SitesBLAST
Comparing Pf6N2E2_1834 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1834 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)
41% identity, 98% coverage: 5:254/256 of query aligns to 5:254/256 of 3h81A
- active site: A64 (= A64), M69 (≠ L69), T79 (≠ E79), F83 (≠ G83), G107 (≠ A107), E110 (= E110), P129 (= P129), E130 (= E130), V135 (≠ I135), P137 (= P137), G138 (= G138), L223 (≠ A223), F233 (= F233)
- binding calcium ion: F233 (= F233), Q238 (≠ K238)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
41% identity, 98% coverage: 5:254/256 of query aligns to 6:255/255 of 3q0jC
- active site: A65 (= A64), M70 (≠ L69), T80 (≠ E79), F84 (≠ G83), G108 (≠ A107), E111 (= E110), P130 (= P129), E131 (= E130), V136 (≠ I135), P138 (= P137), G139 (= G138), L224 (≠ A223), F234 (= F233)
- binding acetoacetyl-coenzyme a: Q23 (≠ E22), A24 (≠ K23), L25 (≠ R24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), K68 (≠ N67), M70 (≠ L69), F84 (≠ G83), G107 (= G106), G108 (≠ A107), 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
41% identity, 98% coverage: 5:254/256 of query aligns to 6:255/255 of 3q0gC
- active site: A65 (= A64), M70 (≠ L69), T80 (≠ E79), F84 (≠ G83), G108 (≠ A107), E111 (= E110), P130 (= P129), E131 (= E130), V136 (≠ I135), P138 (= P137), G139 (= G138), L224 (≠ A223), F234 (= F233)
- binding coenzyme a: L25 (≠ R24), A63 (= A62), I67 (≠ L66), K68 (≠ N67), Y104 (≠ F103), P130 (= P129), E131 (= E130), L134 (≠ V133)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
41% identity, 98% coverage: 5:254/256 of query aligns to 5:250/250 of 3q0gD
- active site: A64 (= A64), M69 (≠ L69), T75 (≠ E79), F79 (≠ G83), G103 (≠ A107), E106 (= E110), P125 (= P129), E126 (= E130), V131 (≠ I135), P133 (= P137), G134 (= G138), L219 (≠ A223), F229 (= F233)
- binding Butyryl Coenzyme A: F225 (= F229), F241 (= F245)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
40% identity, 96% coverage: 9:253/256 of query aligns to 13:257/260 of 1dubA
- active site: A68 (= A64), M73 (≠ L69), S83 (≠ E79), L87 (≠ G83), G111 (≠ A107), E114 (= E110), P133 (= P129), E134 (= E130), T139 (≠ I135), P141 (= P137), G142 (= G138), K227 (≠ A223), F237 (= F233)
- binding acetoacetyl-coenzyme a: K26 (≠ E22), A27 (≠ K23), L28 (≠ R24), A30 (= A26), A66 (= A62), A68 (= A64), D69 (= D65), I70 (≠ L66), Y107 (≠ F103), G110 (= G106), G111 (≠ A107), E114 (= E110), P133 (= P129), E134 (= E130), L137 (≠ V133), G142 (= G138), F233 (= F229), F249 (= F245)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
40% identity, 96% coverage: 9:253/256 of query aligns to 11:255/258 of 1ey3A
- active site: A66 (= A64), M71 (≠ L69), S81 (≠ E79), L85 (≠ G83), G109 (≠ A107), E112 (= E110), P131 (= P129), E132 (= E130), T137 (≠ I135), P139 (= P137), G140 (= G138), K225 (≠ A223), F235 (= F233)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E22), L26 (≠ R24), A28 (= A26), A64 (= A62), G65 (= G63), A66 (= A64), D67 (= D65), I68 (≠ L66), L85 (≠ G83), W88 (= W86), G109 (≠ A107), P131 (= P129), L135 (≠ V133), G140 (= G138)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
40% identity, 96% coverage: 9:253/256 of query aligns to 12:251/254 of 2dubA
- active site: A67 (= A64), M72 (≠ L69), S82 (≠ Q84), G105 (≠ A107), E108 (= E110), P127 (= P129), E128 (= E130), T133 (≠ I135), P135 (= P137), G136 (= G138), K221 (≠ A223), F231 (= F233)
- binding octanoyl-coenzyme a: K25 (≠ E22), A26 (≠ K23), L27 (≠ R24), A29 (= A26), A65 (= A62), A67 (= A64), D68 (= D65), I69 (≠ L66), K70 (≠ N67), G105 (≠ A107), 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)
40% identity, 96% coverage: 9:253/256 of query aligns to 43:287/290 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
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
40% identity, 96% coverage: 9:253/256 of query aligns to 13:257/260 of 2hw5C
- active site: A68 (= A64), M73 (≠ L69), S83 (≠ E79), L87 (≠ G83), G111 (≠ A107), E114 (= E110), P133 (= P129), E134 (= E130), T139 (≠ I135), P141 (= P137), G142 (= G138), K227 (≠ A223), F237 (= F233)
- binding crotonyl coenzyme a: K26 (≠ E22), A27 (≠ K23), L28 (≠ R24), A30 (= A26), K62 (≠ S58), I70 (≠ L66), F109 (≠ L105)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
40% identity, 96% coverage: 9:253/256 of query aligns to 13:255/258 of 1mj3A
- active site: A68 (= A64), M73 (≠ L69), S83 (≠ D81), L85 (≠ G83), G109 (≠ A107), E112 (= E110), P131 (= P129), E132 (= E130), T137 (≠ I135), P139 (= P137), G140 (= G138), K225 (≠ A223), F235 (= F233)
- binding hexanoyl-coenzyme a: K26 (≠ E22), A27 (≠ K23), L28 (≠ R24), A30 (= A26), A66 (= A62), G67 (= G63), A68 (= A64), D69 (= D65), I70 (≠ L66), G109 (≠ A107), P131 (= P129), E132 (= E130), L135 (≠ V133), G140 (= G138)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
36% identity, 98% coverage: 5:256/256 of query aligns to 6:259/259 of 5zaiC
- active site: A65 (= A64), F70 (≠ V77), S82 (≠ V89), R86 (≠ Q93), G110 (≠ A107), E113 (= E110), P132 (= P129), E133 (= E130), I138 (= I135), P140 (= P137), G141 (= G138), A226 (= A223), F236 (= F233)
- binding coenzyme a: K24 (= K23), L25 (≠ R24), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), P132 (= P129), R166 (≠ L163), F248 (= F245), K251 (= K248)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
38% identity, 97% coverage: 7:255/256 of query aligns to 9:260/261 of 5jbxB
- active site: A67 (= A64), R72 (≠ L69), L84 (= L80), R88 (≠ G83), G112 (≠ A107), E115 (= E110), T134 (≠ P129), E135 (= E130), I140 (= I135), P142 (= P137), G143 (= G138), A228 (= A223), L238 (≠ F233)
- binding coenzyme a: S24 (≠ E22), R25 (≠ K23), R26 (= R24), A28 (= A26), A65 (= A62), D68 (= D65), L69 (= L66), K70 (≠ N67), L110 (= L105), G111 (= G106), T134 (≠ P129), E135 (= E130), L138 (≠ V133), R168 (≠ L163)
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, 94% coverage: 13:253/256 of query aligns to 21:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 98% coverage: 5:255/256 of query aligns to 5:256/257 of 6slbAAA
- active site: Q64 (≠ A64), F69 (≠ L69), L80 (= L80), N84 (≠ G83), A108 (= A107), S111 (≠ E110), A130 (≠ P129), F131 (≠ E130), L136 (≠ I135), P138 (= P137), D139 (≠ G138), A224 (= A223), 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 (≠ S58), A62 (= A62), Q64 (≠ A64), D65 (= D65), L66 (= L66), Y76 (≠ Q76), A108 (= A107), F131 (≠ E130), D139 (≠ G138)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 97% coverage: 6:253/256 of query aligns to 11:263/266 of O53561
- K135 (≠ R125) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 125:132, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ R132) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 98% coverage: 5:256/256 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A64), L68 (≠ D71), N72 (≠ Q75), A96 (= A107), S99 (≠ E110), A118 (≠ P129), F119 (≠ E130), L124 (≠ I135), P126 (= P137), N127 (≠ G138), A212 (= A223), 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 (≠ R24), A59 (= A62), Q61 (≠ A64), D62 (= D65), L63 (= L66), L68 (≠ D71), Y71 (≠ A74), A94 (≠ L105), G95 (= G106), A96 (= A107), F119 (≠ E130), I122 (≠ V133), L124 (≠ I135), N127 (≠ G138), F234 (= F245), K237 (= K248)
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)
34% identity, 97% coverage: 8:256/256 of query aligns to 84:339/339 of Q13825
- K105 (≠ L29) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 29:43, 13% identical) RNA-binding
- K109 (≠ V33) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ S37) 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
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
39% identity, 76% coverage: 13:206/256 of query aligns to 11:191/224 of 3p85A
- active site: L62 (≠ A64), L67 (= L69), P68 (≠ V70), G92 (≠ A107), E95 (= E110), T114 (≠ P129), H115 (≠ E130), L120 (≠ I135), P122 (= P137), T123 (≠ G138)
- binding calcium ion: D43 (= D45), D45 (≠ G47)
Sites not aligning to the query:
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
29% identity, 95% coverage: 12:254/256 of query aligns to 33:279/285 of Q7CQ56
Q8GYN9 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; DHNS; Enoyl-CoA hydratase/isomerase D; ECHID; Naphthoate synthase; EC 4.1.3.36 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 95% coverage: 13:254/256 of query aligns to 87:331/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
Query Sequence
>Pf6N2E2_1834 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1834
MSAPVVVERNGAVAILRLNRVEKRNALDLSMRVAIASAMQELERDSGVAVIVITGGDSVF
AAGADLNLLVDKGAQQVAELDLGQYWAPVAKSQKPLIAAVSGFALGAGCELAMMCDILVA
DNSARFGQPEARVGIMPGAGGTQRLLRAVGKPVASLMLLAGELLSAERASQLGLVSELVT
EGSALARAIVLAQATATMPPKALRAIKRVLALGADQSLDLALALENREFLLLFDTQDKTE
GMRAFLDKRPPRYTGN
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