SitesBLAST
Comparing AO356_26370 FitnessBrowser__pseudo5_N2C3_1:AO356_26370 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)
3bptA Crystal structure of human beta-hydroxyisobutyryl-coa hydrolase in complex with quercetin
36% identity, 93% coverage: 17:360/368 of query aligns to 4:345/362 of 3bptA
- active site: G67 (= G80), P84 (≠ E97), R88 (≠ V101), G115 (= G128), G118 (= G131), E138 (= E151), D146 (= D159)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G79), G67 (= G80), I69 (= I82), E90 (= E103), G114 (= G127), G115 (= G128), E138 (= E151), D146 (= D159), V147 (= V160)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ G38), L26 (= L39), A28 (= A41), G66 (= G79), G67 (= G80), I69 (= I82), P137 (= P150), I141 (= I154), L319 (= L334)
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
37% identity, 94% coverage: 18:364/368 of query aligns to 2:332/340 of 4hdtA
- active site: G64 (= G80), I69 (≠ L85), W84 (≠ F100), Y88 (= Y104), G112 (= G128), G115 (= G131), E135 (= E151), P142 (= P158), D143 (= D159), R283 (≠ A311)
- binding zinc ion: H28 (≠ L44), E42 (≠ A58), E57 (≠ D73), E79 (≠ L95), H93 (≠ T109), H185 (≠ S201)
Sites not aligning to the query:
Q9LKJ1 3-hydroxyisobutyryl-CoA hydrolase 1; CoA-thioester hydrolase CHY1; EC 3.1.2.-; EC 3.1.2.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 93% coverage: 18:361/368 of query aligns to 9:354/378 of Q9LKJ1
- G70 (= G80) mutation to S: Loss of activity.
- E142 (= E151) mutation to A: Loss of activity.
- D150 (= D159) mutation to G: Reduced activity.
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
36% identity, 46% coverage: 26:194/368 of query aligns to 14:172/254 of 2dubA
- active site: A67 (≠ G80), M72 (≠ L85), S82 (≠ L95), G105 (= G128), E108 (≠ G131), P127 (= P150), E128 (= E151), T133 (≠ Y156), P135 (= P158), G136 (≠ D159)
- binding octanoyl-coenzyme a: K25 (≠ A37), A26 (≠ G38), L27 (= L39), A29 (= A41), A65 (= A78), A67 (≠ G80), D68 (= D81), I69 (= I82), K70 (≠ R83), G105 (= G128), E108 (≠ G131), P127 (= P150), E128 (= E151), G136 (≠ D159), A137 (≠ V160)
Sites not aligning to the query:
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)
36% identity, 46% coverage: 26:194/368 of query aligns to 45:208/290 of P14604
- E144 (≠ G131) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E151) 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
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
36% identity, 46% coverage: 25:194/368 of query aligns to 14:178/260 of 1dubA
- active site: A68 (≠ G80), M73 (≠ L85), S83 (≠ E97), L87 (≠ V101), G111 (= G128), E114 (≠ G131), P133 (= P150), E134 (= E151), T139 (≠ Y156), P141 (= P158), G142 (≠ D159)
- binding acetoacetyl-coenzyme a: K26 (≠ A37), A27 (≠ G38), L28 (= L39), A30 (= A41), A66 (= A78), A68 (≠ G80), D69 (= D81), I70 (= I82), Y107 (≠ F124), G110 (= G127), G111 (= G128), E114 (≠ G131), P133 (= P150), E134 (= E151), L137 (≠ I154), G142 (≠ D159)
Sites not aligning to the query:
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
36% identity, 46% coverage: 26:194/368 of query aligns to 13:176/258 of 1ey3A
- active site: A66 (≠ G80), M71 (≠ L85), S81 (≠ E97), L85 (≠ V101), G109 (= G128), E112 (≠ G131), P131 (= P150), E132 (= E151), T137 (≠ Y156), P139 (= P158), G140 (≠ D159)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A37), L26 (= L39), A28 (= A41), A64 (= A78), G65 (= G79), A66 (≠ G80), D67 (= D81), I68 (= I82), L85 (≠ V101), W88 (≠ Y104), G109 (= G128), P131 (= P150), L135 (≠ I154), G140 (≠ D159)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
36% identity, 46% coverage: 25:194/368 of query aligns to 14:176/258 of 1mj3A
- active site: A68 (≠ G80), M73 (≠ L85), S83 (≠ V101), L85 (≠ E103), G109 (= G128), E112 (≠ G131), P131 (= P150), E132 (= E151), T137 (≠ Y156), P139 (= P158), G140 (≠ D159)
- binding hexanoyl-coenzyme a: K26 (≠ A37), A27 (≠ G38), L28 (= L39), A30 (= A41), A66 (= A78), G67 (= G79), A68 (≠ G80), D69 (= D81), I70 (= I82), G109 (= G128), P131 (= P150), E132 (= E151), L135 (≠ I154), G140 (≠ D159)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
31% identity, 58% coverage: 31:244/368 of query aligns to 17:225/259 of 5zaiC
- active site: A65 (≠ G80), F70 (≠ L85), S82 (≠ F100), R86 (≠ Y104), G110 (= G128), E113 (≠ G131), P132 (= P150), E133 (= E151), I138 (≠ Y156), P140 (= P158), G141 (≠ D159)
- binding coenzyme a: K24 (≠ G38), L25 (= L39), A63 (= A78), G64 (= G79), A65 (≠ G80), D66 (= D81), I67 (= I82), P132 (= P150), R166 (≠ Q183)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 46% coverage: 25:194/368 of query aligns to 14:178/260 of 2hw5C
- active site: A68 (≠ G80), M73 (≠ L85), S83 (≠ A105), L87 (≠ T109), G111 (= G128), E114 (≠ G131), P133 (= P150), E134 (= E151), T139 (≠ Y156), P141 (= P158), G142 (≠ D159)
- binding crotonyl coenzyme a: K26 (≠ A37), A27 (≠ G38), L28 (= L39), A30 (= A41), K62 (= K74), I70 (= I82), F109 (≠ L126)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 48% coverage: 20:194/368 of query aligns to 5:170/250 of 3q0gD
- active site: A64 (≠ G80), M69 (≠ L85), T75 (≠ H96), F79 (= F100), G103 (= G128), E106 (≠ G131), P125 (= P150), E126 (= E151), V131 (≠ Y156), P133 (= P158), G134 (≠ D159)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 48% coverage: 20:194/368 of query aligns to 6:175/255 of 3q0jC
- active site: A65 (≠ G80), M70 (≠ L85), T80 (≠ H96), F84 (= F100), G108 (= G128), E111 (≠ G131), P130 (= P150), E131 (= E151), V136 (≠ Y156), P138 (= P158), G139 (≠ D159)
- binding acetoacetyl-coenzyme a: Q23 (≠ A37), A24 (≠ G38), L25 (= L39), A27 (= A41), A63 (= A78), G64 (= G79), A65 (≠ G80), D66 (= D81), I67 (= I82), K68 (≠ R83), M70 (≠ L85), F84 (= F100), G107 (= G127), G108 (= G128), E111 (≠ G131), P130 (= P150), E131 (= E151), P138 (= P158), G139 (≠ D159), M140 (≠ V160)
Sites not aligning to the query:
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 48% coverage: 20:194/368 of query aligns to 6:175/255 of 3q0gC
- active site: A65 (≠ G80), M70 (≠ L85), T80 (≠ H96), F84 (= F100), G108 (= G128), E111 (≠ G131), P130 (= P150), E131 (= E151), V136 (≠ Y156), P138 (= P158), G139 (≠ D159)
- binding coenzyme a: L25 (= L39), A63 (= A78), I67 (= I82), K68 (≠ R83), Y104 (≠ F124), P130 (= P150), E131 (= E151), L134 (≠ I154)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
35% identity, 48% coverage: 20:194/368 of query aligns to 5:174/256 of 3h81A
- active site: A64 (≠ G80), M69 (≠ L85), T79 (≠ H96), F83 (= F100), G107 (= G128), E110 (≠ G131), P129 (= P150), E130 (= E151), V135 (≠ Y156), P137 (= P158), G138 (≠ D159)
Sites not aligning to the query:
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
34% identity, 49% coverage: 13:194/368 of query aligns to 1:184/266 of O53561
- K135 (≠ R146) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 146:153, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ A153) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
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)
32% identity, 55% coverage: 26:227/368 of query aligns to 9:206/723 of Q08426
- V40 (≠ A58) to G: in dbSNP:rs1062551
- I41 (≠ L59) to R: in dbSNP:rs1062552
- T75 (= T94) to I: in dbSNP:rs1062553
- K165 (≠ Y191) 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 (≠ W197) 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
6z1pBI mS93 (see paper)
29% identity, 44% coverage: 33:195/368 of query aligns to 37:201/1413 of 6z1pBI
- active site: T85 (≠ G80), S134 (≠ G128), E157 (= E151), D165 (= D159)
- binding : Y41 (≠ A37), K42 (≠ G38), Q43 (≠ L39), T45 (≠ A41), D47 (≠ T43), H49 (≠ G45), K83 (≠ A78), T85 (≠ G80), D86 (= D81), F87 (≠ I82), K88 (≠ R83), K92 (≠ D87), L130 (≠ F124), K152 (≠ R146)
Sites not aligning to the query:
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 48% coverage: 19:196/368 of query aligns to 6:181/261 of 5jbxB
- active site: A67 (≠ G80), R72 (≠ G92), L84 (≠ V101), R88 (≠ D107), G112 (= G128), E115 (≠ G131), T134 (≠ P150), E135 (= E151), I140 (≠ Y156), P142 (= P158), G143 (≠ D159)
- binding coenzyme a: S24 (≠ A37), R25 (≠ G38), R26 (≠ L39), A28 (= A41), A65 (= A78), D68 (= D81), L69 (≠ I82), K70 (≠ Q90), L110 (= L126), G111 (= G127), T134 (≠ P150), E135 (= E151), L138 (≠ I154), R168 (≠ Q183)
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)
31% identity, 42% coverage: 17:172/368 of query aligns to 18:177/285 of Q7CQ56
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
31% identity, 45% coverage: 9:172/368 of query aligns to 14:173/281 of 3t88A
- active site: G82 (= G80), R87 (= R83), Y93 (≠ H89), H101 (≠ E97), L105 (≠ V101), G129 (= G128), V132 (≠ G131), G152 (≠ E151), S157 (≠ Y156), D159 (≠ P158), G160 (≠ D159)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ A37), V40 (≠ G38), R41 (≠ L39), A43 (= A41), S80 (≠ A78), G81 (= G79), G82 (= G80), D83 (= D81), Q84 (vs. gap), K85 (vs. gap), Y93 (≠ H89), V104 (≠ F100), L105 (≠ V101), Y125 (≠ F124), G129 (= G128), T151 (≠ P150), V155 (≠ I154), F158 (= F157), D159 (≠ P158)
Sites not aligning to the query:
Query Sequence
>AO356_26370 FitnessBrowser__pseudo5_N2C3_1:AO356_26370
MTAQVSSQAAETMETVANEVLVDVRNHIGHLTLNRPAGLNALTLGMVRSLQQQLDTWALD
PHIRAVVLRGAGDKAFCAGGDIRSLYDSHQQGDTLHEDFFVEEYALDLTIHHYRKPVLAL
MDGFVLGGGMGLVQGADLRIVTERSRLGMPEVAIGYFPDVGGSYFLPRIPGELGIYLGVS
GVQIRAADALYCGLADWYLDSRKLKQLDERLDRLEWHDAPLKDLQSLLAKLGQQQLPAPP
LADLRPAIDHFFALPDVPSMVEQLRQVTVVNSHEWALKTADVLESRSPLAMAVTLEMLRR
GRHLSLEDCFALELHLDRQWFERGDLIEGVRALLIDKDKNPRWNPPTLEALDADHVASFF
DGFDDHGN
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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