SitesBLAST
Comparing Pf1N1B4_3308 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3308 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
34% identity, 95% coverage: 7:358/371 of query aligns to 6:348/362 of 3bptA
- active site: G67 (= G69), P84 (= P87), R88 (≠ A94), G115 (= G121), G118 (= G124), E138 (= E144), D146 (= D152)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G68), G67 (= G69), I69 (≠ V71), E90 (= E96), G114 (= G120), G115 (= G121), E138 (= E144), D146 (= D152), V147 (= V153)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ S27), L26 (= L28), A28 (= A30), G66 (= G68), G67 (= G69), I69 (≠ V71), P137 (= P143), I141 (= I147), L319 (= L329)
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)
32% identity, 93% coverage: 13:358/371 of query aligns to 15:356/378 of Q9LKJ1
- G70 (= G69) mutation to S: Loss of activity.
- E142 (= E144) mutation to A: Loss of activity.
- D150 (= D152) mutation to G: Reduced activity.
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
35% identity, 92% coverage: 17:358/371 of query aligns to 12:331/340 of 4hdtA
- active site: G64 (= G69), I69 (≠ L74), W84 (≠ F93), Y88 (= Y97), G112 (= G121), G115 (= G124), E135 (= E144), P142 (= P151), D143 (= D152), R283 (≠ Q306)
- binding zinc ion: H28 (≠ L33), E42 (≠ A47), E57 (≠ T62), E79 (= E84), H93 (≠ N102), H185 (≠ D194)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
29% identity, 51% coverage: 4:192/371 of query aligns to 1:182/259 of 5zaiC
- active site: A65 (≠ G69), F70 (≠ L74), S82 (≠ A94), R86 (= R98), G110 (= G121), E113 (≠ G124), P132 (= P143), E133 (= E144), I138 (≠ L149), P140 (= P151), G141 (≠ D152)
- binding coenzyme a: K24 (≠ S27), L25 (= L28), A63 (= A67), G64 (= G68), A65 (≠ G69), D66 (≠ E70), I67 (≠ V71), P132 (= P143), R166 (≠ Q176)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
29% identity, 49% coverage: 16:195/371 of query aligns to 12:182/256 of 3h81A
- active site: A64 (≠ G69), M69 (≠ L74), T79 (≠ A89), F83 (= F93), G107 (= G121), E110 (≠ G124), P129 (= P143), E130 (= E144), V135 (≠ L149), P137 (= P151), G138 (≠ D152)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
29% identity, 49% coverage: 16:195/371 of query aligns to 13:183/255 of 3q0jC
- active site: A65 (≠ G69), M70 (≠ L74), T80 (≠ A89), F84 (= F93), G108 (= G121), E111 (≠ G124), P130 (= P143), E131 (= E144), V136 (≠ L149), P138 (= P151), G139 (≠ D152)
- binding acetoacetyl-coenzyme a: Q23 (≠ K26), A24 (≠ S27), L25 (= L28), A27 (= A30), A63 (= A67), G64 (= G68), A65 (≠ G69), D66 (≠ E70), I67 (≠ V71), K68 (≠ R72), M70 (≠ L74), F84 (= F93), G107 (= G120), G108 (= G121), E111 (≠ G124), P130 (= P143), E131 (= E144), P138 (= P151), G139 (≠ D152), M140 (≠ V153)
Sites not aligning to the query:
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 49% coverage: 16:195/371 of query aligns to 13:183/255 of 3q0gC
- active site: A65 (≠ G69), M70 (≠ L74), T80 (≠ A89), F84 (= F93), G108 (= G121), E111 (≠ G124), P130 (= P143), E131 (= E144), V136 (≠ L149), P138 (= P151), G139 (≠ D152)
- binding coenzyme a: L25 (= L28), A63 (= A67), I67 (≠ V71), K68 (≠ R72), Y104 (= Y117), P130 (= P143), E131 (= E144), L134 (≠ I147)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 49% coverage: 16:195/371 of query aligns to 12:178/250 of 3q0gD
- active site: A64 (≠ G69), M69 (≠ L74), T75 (≠ A89), F79 (= F93), G103 (= G121), E106 (≠ G124), P125 (= P143), E126 (= E144), V131 (≠ L149), P133 (= P151), G134 (≠ D152)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
30% identity, 47% coverage: 17:191/371 of query aligns to 17:182/260 of 2hw5C
- active site: A68 (≠ G69), M73 (≠ V85), S83 (≠ R98), L87 (vs. gap), G111 (= G121), E114 (≠ G124), P133 (= P143), E134 (= E144), T139 (≠ L149), P141 (= P151), G142 (≠ D152)
- binding crotonyl coenzyme a: K26 (= K26), A27 (≠ S27), L28 (= L28), A30 (= A30), K62 (= K63), I70 (≠ V71), F109 (≠ L119)
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)
28% identity, 48% coverage: 15:192/371 of query aligns to 45:213/290 of P14604
- E144 (≠ G124) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E144) 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)
28% identity, 48% coverage: 15:192/371 of query aligns to 15:183/260 of 1dubA
- active site: A68 (≠ G69), M73 (≠ L74), S83 (≠ R98), L87 (≠ N102), G111 (= G121), E114 (≠ G124), P133 (= P143), E134 (= E144), T139 (≠ L149), P141 (= P151), G142 (≠ D152)
- binding acetoacetyl-coenzyme a: K26 (= K26), A27 (≠ S27), L28 (= L28), A30 (= A30), A66 (= A67), A68 (≠ G69), D69 (≠ E70), I70 (≠ V71), Y107 (= Y117), G110 (= G120), G111 (= G121), E114 (≠ G124), P133 (= P143), E134 (= E144), L137 (≠ I147), G142 (≠ D152)
Sites not aligning to the query:
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
28% identity, 48% coverage: 15:192/371 of query aligns to 13:181/258 of 1ey3A
- active site: A66 (≠ G69), M71 (≠ L74), S81 (≠ R98), L85 (≠ N102), G109 (= G121), E112 (≠ G124), P131 (= P143), E132 (= E144), T137 (≠ L149), P139 (= P151), G140 (≠ D152)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K26), L26 (= L28), A28 (= A30), A64 (= A67), G65 (= G68), A66 (≠ G69), D67 (≠ E70), I68 (≠ V71), L85 (≠ N102), W88 (vs. gap), G109 (= G121), P131 (= P143), L135 (≠ I147), G140 (≠ D152)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
27% identity, 48% coverage: 15:192/371 of query aligns to 14:177/254 of 2dubA
- active site: A67 (≠ G69), M72 (≠ L74), S82 (≠ R98), G105 (= G121), E108 (≠ G124), P127 (= P143), E128 (= E144), T133 (≠ L149), P135 (= P151), G136 (≠ D152)
- binding octanoyl-coenzyme a: K25 (= K26), A26 (≠ S27), L27 (= L28), A29 (= A30), A65 (= A67), A67 (≠ G69), D68 (≠ E70), I69 (≠ V71), K70 (≠ R72), G105 (= G121), E108 (≠ G124), P127 (= P143), E128 (= E144), G136 (≠ D152), A137 (≠ V153)
Sites not aligning to the query:
6z1pBI mS93 (see paper)
28% identity, 56% coverage: 17:222/371 of query aligns to 32:237/1413 of 6z1pBI
- active site: T85 (≠ G69), S134 (≠ G121), E157 (= E144), D165 (= D152)
- binding : Y41 (≠ K26), K42 (≠ S27), Q43 (≠ L28), T45 (≠ A30), D47 (≠ S32), H49 (≠ P34), K83 (≠ A67), T85 (≠ G69), D86 (≠ E70), F87 (≠ V71), K88 (≠ R72), K92 (≠ R79), L130 (≠ Y117), K152 (≠ R139)
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)
28% identity, 49% coverage: 14:195/371 of query aligns to 864:1032/1804 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
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
28% identity, 46% coverage: 21:191/371 of query aligns to 19:183/261 of 5jbxB
- active site: A67 (≠ G69), R72 (= R79), L84 (≠ F93), R88 (≠ Y97), G112 (= G121), E115 (≠ G124), T134 (≠ P143), E135 (= E144), I140 (≠ L149), P142 (= P151), G143 (≠ D152)
- binding coenzyme a: S24 (≠ K26), R25 (≠ S27), R26 (≠ L28), A28 (= A30), A65 (= A67), D68 (≠ E70), L69 (≠ V71), K70 (≠ R72), L110 (= L119), G111 (= G120), T134 (≠ P143), E135 (= E144), L138 (≠ I147), R168 (≠ Q176)
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: 5:175/371 of query aligns to 13:176/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
30% identity, 48% coverage: 19:196/371 of query aligns to 20:193/266 of O53561
- K135 (≠ R139) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 139:146, 13% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ G146) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
25% identity, 55% coverage: 18:220/371 of query aligns to 16:222/719 of 6tnmA
Sites not aligning to the query:
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)
25% identity, 55% coverage: 18:220/371 of query aligns to 16:222/729 of P21177
- G116 (= G121) 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.
Query Sequence
>Pf1N1B4_3308 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_3308
MMNLHFEELTGTDGARIGIASLDAEKSLNALSLPMINALRDQLDAWAKEPQIVCVLLRGN
GTKAFCAGGEVRSLVEACRALPGEVPPLAAHFFAAEYRLDFNLHTYPKPLICWGHGYVLG
GGMGLLQGASIRIVTPSSRLAMPEIGIGLYPDVGASWFLSRLPGKLGLFLGLTGAQMNGR
DAIDLDLADRFLRDDQQHELIEGLLQLNWQEQTAMQLNSLLKALQQEAIAQMPQAQWLPR
RELIDELLDVSDVRCAWKAISALRDHSDPLLGRAAKTMAEGSPLTAHLVWEQIVRARHLS
LAQVFQMEYTMSLNCCRHPEFSEGVRARLIDKDHKPHWHWPDINNVPEAAVEAHFRKVWE
GRHPLADLSEY
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