SitesBLAST
Comparing GFF930 FitnessBrowser__Marino:GFF930 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
38% identity, 97% coverage: 9:355/356 of query aligns to 5:345/362 of 3bptA
- active site: G67 (= G71), P84 (vs. gap), R88 (≠ T94), G115 (= G121), G118 (= G124), E138 (= E144), D146 (= D152)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G70), G67 (= G71), I69 (= I73), E90 (= E96), G114 (= G120), G115 (= G121), E138 (= E144), D146 (= D152), V147 (= V153)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ A29), L26 (= L30), A28 (≠ S32), G66 (= G70), G67 (= G71), I69 (= I73), 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)
34% identity, 100% coverage: 1:355/356 of query aligns to 5:353/378 of Q9LKJ1
- G70 (= G71) 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)
36% identity, 94% coverage: 24:356/356 of query aligns to 17:329/340 of 4hdtA
- active site: G64 (= G71), I69 (≠ L76), W84 (≠ F93), Y88 (= Y97), G112 (= G121), G115 (= G124), E135 (= E144), P142 (= P151), D143 (= D152), R283 (≠ D306)
- binding zinc ion: H28 (≠ L35), E42 (≠ A49), E57 (≠ D64), E79 (= E88), H93 (≠ L102), H185 (= H194)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
31% identity, 47% coverage: 24:192/356 of query aligns to 19:182/259 of 5zaiC
- active site: A65 (≠ G71), F70 (≠ Y77), S82 (≠ F93), R86 (≠ Y97), G110 (= G121), E113 (≠ G124), P132 (= P143), E133 (= E144), I138 (≠ L149), P140 (= P151), G141 (≠ D152)
- binding coenzyme a: K24 (≠ A29), L25 (= L30), A63 (= A69), G64 (= G70), A65 (≠ G71), D66 (= D72), I67 (= I73), P132 (= P143), R166 (= R176)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
32% identity, 51% coverage: 12:191/356 of query aligns to 10:182/260 of 2hw5C
- active site: A68 (≠ G71), M73 (≠ P83), S83 (≠ E98), L87 (= L102), G111 (= G121), E114 (≠ G124), P133 (= P143), E134 (= E144), T139 (≠ L149), P141 (= P151), G142 (≠ D152)
- binding crotonyl coenzyme a: K26 (= K28), A27 (= A29), L28 (= L30), A30 (≠ S32), K62 (= K65), I70 (= I73), F109 (≠ M119)
Sites not aligning to the query:
6z1pBI mS93 (see paper)
29% identity, 50% coverage: 12:188/356 of query aligns to 28:201/1413 of 6z1pBI
- active site: T85 (≠ G71), S134 (≠ G121), E157 (= E144), D165 (= D152)
- binding : Y41 (≠ K28), K42 (≠ A29), Q43 (≠ L30), T45 (≠ S32), D47 (≠ S34), H49 (≠ E36), K83 (≠ A69), T85 (≠ G71), D86 (= D72), F87 (≠ I73), K88 (≠ V74), K92 (≠ R78), L130 (≠ I117), K152 (= K139)
Sites not aligning to the query:
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
29% identity, 57% coverage: 19:222/356 of query aligns to 13:216/707 of 6yswA
- active site: A66 (≠ G71), I71 (≠ L76), A84 (≠ F93), Q88 (≠ Y97), G112 (= G121), E115 (≠ G124), P136 (= P143), E137 (= E144), G145 (≠ D152)
- binding coenzyme a: E23 (≠ K28), M25 (≠ L30), A66 (≠ G71), D67 (= D72), I68 (= I73), P136 (= P143), E137 (= E144), L140 (≠ I147)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
30% identity, 53% coverage: 4:192/356 of query aligns to 4:183/260 of 1dubA
- active site: A68 (≠ G71), M73 (≠ P83), S83 (≠ E98), L87 (= L102), G111 (= G121), E114 (≠ G124), P133 (= P143), E134 (= E144), T139 (≠ L149), P141 (= P151), G142 (≠ D152)
- binding acetoacetyl-coenzyme a: K26 (= K28), A27 (= A29), L28 (= L30), A30 (≠ S32), A66 (= A69), A68 (≠ G71), D69 (= D72), I70 (= I73), Y107 (≠ I117), 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)
30% identity, 53% coverage: 4:192/356 of query aligns to 2:181/258 of 1ey3A
- active site: A66 (≠ G71), M71 (≠ P83), S81 (≠ E98), L85 (= L102), G109 (= G121), E112 (≠ G124), P131 (= P143), E132 (= E144), T137 (≠ L149), P139 (= P151), G140 (≠ D152)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K28), L26 (= L30), A28 (≠ S32), A64 (= A69), G65 (= G70), A66 (≠ G71), D67 (= D72), I68 (= I73), L85 (= L102), W88 (vs. gap), G109 (= G121), P131 (= P143), L135 (≠ I147), G140 (≠ D152)
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, 53% coverage: 4:192/356 of query aligns to 34:213/290 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
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 53% coverage: 4:191/356 of query aligns to 3:176/254 of 2dubA
- active site: A67 (≠ G71), M72 (≠ P83), S82 (≠ E98), G105 (= G121), E108 (≠ G124), P127 (= P143), E128 (= E144), T133 (≠ L149), P135 (= P151), G136 (≠ D152)
- binding octanoyl-coenzyme a: K25 (= K28), A26 (= A29), L27 (= L30), A29 (≠ S32), A65 (= A69), A67 (≠ G71), D68 (= D72), I69 (= I73), K70 (≠ T81), G105 (= G121), E108 (≠ G124), P127 (= P143), E128 (= E144), G136 (≠ D152), A137 (≠ V153)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
30% identity, 53% coverage: 4:191/356 of query aligns to 4:180/258 of 1mj3A
- active site: A68 (≠ G71), M73 (≠ L76), S83 (≠ E98), L85 (= L99), G109 (= G121), E112 (≠ G124), P131 (= P143), E132 (= E144), T137 (≠ L149), P139 (= P151), G140 (≠ D152)
- binding hexanoyl-coenzyme a: K26 (= K28), A27 (= A29), L28 (= L30), A30 (≠ S32), A66 (= A69), G67 (= G70), A68 (≠ G71), D69 (= D72), I70 (= I73), G109 (= G121), P131 (= P143), E132 (= E144), L135 (≠ I147), G140 (≠ D152)
Sites not aligning to the query:
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
27% identity, 44% coverage: 10:164/356 of query aligns to 3:144/692 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
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
25% identity, 50% coverage: 19:195/356 of query aligns to 13:178/250 of 3q0gD
- active site: A64 (≠ G71), M69 (≠ L76), T75 (≠ F93), F79 (≠ Y97), G103 (= G121), E106 (≠ G124), P125 (= P143), E126 (= E144), V131 (≠ L149), P133 (= P151), G134 (≠ D152)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
25% identity, 50% coverage: 19:195/356 of query aligns to 14:183/255 of 3q0jC
- active site: A65 (≠ G71), M70 (≠ L76), T80 (≠ E98), F84 (≠ L102), G108 (= G121), E111 (≠ G124), P130 (= P143), E131 (= E144), V136 (≠ L149), P138 (= P151), G139 (≠ D152)
- binding acetoacetyl-coenzyme a: Q23 (≠ K28), A24 (= A29), L25 (= L30), A27 (≠ S32), A63 (= A69), G64 (= G70), A65 (≠ G71), D66 (= D72), I67 (= I73), K68 (≠ V74), M70 (≠ L76), F84 (≠ L102), 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
25% identity, 50% coverage: 19:195/356 of query aligns to 14:183/255 of 3q0gC
- active site: A65 (≠ G71), M70 (≠ L76), T80 (≠ E98), F84 (≠ L102), G108 (= G121), E111 (≠ G124), P130 (= P143), E131 (= E144), V136 (≠ L149), P138 (= P151), G139 (≠ D152)
- binding coenzyme a: L25 (= L30), A63 (= A69), I67 (= I73), K68 (≠ V74), Y104 (≠ I117), P130 (= P143), E131 (= E144), L134 (≠ I147)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
25% identity, 50% coverage: 19:195/356 of query aligns to 13:182/256 of 3h81A
- active site: A64 (≠ G71), M69 (≠ L76), T79 (≠ E98), F83 (≠ L102), G107 (= G121), E110 (≠ G124), P129 (= P143), E130 (= E144), V135 (≠ L149), P137 (= P151), G138 (≠ D152)
Sites not aligning to the query:
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
30% identity, 45% coverage: 31:191/356 of query aligns to 27:183/261 of 5jbxB
- active site: A67 (≠ G71), R72 (≠ Y77), L84 (= L99), R88 (≠ I103), G112 (= G121), E115 (≠ G124), T134 (≠ P143), E135 (= E144), I140 (≠ L149), P142 (= P151), G143 (≠ D152)
- binding coenzyme a: A28 (≠ S32), A65 (= A69), D68 (= D72), L69 (≠ I73), K70 (≠ V74), L110 (≠ M119), G111 (= G120), T134 (≠ P143), E135 (= E144), L138 (≠ I147), R168 (= R176)
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)
26% identity, 50% coverage: 19:195/356 of query aligns to 11:176/723 of Q08426
- V40 (≠ A49) to G: in dbSNP:rs1062551
- I41 (≠ E50) to R: in dbSNP:rs1062552
- T75 (≠ G89) to I: in dbSNP:rs1062553
- K165 (≠ F184) 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 (≠ R190) 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
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
27% identity, 58% coverage: 6:211/356 of query aligns to 4:199/257 of 6slbAAA
- active site: Q64 (≠ G71), F69 (≠ L76), L80 (≠ F93), N84 (≠ Y97), A108 (≠ G121), S111 (≠ G124), A130 (≠ P143), F131 (≠ E144), L136 (= L149), P138 (= P151), D139 (= D152)
- binding (~{E})-6-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-6-oxidanylidene-hex-3-enoic acid: R58 (≠ K65), A62 (= A69), Q64 (≠ G71), D65 (= D72), L66 (≠ I73), Y76 (≠ G89), A108 (≠ G121), F131 (≠ E144), D139 (= D152)
Sites not aligning to the query:
Query Sequence
>GFF930 FitnessBrowser__Marino:GFF930
MSDQPIIFEEWKTGDGALIAVARLNTPKALNSLSLEMIRLLTPQLKRWAEDPVIQAVWLE
SEGDKAFCAGGDIVALYRSMTEPQGASEGEAFFTEEYELDYLIHTFPKPLVCWGHGIVMG
GGMGIMEGASHRVVTEGSKLAMPEITIGLYPDVAAGWFLNRTPGRTGLFLGLTGARLNGA
DAIFTGLADRFIRHDLKADVIAELCKRNWQGEDPHAVVGSVLRRYERESADAMPESPVRT
HFDEINRVTDADSLEATVNQLKELSGGDGWVAKATRSLAGASPTSLALVWRHLHGCKHDS
LKEVLDKELVLSTKCLTKGEFAEGIRALLIDKDQQPRWRYASLAEMDSAWIDDFFS
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