SitesBLAST
Comparing BPHYT_RS28020 BPHYT_RS28020 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)
36% identity, 93% coverage: 4:256/272 of query aligns to 6:257/259 of 5zaiC
- active site: A65 (= A63), F70 (= F68), S82 (≠ A80), R86 (≠ G84), G110 (= G108), E113 (= E111), P132 (= P130), E133 (= E131), I138 (≠ L136), P140 (= P138), G141 (≠ C139), A226 (= A225), F236 (= F235)
- binding coenzyme a: K24 (≠ A22), L25 (vs. gap), A63 (= A61), G64 (= G62), A65 (= A63), D66 (= D64), I67 (≠ L65), P132 (= P130), R166 (= R164), F248 (= F247), K251 (= K250)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
40% identity, 86% coverage: 23:256/272 of query aligns to 27:259/261 of 5jbxB
- active site: A67 (= A63), R72 (≠ F68), L84 (≠ A80), R88 (≠ G84), G112 (= G108), E115 (= E111), T134 (≠ P130), E135 (= E131), I140 (≠ L136), P142 (= P138), G143 (≠ C139), A228 (= A225), L238 (≠ F235)
- binding coenzyme a: A28 (= A24), A65 (= A61), D68 (= D64), L69 (= L65), K70 (≠ N66), L110 (≠ M106), G111 (= G107), T134 (≠ P130), E135 (= E131), L138 (≠ V134), R168 (= R164)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 91% coverage: 9:256/272 of query aligns to 14:258/260 of 1dubA
- active site: A68 (= A63), M73 (≠ F68), S83 (≠ A80), L87 (≠ G84), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (≠ L136), P141 (= P138), G142 (≠ C139), K227 (≠ A225), F237 (= F235)
- binding acetoacetyl-coenzyme a: K26 (≠ P21), A27 (= A22), L28 (vs. gap), A30 (= A24), A66 (= A61), A68 (= A63), D69 (= D64), I70 (≠ L65), Y107 (= Y104), G110 (= G107), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), L137 (≠ V134), G142 (≠ C139), F233 (= F231), F249 (= F247)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
34% identity, 91% coverage: 9:256/272 of query aligns to 12:256/258 of 1ey3A
- active site: A66 (= A63), M71 (≠ F68), S81 (≠ A80), L85 (≠ G84), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (≠ L136), P139 (= P138), G140 (≠ C139), K225 (≠ A225), F235 (= F235)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ P21), L26 (vs. gap), A28 (= A24), A64 (= A61), G65 (= G62), A66 (= A63), D67 (= D64), I68 (≠ L65), L85 (≠ G84), W88 (≠ F87), G109 (= G108), P131 (= P130), L135 (≠ V134), G140 (≠ C139)
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)
34% identity, 91% coverage: 9:256/272 of query aligns to 44:288/290 of P14604
- E144 (= E111) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E131) 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
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
33% identity, 91% coverage: 9:256/272 of query aligns to 14:258/260 of 2hw5C
- active site: A68 (= A63), M73 (≠ F68), S83 (≠ A80), L87 (≠ G84), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (≠ L136), P141 (= P138), G142 (≠ C139), K227 (≠ A225), F237 (= F235)
- binding crotonyl coenzyme a: K26 (≠ P21), A27 (= A22), L28 (≠ N23), A30 (≠ F25), K62 (= K57), I70 (≠ L65), F109 (≠ M106)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
36% identity, 91% coverage: 9:255/272 of query aligns to 11:254/255 of 3q0jC
- active site: A65 (= A63), M70 (≠ F68), T80 (= T78), F84 (≠ G84), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (≠ L136), P138 (= P138), G139 (≠ C139), L224 (≠ A225), F234 (= F235)
- binding acetoacetyl-coenzyme a: Q23 (≠ P21), A24 (= A22), L25 (vs. gap), A27 (= A24), A63 (= A61), G64 (= G62), A65 (= A63), D66 (= D64), I67 (≠ L65), K68 (≠ N66), M70 (≠ F68), F84 (≠ G84), G107 (= G107), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), P138 (= P138), G139 (≠ C139), M140 (≠ G140)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 91% coverage: 9:255/272 of query aligns to 11:254/255 of 3q0gC
- active site: A65 (= A63), M70 (≠ F68), T80 (= T78), F84 (≠ G84), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (≠ L136), P138 (= P138), G139 (≠ C139), L224 (≠ A225), F234 (= F235)
- binding coenzyme a: L25 (vs. gap), A63 (= A61), I67 (≠ L65), K68 (≠ N66), Y104 (= Y104), P130 (= P130), E131 (= E131), L134 (≠ V134)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
36% identity, 91% coverage: 9:255/272 of query aligns to 10:253/256 of 3h81A
- active site: A64 (= A63), M69 (≠ F68), T79 (= T78), F83 (≠ G84), G107 (= G108), E110 (= E111), P129 (= P130), E130 (= E131), V135 (≠ L136), P137 (= P138), G138 (≠ C139), L223 (≠ A225), F233 (= F235)
- binding calcium ion: F233 (= F235), Q238 (= Q240)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 91% coverage: 9:255/272 of query aligns to 10:249/250 of 3q0gD
- active site: A64 (= A63), M69 (≠ T67), T75 (≠ A80), F79 (≠ G84), G103 (= G108), E106 (= E111), P125 (= P130), E126 (= E131), V131 (≠ L136), P133 (= P138), G134 (≠ C139), L219 (≠ A225), F229 (= F235)
- binding Butyryl Coenzyme A: F225 (= F231), F241 (= F247)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 91% coverage: 9:256/272 of query aligns to 13:252/254 of 2dubA
- active site: A67 (= A63), M72 (≠ V75), S82 (≠ A85), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), T133 (≠ L136), P135 (= P138), G136 (≠ C139), K221 (≠ A225), F231 (= F235)
- binding octanoyl-coenzyme a: K25 (≠ P21), A26 (= A22), L27 (vs. gap), A29 (= A24), A65 (= A61), A67 (= A63), D68 (= D64), I69 (≠ L65), K70 (≠ R73), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), G136 (≠ C139), A137 (≠ G140)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
33% identity, 91% coverage: 9:256/272 of query aligns to 14:256/258 of 1mj3A
- active site: A68 (= A63), M73 (≠ F68), S83 (≠ T78), L85 (≠ A80), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (≠ L136), P139 (= P138), G140 (≠ C139), K225 (≠ A225), F235 (= F235)
- binding hexanoyl-coenzyme a: K26 (≠ P21), A27 (= A22), L28 (vs. gap), A30 (= A24), A66 (= A61), G67 (= G62), A68 (= A63), D69 (= D64), I70 (≠ L65), G109 (= G108), P131 (= P130), E132 (= E131), L135 (≠ V134), G140 (≠ C139)
Q08426 Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens (Human) (see 5 papers)
38% identity, 69% coverage: 9:197/272 of query aligns to 8:189/723 of Q08426
- V40 (≠ N41) to G: in dbSNP:rs1062551
- I41 (≠ G42) to R: in dbSNP:rs1062552
- T75 (≠ R82) to I: in dbSNP:rs1062553
- K165 (≠ R172) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.
- K171 (≠ E178) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.
Sites not aligning to the query:
- 3 E → K: in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells; dbSNP:rs398124646
- 274 A → T: in dbSNP:rs2302819
- 325 A → G: in dbSNP:rs1062555
- 346 modified: N6-acetyllysine; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
- 584 modified: N6-acetyllysine; alternate; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
- 598 K → T: in dbSNP:rs1042437
- 606 T → P: in dbSNP:rs1042438
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)
35% identity, 86% coverage: 23:256/272 of query aligns to 101:337/339 of Q13825
- K105 (≠ P27) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 27:41, 20% identical) RNA-binding
- K109 (≠ L31) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ Q35) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G162) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
37% identity, 69% coverage: 8:195/272 of query aligns to 11:201/707 of 6yswA
- active site: A66 (= A63), I71 (≠ F68), A84 (= A81), Q88 (≠ A85), G112 (= G108), E115 (= E111), P136 (= P130), E137 (= E131), G145 (≠ C139)
- binding coenzyme a: E23 (≠ P20), M25 (≠ A22), A66 (= A63), D67 (= D64), I68 (≠ L65), P136 (= P130), E137 (= E131), L140 (≠ V134)
Sites not aligning to the query:
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)
32% identity, 96% coverage: 2:263/272 of query aligns to 15:276/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 91% coverage: 9:256/272 of query aligns to 11:255/257 of 6slbAAA
- active site: Q64 (≠ A63), F69 (= F68), L80 (≠ A80), N84 (≠ G84), A108 (≠ G108), S111 (≠ E111), A130 (≠ P130), F131 (≠ E131), L136 (= L136), P138 (= P138), D139 (≠ C139), A224 (= A225), G234 (≠ F235)
- 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 (≠ K57), A62 (= A61), Q64 (≠ A63), D65 (= D64), L66 (= L65), Y76 (≠ V75), A108 (≠ G108), F131 (≠ E131), D139 (≠ C139)
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)
31% identity, 90% coverage: 15:259/272 of query aligns to 24:269/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
38% identity, 65% coverage: 6:181/272 of query aligns to 4:174/692 of 6iunB
Sites not aligning to the query:
- active site: 248, 407, 428, 440, 478
- binding nicotinamide-adenine-dinucleotide: 300, 301, 302, 321, 322, 365, 377, 378, 380, 384, 388, 405, 407
4jvtA Crystal structure of tfu_1878, a putative enoyl-coa hydratase fromthermobifida fusca yx in complex with coa
42% identity, 66% coverage: 9:188/272 of query aligns to 20:208/257 of 4jvtA
- active site: I72 (≠ A63), F77 (= F68), I97 (vs. gap), Q101 (≠ G84), A125 (≠ G108), Q128 (≠ E111), K147 (≠ P130), E148 (= E131), D156 (≠ C139)
- binding acetyl coenzyme *a: H32 (≠ P21), R33 (≠ A22), R34 (vs. gap), A36 (= A24), S70 (≠ A61), G71 (= G62), I72 (≠ A63), I123 (≠ M106), G124 (= G107)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS28020 BPHYT_RS28020 enoyl-CoA hydratase
MIELDYADDGAVAQLTLKRPPANAFTPEGLLQLQQTVERLNGEARVRAIVITGDGPKFFS
AGADLNTFADGNREVARTAAARFGAAFETLQNARPVVIAAINGYAMGGGLECALACDIRI
AEQHALLALPETAVGLLPCGCGTQTLPWLVGEGWAKRMILTGERVDAATALRIGLVEEVV
EKGAARDAALVMAARVATLSPQAVGFSKTLIHQGRSGVPRAAALALERERFVDLFDGADQ
REGVNAFLEKRPPRWQVTQSAQTDASQPEMRQ
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