SitesBLAST
Comparing WP_019620414.1 NCBI__GCF_000381785.1:WP_019620414.1 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)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
52% identity, 95% coverage: 11:257/259 of query aligns to 12:258/260 of 2hw5C
- active site: A68 (= A67), M73 (= M72), S83 (≠ K82), L87 (≠ V86), G111 (= G110), E114 (= E113), P133 (= P132), E134 (= E133), T139 (≠ I138), P141 (= P140), G142 (= G141), K227 (≠ L226), F237 (≠ A236)
- binding crotonyl coenzyme a: K26 (≠ E25), A27 (= A26), L28 (= L27), A30 (= A29), K62 (= K61), I70 (≠ V69), F109 (= F108)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
52% identity, 95% coverage: 11:257/259 of query aligns to 10:256/258 of 1ey3A
- active site: A66 (= A67), M71 (= M72), S81 (≠ K82), L85 (≠ V86), G109 (= G110), E112 (= E113), P131 (= P132), E132 (= E133), T137 (≠ I138), P139 (= P140), G140 (= G141), K225 (≠ L226), F235 (≠ A236)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E25), L26 (= L27), A28 (= A29), A64 (= A65), G65 (= G66), A66 (= A67), D67 (= D68), I68 (≠ V69), L85 (≠ V86), W88 (= W89), G109 (= G110), P131 (= P132), L135 (= L136), G140 (= G141)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
52% identity, 95% coverage: 11:257/259 of query aligns to 12:258/260 of 1dubA
- active site: A68 (= A67), M73 (= M72), S83 (≠ K82), L87 (≠ V86), G111 (= G110), E114 (= E113), P133 (= P132), E134 (= E133), T139 (≠ I138), P141 (= P140), G142 (= G141), K227 (≠ L226), F237 (≠ A236)
- binding acetoacetyl-coenzyme a: K26 (≠ E25), A27 (= A26), L28 (= L27), A30 (= A29), A66 (= A65), A68 (= A67), D69 (= D68), I70 (≠ V69), Y107 (≠ F106), G110 (= G109), G111 (= G110), E114 (= E113), P133 (= P132), E134 (= E133), L137 (= L136), G142 (= G141), F233 (= F232), F249 (= F248)
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)
52% identity, 95% coverage: 11:257/259 of query aligns to 42:288/290 of P14604
- E144 (= E113) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E133) 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
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
53% identity, 95% coverage: 11:257/259 of query aligns to 11:252/254 of 2dubA
- active site: A67 (= A67), M72 (= M72), S82 (≠ E87), G105 (= G110), E108 (= E113), P127 (= P132), E128 (= E133), T133 (≠ I138), P135 (= P140), G136 (= G141), K221 (≠ L226), F231 (≠ A236)
- binding octanoyl-coenzyme a: K25 (≠ E25), A26 (= A26), L27 (= L27), A29 (= A29), A65 (= A65), A67 (= A67), D68 (= D68), I69 (≠ V69), K70 (≠ R70), G105 (= G110), E108 (= E113), P127 (= P132), E128 (= E133), G136 (= G141), A137 (= A142)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
52% identity, 95% coverage: 11:257/259 of query aligns to 12:256/258 of 1mj3A
- active site: A68 (= A67), M73 (= M72), S83 (vs. gap), L85 (≠ V86), G109 (= G110), E112 (= E113), P131 (= P132), E132 (= E133), T137 (≠ I138), P139 (= P140), G140 (= G141), K225 (≠ L226), F235 (≠ A236)
- binding hexanoyl-coenzyme a: K26 (≠ E25), A27 (= A26), L28 (= L27), A30 (= A29), A66 (= A65), G67 (= G66), A68 (= A67), D69 (= D68), I70 (≠ V69), G109 (= G110), P131 (= P132), E132 (= E133), L135 (= L136), G140 (= G141)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
49% identity, 92% coverage: 19:256/259 of query aligns to 17:254/255 of 3q0jC
- active site: A65 (= A67), M70 (= M72), T80 (≠ K82), F84 (≠ V86), G108 (= G110), E111 (= E113), P130 (= P132), E131 (= E133), V136 (≠ I138), P138 (= P140), G139 (= G141), L224 (= L226), F234 (≠ A236)
- binding acetoacetyl-coenzyme a: Q23 (≠ E25), A24 (= A26), L25 (= L27), A27 (= A29), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (≠ V69), K68 (≠ R70), M70 (= M72), F84 (≠ V86), G107 (= G109), G108 (= G110), E111 (= E113), P130 (= P132), E131 (= E133), P138 (= P140), G139 (= G141), M140 (≠ A142)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
49% identity, 92% coverage: 19:256/259 of query aligns to 17:254/255 of 3q0gC
- active site: A65 (= A67), M70 (= M72), T80 (≠ K82), F84 (≠ V86), G108 (= G110), E111 (= E113), P130 (= P132), E131 (= E133), V136 (≠ I138), P138 (= P140), G139 (= G141), L224 (= L226), F234 (≠ A236)
- binding coenzyme a: L25 (= L27), A63 (= A65), I67 (≠ V69), K68 (≠ R70), Y104 (≠ F106), P130 (= P132), E131 (= E133), L134 (= L136)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
49% identity, 92% coverage: 19:256/259 of query aligns to 16:253/256 of 3h81A
- active site: A64 (= A67), M69 (= M72), T79 (≠ K82), F83 (≠ V86), G107 (= G110), E110 (= E113), P129 (= P132), E130 (= E133), V135 (≠ I138), P137 (= P140), G138 (= G141), L223 (= L226), F233 (≠ A236)
- binding calcium ion: F233 (≠ A236), Q238 (≠ R241)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
49% identity, 92% coverage: 19:256/259 of query aligns to 16:249/250 of 3q0gD
- active site: A64 (= A67), M69 (= M72), T75 (≠ K82), F79 (≠ V86), G103 (= G110), E106 (= E113), P125 (= P132), E126 (= E133), V131 (≠ I138), P133 (= P140), G134 (= G141), L219 (= L226), F229 (≠ A236)
- binding Butyryl Coenzyme A: F225 (= F232), F241 (= F248)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
42% identity, 94% coverage: 16:258/259 of query aligns to 14:258/259 of 5zaiC
- active site: A65 (= A67), F70 (≠ M72), S82 (≠ P84), R86 (vs. gap), G110 (= G110), E113 (= E113), P132 (= P132), E133 (= E133), I138 (= I138), P140 (= P140), G141 (= G141), A226 (≠ L226), F236 (≠ A236)
- binding coenzyme a: K24 (≠ A26), L25 (= L27), A63 (= A65), G64 (= G66), A65 (= A67), D66 (= D68), I67 (≠ V69), P132 (= P132), R166 (≠ P166), F248 (= F248), K251 (= K251)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
40% identity, 89% coverage: 28:258/259 of query aligns to 27:260/261 of 5jbxB
- active site: A67 (= A67), R72 (≠ M72), L84 (≠ K82), R88 (≠ V86), G112 (= G110), E115 (= E113), T134 (≠ P132), E135 (= E133), I140 (= I138), P142 (= P140), G143 (= G141), A228 (≠ L226), L238 (≠ A236)
- binding coenzyme a: A28 (= A29), A65 (= A65), D68 (= D68), L69 (≠ V69), K70 (≠ R70), L110 (≠ F108), G111 (= G109), T134 (≠ P132), E135 (= E133), L138 (= L136), R168 (≠ P166)
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)
34% identity, 97% coverage: 8:257/259 of query aligns to 13:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
36% identity, 86% coverage: 7:228/259 of query aligns to 2:210/224 of 3p85A
- active site: L62 (≠ A67), L67 (≠ M72), P68 (≠ A73), G92 (= G110), E95 (= E113), T114 (≠ P132), H115 (≠ E133), L120 (≠ I138), P122 (= P140), T123 (≠ G141), W208 (≠ L226)
- binding calcium ion: D43 (≠ N48), D45 (= D50)
Sites not aligning to the query:
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
31% identity, 95% coverage: 13:258/259 of query aligns to 10:256/257 of 6slbAAA
- active site: Q64 (≠ A67), F69 (≠ M72), L80 (≠ W89), N84 (vs. gap), A108 (≠ G110), S111 (≠ E113), A130 (≠ P132), F131 (≠ E133), L136 (≠ I138), P138 (= P140), D139 (≠ G141), A224 (≠ L226), G234 (≠ A236)
- 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 (≠ K61), A62 (= A65), Q64 (≠ A67), D65 (= D68), L66 (≠ V69), Y76 (≠ V86), A108 (≠ G110), F131 (≠ E133), D139 (≠ G141)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
31% identity, 95% coverage: 13:258/259 of query aligns to 7:244/245 of 6slaAAA
- active site: Q61 (≠ A67), L68 (≠ V86), N72 (≠ K90), A96 (≠ G110), S99 (≠ E113), A118 (≠ P132), F119 (≠ E133), L124 (≠ I138), P126 (= P140), N127 (≠ G141), A212 (≠ L226), G222 (≠ A236)
- 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 (= L27), A59 (= A65), Q61 (≠ A67), D62 (= D68), L63 (= L81), L68 (≠ V86), Y71 (≠ W89), A94 (≠ F108), G95 (= G109), A96 (≠ G110), F119 (≠ E133), I122 (≠ L136), L124 (≠ I138), N127 (≠ G141), F234 (= F248), K237 (= K251)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 93% coverage: 16:257/259 of query aligns to 18:264/266 of O53561
- K135 (= K128) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 128:135, 63% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K135) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
31% identity, 95% coverage: 6:252/259 of query aligns to 56:317/327 of Q62651
- D176 (≠ E113) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E133) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ G141) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
5dufA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk729a (see paper)
35% identity, 95% coverage: 13:259/259 of query aligns to 9:245/245 of 5dufA
- active site: A62 (= A67), D67 (= D76), P74 (≠ K82), I78 (≠ V86), A102 (≠ G110), Q105 (≠ E113), P124 (= P132), T125 (≠ E133), L130 (≠ I138), L132 (≠ P140), D133 (≠ G141), P212 (≠ L226), W222 (≠ A236)
- binding (5R,7S)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxylic acid: L77 (≠ R85), I78 (≠ V86), H81 (≠ W89), D85 (≠ T93), Q105 (≠ E113), D133 (≠ G141), W135 (≠ G143)
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
31% identity, 82% coverage: 15:226/259 of query aligns to 15:235/246 of 6p5uE
- active site: M67 (≠ A67), Y72 (≠ M72), D77 (vs. gap), R89 (≠ K82), A93 (≠ V86), G117 (= G110), T120 (≠ E113), E140 (= E133), I145 (= I138), P147 (= P140), A148 (≠ G141)
- binding coenzyme a: D25 (≠ E25), K26 (≠ A26), R27 (≠ L27), A29 (= A29), A65 (= A65), M67 (≠ A67), D68 (= D68), L69 (≠ V69), W113 (≠ F106), F115 (= F108), S139 (≠ P132), W143 (≠ L136)
Sites not aligning to the query:
Query Sequence
>WP_019620414.1 NCBI__GCF_000381785.1:WP_019620414.1
MNTPTNLLISGPSNGVLTITLHRPEALNALNTKLLEELVEQLEAAEKNNDIGAVVITGSA
KAFAAGADVREMASLDAVGVLKDPRVEHWKRVTAFKKPIIAAVNGFCFGGGCELAMHADI
IIAGEDAKFGQPEIKLGIMPGAGGTQRLLRSVGKSLAMQMVLTGEPITAGQAMSAGLISE
ITLSEMTLERAQTVAAQISRHAPIAVEMAKDALLKAFDTDLSSGLLYERKAFTLLAATED
RNEGINAFLEKRKPLFKGC
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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