SitesBLAST
Comparing Ga0059261_2902 Ga0059261_2902 Enoyl-CoA hydratase/carnithine racemase to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 96% coverage: 12:273/273 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ G72), F69 (≠ M77), L80 (≠ I91), N84 (≠ Q100), A108 (= A124), S111 (≠ D127), A130 (≠ S146), F131 (= F147), L136 (= L152), P138 (≠ S154), D139 (≠ A155), A224 (≠ E240), G234 (≠ Q250)
- 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 (≠ D66), A62 (= A70), Q64 (≠ G72), D65 (≠ N73), L66 (= L74), Y76 (≠ F84), A108 (= A124), F131 (= F147), D139 (≠ A155)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 96% coverage: 12:273/273 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ G72), L68 (≠ I91), N72 (≠ Q100), A96 (= A124), S99 (≠ D127), A118 (≠ S146), F119 (= F147), L124 (= L152), P126 (≠ S154), N127 (≠ A155), A212 (≠ E240), G222 (≠ Q250)
- 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 (≠ R32), A59 (= A70), Q61 (≠ G72), D62 (≠ N73), L63 (= L74), L68 (≠ I91), Y71 (≠ V99), A94 (≠ M122), G95 (= G123), A96 (= A124), F119 (= F147), I122 (≠ L150), L124 (= L152), N127 (≠ A155), F234 (≠ V262), K237 (≠ R265)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 94% coverage: 15:271/273 of query aligns to 7:250/250 of 3q0gD
- active site: A64 (≠ G72), M69 (= M77), T75 (≠ A88), F79 (≠ R92), G103 (≠ A124), E106 (≠ D127), P125 (≠ S146), E126 (≠ F147), V131 (≠ L152), P133 (≠ S154), G134 (≠ A155), L219 (≠ E240), F229 (≠ Q250)
- binding Butyryl Coenzyme A: F225 (≠ Q246), F241 (≠ V262)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
37% identity, 95% coverage: 15:273/273 of query aligns to 7:256/256 of 3h81A
- active site: A64 (≠ G72), M69 (= M77), T79 (≠ A85), F83 (≠ R92), G107 (≠ A124), E110 (≠ D127), P129 (≠ S146), E130 (≠ F147), V135 (≠ L152), P137 (≠ S154), G138 (≠ A155), L223 (≠ E240), F233 (≠ Q250)
- binding calcium ion: F233 (≠ Q250), Q238 (= Q255)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
37% identity, 94% coverage: 15:271/273 of query aligns to 8:255/255 of 3q0jC
- active site: A65 (≠ G72), M70 (= M77), T80 (≠ A85), F84 (≠ R92), G108 (≠ A124), E111 (≠ D127), P130 (≠ S146), E131 (≠ F147), V136 (≠ L152), P138 (≠ S154), G139 (≠ A155), L224 (≠ E240), F234 (≠ Q250)
- binding acetoacetyl-coenzyme a: Q23 (≠ G30), A24 (≠ T31), L25 (≠ R32), A27 (= A34), A63 (= A70), G64 (= G71), A65 (≠ G72), D66 (≠ N73), I67 (≠ L74), K68 (= K75), M70 (= M77), F84 (≠ R92), G107 (= G123), G108 (≠ A124), E111 (≠ D127), P130 (≠ S146), E131 (≠ F147), P138 (≠ S154), G139 (≠ A155), M140 (≠ A156)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 94% coverage: 15:271/273 of query aligns to 8:255/255 of 3q0gC
- active site: A65 (≠ G72), M70 (= M77), T80 (≠ A85), F84 (≠ R92), G108 (≠ A124), E111 (≠ D127), P130 (≠ S146), E131 (≠ F147), V136 (≠ L152), P138 (≠ S154), G139 (≠ A155), L224 (≠ E240), F234 (≠ Q250)
- binding coenzyme a: L25 (≠ R32), A63 (= A70), I67 (≠ L74), K68 (= K75), Y104 (≠ A120), P130 (≠ S146), E131 (≠ F147), L134 (= L150)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
31% identity, 96% coverage: 13:273/273 of query aligns to 6:259/259 of 5zaiC
- active site: A65 (≠ G72), F70 (≠ M77), S82 (≠ A85), R86 (≠ A89), G110 (≠ A124), E113 (≠ D127), P132 (≠ S146), E133 (≠ F147), I138 (≠ L152), P140 (≠ S154), G141 (≠ A155), A226 (≠ E240), F236 (≠ Q250)
- binding coenzyme a: K24 (≠ T31), L25 (≠ R32), A63 (= A70), G64 (= G71), A65 (≠ G72), D66 (≠ N73), I67 (≠ L74), P132 (≠ S146), R166 (≠ T180), F248 (≠ V262), K251 (≠ R265)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
31% identity, 96% coverage: 13:273/273 of query aligns to 7:261/261 of 5jbxB
- active site: A67 (≠ G72), R72 (≠ M77), L84 (= L96), R88 (≠ Q100), G112 (≠ A124), E115 (≠ D127), T134 (≠ S146), E135 (≠ F147), I140 (≠ L152), P142 (≠ S154), G143 (≠ A155), A228 (≠ E240), L238 (≠ Q250)
- binding coenzyme a: S24 (≠ G30), R25 (≠ T31), R26 (= R32), A28 (= A34), A65 (= A70), D68 (≠ N73), L69 (= L74), K70 (= K75), L110 (≠ M122), G111 (= G123), T134 (≠ S146), E135 (≠ F147), L138 (= L150), R168 (≠ T180)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
30% identity, 93% coverage: 17:270/273 of query aligns to 13:257/260 of 1dubA
- active site: A68 (≠ G72), M73 (= M77), S83 (≠ A85), L87 (= L96), G111 (≠ A124), E114 (≠ D127), P133 (≠ S146), E134 (≠ F147), T139 (≠ L152), P141 (≠ S154), G142 (≠ A155), K227 (≠ E240), F237 (≠ Q250)
- binding acetoacetyl-coenzyme a: K26 (≠ G30), A27 (≠ T31), L28 (≠ R32), A30 (= A34), A66 (= A70), A68 (≠ G72), D69 (≠ N73), I70 (≠ L74), Y107 (≠ A120), G110 (= G123), G111 (≠ A124), E114 (≠ D127), P133 (≠ S146), E134 (≠ F147), L137 (= L150), G142 (≠ A155), F233 (≠ Q246), F249 (≠ V262)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 93% coverage: 17:270/273 of query aligns to 11:255/258 of 1ey3A
- active site: A66 (≠ G72), M71 (= M77), S81 (≠ A85), L85 (= L96), G109 (≠ A124), E112 (≠ D127), P131 (≠ S146), E132 (≠ F147), T137 (≠ L152), P139 (≠ S154), G140 (≠ A155), K225 (≠ I248), F235 (vs. gap)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ G30), L26 (≠ R32), A28 (= A34), A64 (= A70), G65 (= G71), A66 (≠ G72), D67 (≠ N73), I68 (≠ L74), L85 (= L96), W88 (≠ V99), G109 (≠ A124), P131 (≠ S146), L135 (= L150), G140 (≠ A155)
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)
31% identity, 93% coverage: 17:270/273 of query aligns to 43:287/290 of P14604
- E144 (≠ D127) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F147) 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)
31% identity, 93% coverage: 17:270/273 of query aligns to 13:255/258 of 1mj3A
- active site: A68 (≠ G72), M73 (= M77), S83 (≠ A85), L85 (= L96), G109 (≠ A124), E112 (≠ D127), P131 (≠ S146), E132 (≠ F147), T137 (≠ L152), P139 (≠ S154), G140 (≠ A155), K225 (≠ I248), F235 (vs. gap)
- binding hexanoyl-coenzyme a: K26 (≠ G30), A27 (≠ T31), L28 (≠ R32), A30 (= A34), A66 (= A70), G67 (= G71), A68 (≠ G72), D69 (≠ N73), I70 (≠ L74), G109 (≠ A124), P131 (≠ S146), E132 (≠ F147), L135 (= L150), G140 (≠ A155)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 93% coverage: 17:270/273 of query aligns to 12:251/254 of 2dubA
- active site: A67 (≠ G72), M72 (= M77), S82 (≠ A97), G105 (≠ A124), E108 (≠ D127), P127 (≠ S146), E128 (≠ F147), T133 (≠ L152), P135 (≠ S154), G136 (≠ A155), K221 (≠ I248), F231 (vs. gap)
- binding octanoyl-coenzyme a: K25 (≠ G30), A26 (≠ T31), L27 (≠ R32), A29 (= A34), A65 (= A70), A67 (≠ G72), D68 (≠ N73), I69 (≠ L74), K70 (= K75), G105 (≠ A124), E108 (≠ D127), P127 (≠ S146), E128 (≠ F147), G136 (≠ A155), A137 (= A156)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
30% identity, 93% coverage: 17:270/273 of query aligns to 13:257/260 of 2hw5C
- active site: A68 (≠ G72), M73 (= M77), S83 (≠ L96), L87 (≠ Q100), G111 (≠ A124), E114 (≠ D127), P133 (≠ S146), E134 (≠ F147), T139 (≠ L152), P141 (≠ S154), G142 (≠ A155), K227 (≠ E240), F237 (≠ Q250)
- binding crotonyl coenzyme a: K26 (≠ G30), A27 (≠ T31), L28 (≠ R32), A30 (= A34), K62 (≠ D66), I70 (≠ L74), F109 (≠ M122)
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, 92% coverage: 21:270/273 of query aligns to 21:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 95% coverage: 15:273/273 of query aligns to 12:266/266 of O53561
- K135 (= K142) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 142:149, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K149) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
36% identity, 73% coverage: 24:221/273 of query aligns to 14:189/224 of 3p85A
- active site: L62 (≠ G72), L67 (≠ M77), P68 (≠ A89), G92 (≠ A124), E95 (≠ D127), T114 (≠ S146), H115 (≠ F147), L120 (= L152), P122 (≠ S154), T123 (≠ A155)
- binding calcium ion: D43 (= D53), D45 (≠ S55)
Sites not aligning to the query:
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
30% identity, 95% coverage: 13:271/273 of query aligns to 21:275/281 of 3t88A
- active site: G82 (= G72), R87 (= R80), Y93 (≠ A88), H101 (≠ L96), L105 (≠ Q100), G129 (≠ A124), V132 (≠ D127), G152 (≠ F147), S157 (≠ L152), D159 (≠ S154), G160 (≠ A155), A246 (= A242), Y254 (≠ Q250)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ G30), V40 (≠ T31), R41 (= R32), A43 (= A34), S80 (≠ A70), G81 (= G71), G82 (= G72), D83 (≠ N73), Q84 (≠ L74), K85 (= K75), Y93 (≠ A88), V104 (= V99), L105 (≠ Q100), Y125 (≠ A120), G129 (≠ A124), T151 (≠ S146), V155 (≠ L150), F158 (≠ T153), D159 (≠ S154), T250 (≠ Q246), Y254 (≠ Q250), F266 (≠ V262), K269 (≠ R265)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
30% identity, 95% coverage: 13:271/273 of query aligns to 25:279/285 of 4i42A
- active site: G86 (= G72), R91 (= R80), Y97 (≠ A88), H105 (≠ L96), L109 (≠ Q100), G133 (≠ A124), V136 (≠ D127), G156 (≠ F147), S161 (≠ L152), D163 (≠ S154), G164 (≠ A155), A250 (= A242), Y258 (≠ Q250)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ T31), R45 (= R32), S84 (≠ A70), G85 (= G71), G86 (= G72), D87 (≠ N73), Q88 (≠ L74), K89 (= K75), Y97 (≠ A88), V108 (= V99), Y129 (≠ A120), G133 (≠ A124), T155 (≠ S146), S161 (≠ L152), T254 (≠ Q246), F270 (≠ V262), K273 (≠ R265)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 95% coverage: 13:271/273 of query aligns to 25:279/285 of P0ABU0
- R45 (= R32) binding in other chain
- SGGDQK 84:89 (≠ AGGNLK 70:75) binding in other chain
- K89 (= K75) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R80) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (≠ A88) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ AAMGA 120:124) binding in other chain
- Q154 (≠ E145) 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 (≠ ESF 145:147) binding
- T155 (≠ S146) binding in other chain
- G156 (≠ F147) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L152) binding in other chain
- W184 (≠ A175) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ Q250) binding
- R267 (≠ V259) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (≠ V262) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (≠ R265) binding ; mutation to A: Impairs protein folding.
Query Sequence
>Ga0059261_2902 Ga0059261_2902 Enoyl-CoA hydratase/carnithine racemase
MSADVNESSRAVLRVERDGPLVILTIDDPGTRNALSPLLTRELVAACDAINADMSVGCVI
LTAAGDVFCAGGNLKDMYARANHFAGNAAEIRRTYLAGVQTIARALHDLEVPSIAAVNGA
AMGAGMDFATMCTMRIASDRAKFAESFIKLGLTSAAGGAWFLTRAIGQSAAAEMALTGDT
LDAEQALAIGLVSRVVQHDALLDEARTLAARITRHPMHSIRLNTRLLRDSARLDLHTALE
IAAGMQAIVQQTDDQHEAVAAVMERRIPAFTGR
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