SitesBLAST
Comparing AO353_17555 FitnessBrowser__pseudo3_N2E3:AO353_17555 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
35% identity, 94% coverage: 6:354/370 of query aligns to 6:345/362 of 3bptA
- active site: G67 (= G68), P84 (≠ A89), R88 (≠ S93), G115 (= G120), G118 (= G123), E138 (= E143), D146 (= D151)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G67), G67 (= G68), I69 (≠ V70), E90 (= E95), G114 (= G119), G115 (= G120), E138 (= E143), D146 (= D151), V147 (= V152)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ S26), L26 (= L27), A28 (= A29), G66 (= G67), G67 (= G68), I69 (≠ V70), P137 (= P142), I141 (= I146), L319 (= L328)
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)
30% identity, 94% coverage: 12:357/370 of query aligns to 15:356/378 of Q9LKJ1
- G70 (= G68) mutation to S: Loss of activity.
- E142 (= E143) mutation to A: Loss of activity.
- D150 (= D151) mutation to G: Reduced activity.
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
32% identity, 92% coverage: 16:357/370 of query aligns to 12:331/340 of 4hdtA
- active site: G64 (= G68), I69 (≠ L73), W84 (≠ F92), Y88 (= Y96), G112 (= G120), G115 (= G123), E135 (= E143), P142 (= P150), D143 (= D151), R283 (≠ Q305)
- binding zinc ion: H28 (≠ L32), E42 (≠ A46), E57 (≠ A61), E79 (= E83), H93 (≠ R101), H185 (≠ D193)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
28% identity, 62% coverage: 3:230/370 of query aligns to 1:215/259 of 5zaiC
- active site: A65 (≠ G68), F70 (≠ L73), S82 (= S93), R86 (= R97), G110 (= G120), E113 (≠ G123), P132 (= P142), E133 (= E143), I138 (≠ L148), P140 (= P150), G141 (≠ D151)
- binding coenzyme a: K24 (≠ S26), L25 (= L27), A63 (= A66), G64 (= G67), A65 (≠ G68), D66 (≠ E69), I67 (≠ V70), P132 (= P142), R166 (≠ Q175)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
28% identity, 51% coverage: 14:201/370 of query aligns to 14:188/254 of 2dubA
- active site: A67 (≠ G68), M72 (≠ L73), S82 (≠ A79), G105 (= G120), E108 (≠ G123), P127 (= P142), E128 (= E143), T133 (≠ L148), P135 (= P150), G136 (≠ D151)
- binding octanoyl-coenzyme a: K25 (= K25), A26 (≠ S26), L27 (= L27), A29 (= A29), A65 (= A66), A67 (≠ G68), D68 (≠ E69), I69 (≠ V70), K70 (≠ R71), G105 (= G120), E108 (≠ G123), P127 (= P142), E128 (= E143), G136 (≠ D151), A137 (≠ V152)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
28% identity, 45% coverage: 15:181/370 of query aligns to 12:169/256 of 3h81A
- active site: A64 (≠ G68), M69 (≠ L73), T79 (≠ R97), F83 (vs. gap), G107 (= G120), E110 (≠ G123), P129 (= P142), E130 (= E143), V135 (≠ L148), P137 (= P150), G138 (≠ D151)
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)
29% identity, 51% coverage: 14:201/370 of query aligns to 45:224/290 of P14604
- E144 (≠ G123) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E143) 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
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
30% identity, 45% coverage: 15:181/370 of query aligns to 13:170/255 of 3q0jC
- active site: A65 (≠ G68), M70 (≠ L73), T80 (≠ A88), F84 (= F92), G108 (= G120), E111 (≠ G123), P130 (= P142), E131 (= E143), V136 (≠ L148), P138 (= P150), G139 (≠ D151)
- binding acetoacetyl-coenzyme a: Q23 (≠ K25), A24 (≠ S26), L25 (= L27), A27 (= A29), A63 (= A66), G64 (= G67), A65 (≠ G68), D66 (≠ E69), I67 (≠ V70), K68 (≠ R71), M70 (≠ L73), F84 (= F92), G107 (= G119), G108 (= G120), E111 (≠ G123), P130 (= P142), E131 (= E143), P138 (= P150), G139 (≠ D151), M140 (≠ V152)
Sites not aligning to the query:
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 45% coverage: 15:181/370 of query aligns to 13:170/255 of 3q0gC
- active site: A65 (≠ G68), M70 (≠ L73), T80 (≠ A88), F84 (= F92), G108 (= G120), E111 (≠ G123), P130 (= P142), E131 (= E143), V136 (≠ L148), P138 (= P150), G139 (≠ D151)
- binding coenzyme a: L25 (= L27), A63 (= A66), I67 (≠ V70), K68 (≠ R71), Y104 (= Y116), P130 (= P142), E131 (= E143), L134 (≠ I146)
Sites not aligning to the query:
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
29% identity, 51% coverage: 14:201/370 of query aligns to 13:192/258 of 1ey3A
- active site: A66 (≠ G68), M71 (≠ L73), S81 (≠ R97), L85 (≠ R101), G109 (= G120), E112 (≠ G123), P131 (= P142), E132 (= E143), T137 (≠ L148), P139 (= P150), G140 (≠ D151)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K25), L26 (= L27), A28 (= A29), A64 (= A66), G65 (= G67), A66 (≠ G68), D67 (≠ E69), I68 (≠ V70), L85 (≠ R101), W88 (vs. gap), G109 (= G120), P131 (= P142), L135 (≠ I146), G140 (≠ D151)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
29% identity, 51% coverage: 14:201/370 of query aligns to 15:194/260 of 1dubA
- active site: A68 (≠ G68), M73 (≠ L73), S83 (≠ R97), L87 (≠ R101), G111 (= G120), E114 (≠ G123), P133 (= P142), E134 (= E143), T139 (≠ L148), P141 (= P150), G142 (≠ D151)
- binding acetoacetyl-coenzyme a: K26 (= K25), A27 (≠ S26), L28 (= L27), A30 (= A29), A66 (= A66), A68 (≠ G68), D69 (≠ E69), I70 (≠ V70), Y107 (= Y116), G110 (= G119), G111 (= G120), E114 (≠ G123), P133 (= P142), E134 (= E143), L137 (≠ I146), G142 (≠ D151)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
28% identity, 45% coverage: 15:181/370 of query aligns to 12:165/250 of 3q0gD
- active site: A64 (≠ G68), M69 (≠ L73), T75 (≠ R97), F79 (vs. gap), G103 (= G120), E106 (≠ G123), P125 (= P142), E126 (= E143), V131 (≠ L148), P133 (= P150), G134 (≠ D151)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 45% coverage: 16:181/370 of query aligns to 17:173/260 of 2hw5C
- active site: A68 (≠ G68), M73 (≠ V84), S83 (≠ R97), L87 (≠ R101), G111 (= G120), E114 (≠ G123), P133 (= P142), E134 (= E143), T139 (≠ L148), P141 (= P150), G142 (≠ D151)
- binding crotonyl coenzyme a: K26 (= K25), A27 (≠ S26), L28 (= L27), A30 (= A29), K62 (= K62), I70 (≠ V70), F109 (≠ L118)
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)
28% identity, 63% coverage: 18:251/370 of query aligns to 20:246/266 of O53561
- K135 (≠ R138) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 138:145, 13% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ S145) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
26% identity, 65% coverage: 20:260/370 of query aligns to 19:251/261 of 5jbxB
- active site: A67 (≠ G68), R72 (= R78), L84 (≠ S93), R88 (= R97), G112 (= G120), E115 (≠ G123), T134 (≠ P142), E135 (= E143), I140 (≠ L148), P142 (= P150), G143 (≠ D151), A228 (≠ W236), L238 (= L247)
- binding coenzyme a: S24 (≠ K25), R25 (≠ S26), R26 (≠ L27), A28 (= A29), A65 (= A66), D68 (≠ E69), L69 (≠ V70), K70 (≠ R71), L110 (= L118), G111 (= G119), T134 (≠ P142), E135 (= E143), L138 (≠ I146), R168 (≠ Q175)
6z1pBI mS93 (see paper)
28% identity, 45% coverage: 16:180/370 of query aligns to 32:194/1413 of 6z1pBI
- active site: T85 (≠ G68), S134 (≠ G120), E157 (= E143), D165 (= D151)
- binding : Y41 (≠ K25), K42 (≠ S26), Q43 (≠ L27), T45 (≠ A29), D47 (≠ S31), H49 (≠ P33), K83 (≠ A66), T85 (≠ G68), D86 (≠ E69), F87 (≠ V70), K88 (≠ R71), K92 (≠ E75), L130 (≠ Y116), K152 (≠ R138)
Sites not aligning to the query:
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
29% identity, 46% coverage: 4:174/370 of query aligns to 13:176/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
P21177 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Escherichia coli (strain K12) (see 2 papers)
28% identity, 50% coverage: 17:202/370 of query aligns to 16:196/729 of P21177
- G116 (= G120) mutation to F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected.
Sites not aligning to the query:
- 322 G→A: 10-fold increase in KM for NADH.
- 450 active site, For 3-hydroxyacyl-CoA dehydrogenase activity; mutation H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
28% identity, 50% coverage: 17:202/370 of query aligns to 16:196/719 of 6tnmA
Sites not aligning to the query:
6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
27% identity, 48% coverage: 13:191/370 of query aligns to 864:1029/1804 of 6eqoA
Sites not aligning to the query:
- binding phosphomethylphosphonic acid adenylate ester: 456, 458, 535, 536, 537, 538, 558, 559, 560, 561, 562, 688, 714
- binding nadp nicotinamide-adenine-dinucleotide phosphate: 1261, 1265, 1379, 1400, 1403, 1404, 1405, 1424, 1425, 1429, 1444, 1492, 1493, 1497, 1514, 1517, 1713, 1730, 1731, 1774
Query Sequence
>AO353_17555 FitnessBrowser__pseudo3_N2E3:AO353_17555
MNLHFEELTGTDGARIGIASLDAEKSLNALSLPMIRALSDQLEAWAKEPQIVCVLLRGNG
AKAFCAGGEVRNLVEACRAHPGEVPPLAAQFFSAEYRLDFRLHTYPKPLICWGHGYVLGG
GLGLLQGASIRIVTPSSRLAMPEISIGLYPDVGASWFLSRLPGKLGLFLGLTGAQMNARD
AIDLDLADRFLLDEQQEELIEGLLQLNWQEQTPMQLNSLLKALQQEAVGKMPEAQWLPRR
QQIDELLDVSDVRCAWRAISLLRDHRDLLLARAAKNLHEGCPLTAHLVWEQIQRARHLSL
AEVFQMEYTMSLNCCRHPEFSEGVRARLIDKDQKPHWHWPDINAIPEAVVQAHFHKVWEG
RHPLADLSGY
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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