74), Y97 (≠ T80), H105 (≠ N88), L109 (≠ A92), G133 (= G116), V136 (≠ E119), G156 (≠ P139), S161 (≠ L144), D163 (≠ I146), G164 (= G147), A250 (= A234), Y258 (≠ F242)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ R28), R45 (≠ L29), S84 (≠ A67), G85 (= G68), G86 (≠ A69), D87 (= D70), Q88 (≠ I71), K89 (≠ S72), Y97 (≠ T80), V108 (= V91), Y129 (≠ H112), G133 (= G116), T155 (= T138), S161 (≠ L144), T254 (≠ V238), F270 (= F254), K273 (= K257)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 92% coverage: 18:262/265 of query aligns to 34:278/285 of P0ABU0
- R45 (≠ L29) binding in other chain
- SGGDQK 84:89 (≠ AGADIS 67:72) binding in other chain
- K89 (≠ S72) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (≠ F74) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ T80) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ HCIGG 112:116) binding in other chain
- Q154 (≠ F137) 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 (≠ FTP 137:139) binding
- T155 (= T138) binding in other chain
- G156 (≠ P139) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L144) binding in other chain
- W184 (≠ L167) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ F242) binding
- R267 (≠ Q251) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F254) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K257) binding ; mutation to A: Impairs protein folding.
Query Sequence
>3607639 Dshi_1048 Enoyl-CoA hydratase/isomerase (RefSeq)
MSRALAEGRLLLDREGPVARITLNNPDRLNAMRLAMWQGLGDLAVELAASDARVVVLRGA
GDRAFCAGADISEFPQVRATPEGVAAYNRTVARALEGLAALPMPVLAAIRGHCIGGGLEI
AVRCDLRLASETARIAFTPAKLGLAIGADEVAALARIAGPAAAAELLYTAQPVDAARAER
WGLVNRRVPEDMLMDEADALARTIAANAPLTLRAVKAGLAAFARPGDAAAASHADALVKT
CFDSADYREGQRAFAEKRRPEFKGQ
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