SitesBLAST
Comparing WP_011384978.1 NCBI__GCF_000009985.1:WP_011384978.1 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)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
44% identity, 99% coverage: 3:256/256 of query aligns to 3:256/256 of 3h81A
- active site: A64 (= A64), M69 (= M69), T79 (≠ Q79), F83 (≠ H83), G107 (= G107), E110 (= E110), P129 (= P129), E130 (= E130), V135 (≠ I135), P137 (= P137), G138 (= G138), L223 (≠ M223), F233 (= F233)
- binding calcium ion: F233 (= F233), Q238 (= Q238)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
44% identity, 98% coverage: 3:253/256 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (= A64), M70 (= M69), T80 (≠ Q79), F84 (≠ H83), G108 (= G107), E111 (= E110), P130 (= P129), E131 (= E130), V136 (≠ I135), P138 (= P137), G139 (= G138), L224 (≠ M223), F234 (= F233)
- binding acetoacetyl-coenzyme a: Q23 (≠ D22), A24 (= A23), L25 (≠ K24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (= I66), K68 (= K67), M70 (= M69), F84 (≠ H83), G107 (= G106), G108 (= G107), E111 (= E110), P130 (= P129), E131 (= E130), P138 (= P137), G139 (= G138), M140 (≠ A139)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
44% identity, 98% coverage: 3:253/256 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (= A64), M70 (= M69), T80 (≠ Q79), F84 (≠ H83), G108 (= G107), E111 (= E110), P130 (= P129), E131 (= E130), V136 (≠ I135), P138 (= P137), G139 (= G138), L224 (≠ M223), F234 (= F233)
- binding coenzyme a: L25 (≠ K24), A63 (= A62), I67 (= I66), K68 (= K67), Y104 (= Y103), P130 (= P129), E131 (= E130), L134 (≠ V133)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
47% identity, 95% coverage: 11:254/256 of query aligns to 15:258/260 of 2hw5C
- active site: A68 (= A64), M73 (= M69), S83 (≠ Q79), L87 (≠ H83), G111 (= G107), E114 (= E110), P133 (= P129), E134 (= E130), T139 (≠ I135), P141 (= P137), G142 (= G138), K227 (≠ M223), F237 (= F233)
- binding crotonyl coenzyme a: K26 (≠ D22), A27 (= A23), L28 (≠ K24), A30 (= A26), K62 (≠ E58), I70 (= I66), F109 (≠ W105)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
48% identity, 95% coverage: 12:254/256 of query aligns to 16:256/258 of 1mj3A
- active site: A68 (= A64), M73 (= M69), S83 (≠ Q79), L85 (≠ N81), G109 (= G107), E112 (= E110), P131 (= P129), E132 (= E130), T137 (≠ I135), P139 (= P137), G140 (= G138), K225 (≠ M223), F235 (= F233)
- binding hexanoyl-coenzyme a: K26 (≠ D22), A27 (= A23), L28 (≠ K24), A30 (= A26), A66 (= A62), G67 (= G63), A68 (= A64), D69 (= D65), I70 (= I66), G109 (= G107), P131 (= P129), E132 (= E130), L135 (≠ V133), G140 (= G138)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
48% identity, 95% coverage: 12:254/256 of query aligns to 14:256/258 of 1ey3A
- active site: A66 (= A64), M71 (= M69), S81 (≠ Q79), L85 (≠ H83), G109 (= G107), E112 (= E110), P131 (= P129), E132 (= E130), T137 (≠ I135), P139 (= P137), G140 (= G138), K225 (≠ M223), F235 (= F233)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D22), L26 (≠ K24), A28 (= A26), A64 (= A62), G65 (= G63), A66 (= A64), D67 (= D65), I68 (= I66), L85 (≠ H83), W88 (= W86), G109 (= G107), P131 (= P129), L135 (≠ V133), G140 (= G138)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
48% identity, 95% coverage: 12:254/256 of query aligns to 16:258/260 of 1dubA
- active site: A68 (= A64), M73 (= M69), S83 (≠ Q79), L87 (≠ H83), G111 (= G107), E114 (= E110), P133 (= P129), E134 (= E130), T139 (≠ I135), P141 (= P137), G142 (= G138), K227 (≠ M223), F237 (= F233)
- binding acetoacetyl-coenzyme a: K26 (≠ D22), A27 (= A23), L28 (≠ K24), A30 (= A26), A66 (= A62), A68 (= A64), D69 (= D65), I70 (= I66), Y107 (= Y103), G110 (= G106), G111 (= G107), E114 (= E110), P133 (= P129), E134 (= E130), L137 (≠ V133), G142 (= G138), F233 (= F229), F249 (= F245)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
48% identity, 95% coverage: 12:254/256 of query aligns to 15:252/254 of 2dubA
- active site: A67 (= A64), M72 (= M69), S82 (≠ L84), G105 (= G107), E108 (= E110), P127 (= P129), E128 (= E130), T133 (≠ I135), P135 (= P137), G136 (= G138), K221 (≠ M223), F231 (= F233)
- binding octanoyl-coenzyme a: K25 (≠ D22), A26 (= A23), L27 (≠ K24), A29 (= A26), A65 (= A62), A67 (= A64), D68 (= D65), I69 (= I66), K70 (= K67), G105 (= G107), E108 (= E110), P127 (= P129), E128 (= E130), G136 (= G138), A137 (= A139)
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)
48% identity, 95% coverage: 11:254/256 of query aligns to 45:288/290 of P14604
- E144 (= E110) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E130) 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
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
44% identity, 98% coverage: 3:253/256 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (= A64), M69 (= M69), T75 (≠ Q79), F79 (≠ H83), G103 (= G107), E106 (= E110), P125 (= P129), E126 (= E130), V131 (≠ I135), P133 (= P137), G134 (= G138), L219 (≠ M223), F229 (= F233)
- binding Butyryl Coenzyme A: F225 (= F229), F241 (= F245)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
40% identity, 99% coverage: 3:256/256 of query aligns to 4:259/259 of 5zaiC
- active site: A65 (= A64), F70 (≠ M69), S82 (vs. gap), R86 (≠ H83), G110 (= G107), E113 (= E110), P132 (= P129), E133 (= E130), I138 (= I135), P140 (= P137), G141 (= G138), A226 (≠ M223), F236 (= F233)
- binding coenzyme a: K24 (≠ A23), L25 (≠ K24), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (= I66), P132 (= P129), R166 (≠ A163), F248 (= F245), K251 (= K248)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
37% identity, 93% coverage: 18:256/256 of query aligns to 20:261/261 of 5jbxB
- active site: A67 (= A64), R72 (≠ M69), L84 (≠ N81), R88 (vs. gap), G112 (= G107), E115 (= E110), T134 (≠ P129), E135 (= E130), I140 (= I135), P142 (= P137), G143 (= G138), A228 (≠ M223), L238 (≠ F233)
- binding coenzyme a: S24 (≠ D22), R25 (≠ A23), R26 (≠ K24), A28 (= A26), A65 (= A62), D68 (= D65), L69 (≠ I66), K70 (= K67), L110 (≠ W105), G111 (= G106), T134 (≠ P129), E135 (= E130), L138 (≠ V133), R168 (≠ A163)
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)
36% identity, 98% coverage: 4:254/256 of query aligns to 12:266/270 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)
34% identity, 95% coverage: 13:256/256 of query aligns to 18:266/266 of O53561
- K135 (≠ S125) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 125:132, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K132) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 99% coverage: 4:256/256 of query aligns to 1:245/245 of 6slaAAA
- active site: Q61 (≠ A64), L68 (≠ M78), N72 (= N82), A96 (≠ G107), S99 (≠ E110), A118 (≠ P129), F119 (≠ E130), L124 (≠ I135), P126 (= P137), N127 (≠ G138), A212 (≠ M223), G222 (≠ F233)
- 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 (≠ K24), A59 (= A62), Q61 (≠ A64), D62 (= D65), L63 (≠ I66), L68 (≠ M78), Y71 (≠ N81), A94 (≠ W105), G95 (= G106), A96 (≠ G107), F119 (≠ E130), I122 (≠ V133), L124 (≠ I135), N127 (≠ G138), F234 (= F245), K237 (= K248)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 99% coverage: 4:256/256 of query aligns to 4:257/257 of 6slbAAA
- active site: Q64 (≠ A64), F69 (≠ M69), L80 (≠ Q79), N84 (≠ H83), A108 (≠ G107), S111 (≠ E110), A130 (≠ P129), F131 (≠ E130), L136 (≠ I135), P138 (= P137), D139 (≠ G138), A224 (≠ M223), G234 (≠ F233)
- 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 (≠ E58), A62 (= A62), Q64 (≠ A64), D65 (= D65), L66 (≠ I66), Y76 (≠ I75), A108 (≠ G107), F131 (≠ E130), D139 (≠ G138)
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, 98% coverage: 2:253/256 of query aligns to 23:278/285 of Q7CQ56
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, 98% coverage: 6:256/256 of query aligns to 82:339/339 of Q13825
- K105 (≠ G29) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 29:43, 13% identical) RNA-binding
- K109 (≠ R33) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ E37) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G161) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
30% identity, 98% coverage: 3:253/256 of query aligns to 20:274/281 of 3t88A
- active site: G82 (≠ A64), R87 (≠ M69), Y93 (≠ I75), H101 (= H83), L105 (vs. gap), G129 (= G107), V132 (≠ E110), G152 (≠ E130), S157 (≠ I135), D159 (≠ P137), G160 (= G138), A246 (≠ E225), Y254 (≠ F233)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ D22), V40 (≠ A23), R41 (≠ K24), A43 (= A26), S80 (≠ A62), G81 (= G63), G82 (≠ A64), D83 (= D65), Q84 (≠ I66), K85 (= K67), Y93 (≠ I75), V104 (vs. gap), L105 (vs. gap), Y125 (= Y103), G129 (= G107), T151 (≠ P129), V155 (= V133), F158 (≠ M136), D159 (≠ P137), T250 (≠ F229), Y254 (≠ F233), F266 (= F245), K269 (= K248)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
30% identity, 98% coverage: 3:253/256 of query aligns to 24:278/285 of 4i42A
- active site: G86 (≠ A64), R91 (≠ M69), Y97 (≠ I75), H105 (= H83), L109 (vs. gap), G133 (= G107), V136 (≠ E110), G156 (≠ E130), S161 (≠ I135), D163 (≠ P137), G164 (= G138), A250 (≠ E225), Y258 (≠ F233)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ A23), R45 (≠ K24), S84 (≠ A62), G85 (= G63), G86 (≠ A64), D87 (= D65), Q88 (≠ I66), K89 (= K67), Y97 (≠ I75), V108 (vs. gap), Y129 (= Y103), G133 (= G107), T155 (≠ P129), S161 (≠ I135), T254 (≠ F229), F270 (= F245), K273 (= K248)
Query Sequence
>WP_011384978.1 NCBI__GCF_000009985.1:WP_011384978.1
MTEVLLEKPFDSVVLLRINRPDAKNALNGEVRRLLAEHMTTLGADPSVRAIVMTGNQEAF
AAGADIKDMAEVGAIELMQRNNHLLWRAIANCPKPVIAAVNGYAWGGGCELVMHADIIVA
GENASFSQPEVKVGIMPGAGGTQRLTRAVGKFKAMLMVMTGQAISGVEAGQMGLASVVVP
DAEVVDKALEIAKTISRMPPVAIAQIKEVLLAGQDASLDTALMLERKAFQLLFASADQKE
GMKAFIEKRKPTYQGK
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