SitesBLAST
Comparing GFF2712 FitnessBrowser__WCS417:GFF2712 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
38% identity, 94% coverage: 17:362/367 of query aligns to 5:348/362 of 3bptA
- active site: G67 (= G79), P84 (≠ Q96), R88 (≠ V100), G115 (= G127), G118 (= G130), E138 (= E150), D146 (= D158)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G78), G67 (= G79), I69 (= I81), E90 (= E102), G114 (= G126), G115 (= G127), E138 (= E150), D146 (= D158), V147 (= V159)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ G37), L26 (= L38), A28 (= A40), G66 (= G78), G67 (= G79), I69 (= I81), P137 (= P149), I141 (= I153), L319 (≠ I333)
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, 95% coverage: 16:364/367 of query aligns to 8:358/378 of Q9LKJ1
- G70 (= G79) mutation to S: Loss of activity.
- E142 (= E150) mutation to A: Loss of activity.
- D150 (= D158) mutation to G: Reduced activity.
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
39% identity, 94% coverage: 16:359/367 of query aligns to 1:328/340 of 4hdtA
- active site: G64 (= G79), I69 (≠ L84), W84 (≠ F99), Y88 (= Y103), G112 (= G127), G115 (= G130), E135 (= E150), P142 (= P157), D143 (= D158), R283 (≠ A310)
- binding zinc ion: H28 (≠ L43), E42 (≠ A57), E57 (= E72), E79 (≠ L94), H93 (≠ A108), H185 (≠ S200)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 48% coverage: 19:193/367 of query aligns to 6:178/260 of 2hw5C
- active site: A68 (≠ G79), M73 (≠ L84), S83 (≠ V100), L87 (≠ I109), G111 (= G127), E114 (≠ G130), P133 (= P149), E134 (= E150), T139 (≠ Y155), P141 (= P157), G142 (≠ D158)
- binding crotonyl coenzyme a: K26 (≠ A36), A27 (≠ G37), L28 (= L38), A30 (= A40), K62 (= K73), I70 (= I81), F109 (≠ L125)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 46% coverage: 24:193/367 of query aligns to 14:178/260 of 1dubA
- active site: A68 (≠ G79), M73 (vs. gap), S83 (≠ K89), L87 (≠ T93), G111 (= G127), E114 (≠ G130), P133 (= P149), E134 (= E150), T139 (≠ Y155), P141 (= P157), G142 (≠ D158)
- binding acetoacetyl-coenzyme a: K26 (≠ A36), A27 (≠ G37), L28 (= L38), A30 (= A40), A66 (= A77), A68 (≠ G79), D69 (= D80), I70 (= I81), Y107 (≠ F123), G110 (= G126), G111 (= G127), E114 (≠ G130), P133 (= P149), E134 (= E150), L137 (≠ I153), G142 (≠ D158)
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)
35% identity, 46% coverage: 25:193/367 of query aligns to 45:208/290 of P14604
- E144 (≠ G130) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E150) 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)
35% identity, 46% coverage: 24:193/367 of query aligns to 12:176/258 of 1ey3A
- active site: A66 (≠ G79), M71 (vs. gap), S81 (≠ K89), L85 (≠ T93), G109 (= G127), E112 (≠ G130), P131 (= P149), E132 (= E150), T137 (≠ Y155), P139 (= P157), G140 (≠ D158)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A36), L26 (= L38), A28 (= A40), A64 (= A77), G65 (= G78), A66 (≠ G79), D67 (= D80), I68 (= I81), L85 (≠ T93), W88 (≠ Q96), G109 (= G127), P131 (= P149), L135 (≠ I153), G140 (≠ D158)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
35% identity, 46% coverage: 24:193/367 of query aligns to 13:172/254 of 2dubA
- active site: A67 (≠ G79), M72 (≠ L84), S82 (≠ L94), G105 (= G127), E108 (≠ G130), P127 (= P149), E128 (= E150), T133 (≠ Y155), P135 (= P157), G136 (≠ D158)
- binding octanoyl-coenzyme a: K25 (≠ A36), A26 (≠ G37), L27 (= L38), A29 (= A40), A65 (= A77), A67 (≠ G79), D68 (= D80), I69 (= I81), K70 (≠ R82), G105 (= G127), E108 (≠ G130), P127 (= P149), E128 (= E150), G136 (≠ D158), A137 (≠ V159)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
35% identity, 46% coverage: 24:193/367 of query aligns to 14:176/258 of 1mj3A
- active site: A68 (≠ G79), M73 (≠ L84), S83 (≠ V100), L85 (≠ E102), G109 (= G127), E112 (≠ G130), P131 (= P149), E132 (= E150), T137 (≠ Y155), P139 (= P157), G140 (≠ D158)
- binding hexanoyl-coenzyme a: K26 (≠ A36), A27 (≠ G37), L28 (= L38), A30 (= A40), A66 (= A77), G67 (= G78), A68 (≠ G79), D69 (= D80), I70 (= I81), G109 (= G127), P131 (= P149), E132 (= E150), L135 (≠ I153), G140 (≠ D158)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
29% identity, 57% coverage: 30:240/367 of query aligns to 17:221/259 of 5zaiC
- active site: A65 (≠ G79), F70 (≠ Y85), S82 (≠ F99), R86 (≠ Y103), G110 (= G127), E113 (≠ G130), P132 (= P149), E133 (= E150), I138 (≠ Y155), P140 (= P157), G141 (≠ D158)
- binding coenzyme a: K24 (≠ G37), L25 (= L38), A63 (= A77), G64 (= G78), A65 (≠ G79), D66 (= D80), I67 (= I81), P132 (= P149), R166 (≠ Q182)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
29% identity, 60% coverage: 17:235/367 of query aligns to 4:211/255 of 3q0jC
- active site: A65 (≠ G79), M70 (≠ L84), T80 (≠ H95), F84 (= F99), G108 (= G127), E111 (≠ G130), P130 (= P149), E131 (= E150), V136 (≠ Y155), P138 (= P157), G139 (≠ D158)
- binding acetoacetyl-coenzyme a: Q23 (≠ A36), A24 (≠ G37), L25 (= L38), A27 (= A40), A63 (= A77), G64 (= G78), A65 (≠ G79), D66 (= D80), I67 (= I81), K68 (≠ R82), M70 (≠ L84), F84 (= F99), G107 (= G126), G108 (= G127), E111 (≠ G130), P130 (= P149), E131 (= E150), P138 (= P157), G139 (≠ D158), M140 (≠ V159)
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, 60% coverage: 17:235/367 of query aligns to 4:211/255 of 3q0gC
- active site: A65 (≠ G79), M70 (≠ L84), T80 (≠ H95), F84 (= F99), G108 (= G127), E111 (≠ G130), P130 (= P149), E131 (= E150), V136 (≠ Y155), P138 (= P157), G139 (≠ D158)
- binding coenzyme a: L25 (= L38), A63 (= A77), I67 (= I81), K68 (≠ R82), Y104 (≠ F123), P130 (= P149), E131 (= E150), L134 (≠ I153)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
29% identity, 60% coverage: 17:235/367 of query aligns to 3:210/256 of 3h81A
- active site: A64 (≠ G79), M69 (≠ L84), T79 (≠ H95), F83 (= F99), G107 (= G127), E110 (≠ G130), P129 (= P149), E130 (= E150), V135 (≠ Y155), P137 (= P157), G138 (≠ D158)
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, 60% coverage: 17:235/367 of query aligns to 3:206/250 of 3q0gD
- active site: A64 (≠ G79), M69 (≠ L84), T75 (≠ H95), F79 (= F99), G103 (= G127), E106 (≠ G130), P125 (= P149), E126 (= E150), V131 (≠ Y155), P133 (= P157), G134 (≠ D158)
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)
32% identity, 48% coverage: 18:193/367 of query aligns to 9:184/266 of O53561
- K135 (≠ R145) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 145:152, 13% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ A152) 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)
30% identity, 58% coverage: 25:237/367 of query aligns to 9:208/723 of Q08426
- V40 (≠ A57) to G: in dbSNP:rs1062551
- I41 (≠ D58) to R: in dbSNP:rs1062552
- T75 (= T93) to I: in dbSNP:rs1062553
- K165 (≠ Y190) 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 (≠ W196) 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)
27% identity, 48% coverage: 19:194/367 of query aligns to 24:201/1413 of 6z1pBI
- active site: T85 (≠ G79), S134 (≠ G127), E157 (= E150), D165 (= D158)
- binding : Y41 (≠ A36), K42 (≠ G37), Q43 (≠ L38), T45 (≠ A40), D47 (≠ T42), H49 (≠ N44), K83 (≠ A77), T85 (≠ G79), D86 (= D80), F87 (≠ I81), K88 (≠ R82), K92 (≠ D86), L130 (≠ F123), K152 (≠ R145)
Sites not aligning to the query:
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
30% identity, 46% coverage: 38:204/367 of query aligns to 32:195/715 of 1wdlA
Sites not aligning to the query:
- active site: 430, 451, 463, 501
- binding nicotinamide-adenine-dinucleotide: 322, 324, 325, 344, 345, 400, 401, 403, 428, 429, 430
P28793 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 Pseudomonas fragi (see paper)
30% identity, 46% coverage: 38:204/367 of query aligns to 32:195/715 of P28793
Sites not aligning to the query:
- 297 binding
- 325 binding
- 344 binding
- 401:403 binding
- 408 binding
- 430 binding
- 454 binding
- 501 binding
- 660 binding
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
30% identity, 46% coverage: 38:204/367 of query aligns to 32:195/707 of 1wdmA
Sites not aligning to the query:
- active site: 430, 451, 463, 501
- binding acetyl coenzyme *a: 297, 459, 501, 534, 652, 658
- binding nicotinamide-adenine-dinucleotide: 321, 322, 324, 325, 344, 401, 403, 428, 430, 454
Query Sequence
>GFF2712 FitnessBrowser__WCS417:GFF2712
MTAQVSSEASHAETLQDEVLAEVRNHIGHLTLNRPAGLNAITLNMVRRLASQLKAWADDP
QVYAVVLRGAGEKAFCAGGDIRSLYDSFKNGDTLHQDFFVEEYALDLAIHHYRKPVLALM
DGFVLGGGMGLVQGADLRVVTERSRLAMPEVAIGYFPDVGGSYFLPRIPGELGIYLGVTG
VQIRAADALYCGLADWYLESSKLADLDNKLDRLQWHDSPLKDLQGVLAKLAVQQLPDAPL
AVLRPAIDHFFALPDVPSIVEQLQQVTVADSHEWALTTAHLMQTRSPLAMAVTLEMLRRG
RRLPLEQCFALELHLDRQWFERGDLIEGVRALIIDKDKAPRWNPPTLHGLALSHVESFFH
NFKKVAN
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