SitesBLAST
Comparing GFF3468 FitnessBrowser__Marino:GFF3468 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)
3bptA Crystal structure of human beta-hydroxyisobutyryl-coa hydrolase in complex with quercetin
33% identity, 95% coverage: 6:353/367 of query aligns to 6:345/362 of 3bptA
- active site: G67 (= G67), P84 (= P85), R88 (≠ S90), G115 (= G117), G118 (= G120), E138 (= E140), D146 (= D148)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G66), G67 (= G67), I69 (= I69), E90 (= E92), G114 (= G116), G115 (= G117), E138 (= E140), D146 (= D148), V147 (= V149)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ T25), L26 (= L26), A28 (= A28), G66 (= G66), G67 (= G67), I69 (= I69), P137 (= P139), I141 (= I143), L319 (≠ A327)
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)
33% identity, 96% coverage: 1:353/367 of query aligns to 5:353/378 of Q9LKJ1
- G70 (= G67) mutation to S: Loss of activity.
- E142 (= E140) mutation to A: Loss of activity.
- D150 (= D148) mutation to G: Reduced activity.
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
36% identity, 94% coverage: 12:355/367 of query aligns to 9:330/340 of 4hdtA
- active site: G64 (= G67), I69 (≠ L72), W84 (≠ F89), Y88 (= Y93), G112 (= G117), G115 (= G120), E135 (= E140), P142 (= P147), D143 (= D148), R283 (= R304)
- binding zinc ion: H28 (≠ E31), E42 (≠ A45), E57 (= E60), E79 (= E81), H93 (≠ N98), H185 (≠ P190)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
29% identity, 53% coverage: 11:203/367 of query aligns to 10:201/259 of 5zaiC
- active site: A65 (≠ G67), F70 (≠ L72), S82 (≠ F89), R86 (≠ Y93), G110 (= G117), E113 (≠ G120), P132 (= P139), E133 (= E140), I138 (≠ L145), P140 (= P147), G141 (≠ D148)
- binding coenzyme a: K24 (≠ T25), L25 (= L26), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (= I69), P132 (= P139), R166 (= R172)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 49% coverage: 11:190/367 of query aligns to 12:178/254 of 2dubA
- active site: A67 (≠ G67), M72 (≠ L72), S82 (≠ R94), G105 (= G117), E108 (≠ G120), P127 (= P139), E128 (= E140), T133 (≠ L145), P135 (= P147), G136 (≠ D148)
- binding octanoyl-coenzyme a: K25 (≠ G24), A26 (≠ T25), L27 (= L26), A29 (= A28), A65 (= A65), A67 (≠ G67), D68 (= D68), I69 (= I69), K70 (≠ R70), G105 (= G117), E108 (≠ G120), P127 (= P139), E128 (= E140), G136 (≠ D148), A137 (≠ V149)
Sites not aligning to the query:
6z1pBI mS93 (see paper)
30% identity, 48% coverage: 8:184/367 of query aligns to 25:201/1413 of 6z1pBI
- active site: T85 (≠ G67), S134 (≠ G117), E157 (= E140), D165 (= D148)
- binding : Y41 (≠ G24), K42 (≠ T25), Q43 (≠ L26), T45 (≠ A28), D47 (≠ S30), H49 (= H32), K83 (≠ A65), T85 (≠ G67), D86 (= D68), F87 (≠ I69), K88 (≠ R70), K92 (≠ D74), L130 (≠ V113), K152 (≠ T135)
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)
30% identity, 47% coverage: 11:183/367 of query aligns to 43:208/290 of P14604
- E144 (≠ G120) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E140) 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
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
30% identity, 49% coverage: 11:190/367 of query aligns to 11:182/258 of 1ey3A
- active site: A66 (≠ G67), M71 (≠ L72), S81 (≠ R94), L85 (vs. gap), G109 (= G117), E112 (≠ G120), P131 (= P139), E132 (= E140), T137 (≠ L145), P139 (= P147), G140 (≠ D148)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ G24), L26 (= L26), A28 (= A28), A64 (= A65), G65 (= G66), A66 (≠ G67), D67 (= D68), I68 (= I69), L85 (vs. gap), W88 (vs. gap), G109 (= G117), P131 (= P139), L135 (≠ I143), G140 (≠ D148)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
30% identity, 47% coverage: 11:183/367 of query aligns to 13:178/260 of 1dubA
- active site: A68 (≠ G67), M73 (≠ L72), S83 (≠ R94), L87 (vs. gap), G111 (= G117), E114 (≠ G120), P133 (= P139), E134 (= E140), T139 (≠ L145), P141 (= P147), G142 (≠ D148)
- binding acetoacetyl-coenzyme a: K26 (≠ G24), A27 (≠ T25), L28 (= L26), A30 (= A28), A66 (= A65), A68 (≠ G67), D69 (= D68), I70 (= I69), Y107 (≠ V113), G110 (= G116), G111 (= G117), E114 (≠ G120), P133 (= P139), E134 (= E140), L137 (≠ I143), G142 (≠ D148)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 47% coverage: 11:183/367 of query aligns to 13:176/258 of 1mj3A
- active site: A68 (≠ G67), M73 (≠ L72), S83 (≠ R94), L85 (≠ M95), G109 (= G117), E112 (≠ G120), P131 (= P139), E132 (= E140), T137 (≠ L145), P139 (= P147), G140 (≠ D148)
- binding hexanoyl-coenzyme a: K26 (≠ G24), A27 (≠ T25), L28 (= L26), A30 (= A28), A66 (= A65), G67 (= G66), A68 (≠ G67), D69 (= D68), I70 (= I69), G109 (= G117), P131 (= P139), E132 (= E140), L135 (≠ I143), G140 (≠ D148)
Sites not aligning to the query:
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
30% identity, 47% coverage: 13:185/367 of query aligns to 13:181/261 of 5jbxB
- active site: A67 (≠ G67), R72 (≠ D78), L84 (≠ S90), R88 (= R94), G112 (= G117), E115 (≠ G120), T134 (≠ P139), E135 (= E140), I140 (≠ L145), P142 (= P147), G143 (≠ D148)
- binding coenzyme a: S24 (≠ G24), R25 (≠ T25), R26 (≠ L26), A28 (= A28), A65 (= A65), D68 (= D68), L69 (≠ I69), K70 (≠ R70), L110 (≠ M115), G111 (= G116), T134 (≠ P139), E135 (= E140), L138 (≠ I143), R168 (= R172)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
27% identity, 52% coverage: 11:202/367 of query aligns to 13:201/260 of 2hw5C
- active site: A68 (≠ G67), M73 (≠ L72), S83 (≠ P82), L87 (≠ V86), G111 (= G117), E114 (≠ G120), P133 (= P139), E134 (= E140), T139 (≠ L145), P141 (= P147), G142 (≠ D148)
- binding crotonyl coenzyme a: K26 (≠ G24), A27 (≠ T25), L28 (= L26), A30 (= A28), K62 (≠ R61), I70 (= I69), F109 (≠ M115)
Sites not aligning to the query:
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
31% identity, 49% coverage: 8:185/367 of query aligns to 6:183/707 of 6yswA
- active site: A66 (≠ G67), I71 (≠ L72), A84 (≠ V86), Q88 (≠ Y93), G112 (= G117), E115 (≠ G120), P136 (= P139), E137 (= E140), G145 (≠ D148)
- binding coenzyme a: E23 (vs. gap), M25 (≠ L26), A66 (≠ G67), D67 (= D68), I68 (= I69), P136 (= P139), E137 (= E140), L140 (≠ I143)
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)
30% identity, 43% coverage: 15:172/367 of query aligns to 867:1017/1804 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
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
25% identity, 57% coverage: 11:218/367 of query aligns to 10:208/255 of 3q0jC
- active site: A65 (≠ G67), M70 (≠ L72), T80 (≠ R94), F84 (vs. gap), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), V136 (≠ L145), P138 (= P147), G139 (≠ D148)
- binding acetoacetyl-coenzyme a: Q23 (≠ G24), A24 (≠ T25), L25 (= L26), A27 (= A28), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (= I69), K68 (≠ R70), M70 (≠ L72), F84 (vs. gap), G107 (= G116), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), P138 (= P147), G139 (≠ D148), M140 (≠ V149)
Sites not aligning to the query:
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
25% identity, 57% coverage: 11:218/367 of query aligns to 10:208/255 of 3q0gC
- active site: A65 (≠ G67), M70 (≠ L72), T80 (≠ R94), F84 (vs. gap), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), V136 (≠ L145), P138 (= P147), G139 (≠ D148)
- binding coenzyme a: L25 (= L26), A63 (= A65), I67 (= I69), K68 (≠ R70), Y104 (≠ V113), P130 (= P139), E131 (= E140), L134 (≠ I143)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
25% identity, 57% coverage: 11:218/367 of query aligns to 9:207/256 of 3h81A
- active site: A64 (≠ G67), M69 (≠ L72), T79 (≠ R94), F83 (vs. gap), G107 (= G117), E110 (≠ G120), P129 (= P139), E130 (= E140), V135 (≠ L145), P137 (= P147), G138 (≠ D148)
Sites not aligning to the query:
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)
30% identity, 47% coverage: 15:188/367 of query aligns to 11:173/723 of Q08426
- V40 (≠ A45) to G: in dbSNP:rs1062551
- I41 (≠ N46) to R: in dbSNP:rs1062552
- T75 (≠ R91) to I: in dbSNP:rs1062553
- K165 (≠ R180) 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 (≠ M186) 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
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
33% identity, 41% coverage: 15:164/367 of query aligns to 10:145/692 of 6iunB
Sites not aligning to the query:
- active site: 248, 407, 428, 440, 478
- binding nicotinamide-adenine-dinucleotide: 300, 301, 302, 321, 322, 365, 377, 378, 380, 384, 388, 405, 407
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
29% identity, 44% coverage: 4:163/367 of query aligns to 55:216/327 of Q62651
- D176 (≠ G120) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E140) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (= D148) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
Query Sequence
>GFF3468 FitnessBrowser__Marino:GFF3468
MSVEAEELACREGHMGVLTLNSPGTLNALSEHMIEQIQDILDRWANDDRICIVVIQGAGE
RAFCAGGDIRELYDAILDGQEPEKPVRFFSREYRMDYNIHRFPKPVLGIAHGVVMGGGLG
VFSGCRYRLVTPDVTLAMPEITIGLFPDVGASWFLKRLPGRLGLFMGLTGARLNVSDTLR
VGLADMAILPEDRDRLLDRLASERWTGQTAADDNRLFRLLNQIQTPDYRTLPPSHLARHE
QRIARLSAGDELPDIVDQLLAAEVDCDWWHACMNTLRNGCPVSAWLVWTQLQKAQQMSLK
DAFRMELAMVSECIRRPDLTEGIRALAIDKDRQPKWSYPSVADVPEDVVAAHFTPEWDDE
TDPMGLE
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