SitesBLAST
Comparing 6937209 FitnessBrowser__SB2B:6937209 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
35% identity, 95% coverage: 19:368/368 of query aligns to 16:359/362 of 3bptA
- active site: G67 (= G70), P84 (≠ K91), R88 (≠ E95), G115 (= G122), G118 (= G125), E138 (= E145), D146 (= D153)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G69), G67 (= G70), I69 (≠ V72), E90 (= E97), G114 (= G121), G115 (= G122), E138 (= E145), D146 (= D153), V147 (= V154)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ A28), L26 (= L29), A28 (= A31), G66 (= G69), G67 (= G70), I69 (≠ V72), P137 (= P144), I141 (= I148), L319 (= L328)
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
36% identity, 89% coverage: 18:345/368 of query aligns to 12:319/340 of 4hdtA
- active site: G64 (= G70), I69 (≠ L75), W84 (≠ F94), Y88 (= Y98), G112 (= G122), G115 (= G125), E135 (= E145), P142 (= P152), D143 (= D153), R283 (= R305)
- binding zinc ion: H28 (≠ L34), E42 (≠ Q48), E57 (≠ D63), E79 (≠ T86), H93 (≠ F103), H185 (≠ S195)
Sites not aligning to the query:
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, 87% coverage: 18:338/368 of query aligns to 19:337/378 of Q9LKJ1
- G70 (= G70) mutation to S: Loss of activity.
- E142 (= E145) mutation to A: Loss of activity.
- D150 (= D153) mutation to G: Reduced activity.
6z1pBI mS93 (see paper)
25% identity, 51% coverage: 3:189/368 of query aligns to 18:201/1413 of 6z1pBI
- active site: T85 (≠ G70), S134 (≠ G122), E157 (= E145), D165 (= D153)
- binding : Y41 (≠ A27), K42 (≠ A28), Q43 (≠ L29), T45 (≠ A31), D47 (= D33), H49 (≠ D35), K83 (≠ A68), T85 (≠ G70), D86 (= D71), F87 (≠ V72), K88 (≠ R73), K92 (≠ Q77), L130 (≠ I118), K152 (≠ R140)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
30% identity, 55% coverage: 7:207/368 of query aligns to 3:196/259 of 5zaiC
- active site: A65 (≠ G70), F70 (≠ L75), S82 (≠ F94), R86 (≠ Y98), G110 (= G122), E113 (≠ G125), P132 (= P144), E133 (= E145), I138 (≠ L150), P140 (= P152), G141 (≠ D153)
- binding coenzyme a: K24 (≠ A28), L25 (= L29), A63 (= A68), G64 (= G69), A65 (≠ G70), D66 (= D71), I67 (≠ V72), P132 (= P144), R166 (≠ Q177)
Sites not aligning to the query:
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
28% identity, 46% coverage: 22:192/368 of query aligns to 19:183/261 of 5jbxB
- active site: A67 (≠ G70), R72 (≠ L75), L84 (≠ F94), R88 (≠ Y98), G112 (= G122), E115 (≠ G125), T134 (≠ P144), E135 (= E145), I140 (≠ L150), P142 (= P152), G143 (≠ D153)
- binding coenzyme a: S24 (≠ A27), R25 (≠ A28), R26 (≠ L29), A28 (= A31), A65 (= A68), D68 (= D71), L69 (≠ V72), K70 (≠ R73), L110 (≠ M120), G111 (= G121), T134 (≠ P144), E135 (= E145), L138 (≠ I148), R168 (≠ Q177)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
30% identity, 46% coverage: 18:187/368 of query aligns to 17:177/260 of 2hw5C
- active site: A68 (≠ G70), M73 (≠ L75), S83 (≠ R99), L87 (≠ F103), G111 (= G122), E114 (≠ G125), P133 (= P144), E134 (= E145), T139 (≠ L150), P141 (= P152), G142 (≠ D153)
- binding crotonyl coenzyme a: K26 (≠ A27), A27 (= A28), L28 (= L29), A30 (= A31), K62 (= K64), I70 (≠ V72), F109 (≠ M120)
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)
27% identity, 50% coverage: 3:187/368 of query aligns to 34:207/290 of P14604
- E144 (≠ G125) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E145) 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)
27% identity, 50% coverage: 3:187/368 of query aligns to 3:171/254 of 2dubA
- active site: A67 (≠ G70), M72 (≠ L75), S82 (≠ R99), G105 (= G122), E108 (≠ G125), P127 (= P144), E128 (= E145), T133 (≠ L150), P135 (= P152), G136 (≠ D153)
- binding octanoyl-coenzyme a: K25 (≠ A27), A26 (= A28), L27 (= L29), A29 (= A31), A65 (= A68), A67 (≠ G70), D68 (= D71), I69 (≠ V72), K70 (≠ R73), G105 (= G122), E108 (≠ G125), P127 (= P144), E128 (= E145), G136 (≠ D153), A137 (≠ V154)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
27% identity, 50% coverage: 3:187/368 of query aligns to 4:177/260 of 1dubA
- active site: A68 (≠ G70), M73 (≠ L75), S83 (≠ R99), L87 (≠ F103), G111 (= G122), E114 (≠ G125), P133 (= P144), E134 (= E145), T139 (≠ L150), P141 (= P152), G142 (≠ D153)
- binding acetoacetyl-coenzyme a: K26 (≠ A27), A27 (= A28), L28 (= L29), A30 (= A31), A66 (= A68), A68 (≠ G70), D69 (= D71), I70 (≠ V72), Y107 (≠ I118), G110 (= G121), G111 (= G122), E114 (≠ G125), P133 (= P144), E134 (= E145), L137 (≠ I148), G142 (≠ D153)
Sites not aligning to the query:
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
27% identity, 50% coverage: 3:187/368 of query aligns to 2:175/258 of 1ey3A
- active site: A66 (≠ G70), M71 (≠ L75), S81 (≠ R99), L85 (≠ F103), G109 (= G122), E112 (≠ G125), P131 (= P144), E132 (= E145), T137 (≠ L150), P139 (= P152), G140 (≠ D153)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A27), L26 (= L29), A28 (= A31), A64 (= A68), G65 (= G69), A66 (≠ G70), D67 (= D71), I68 (≠ V72), L85 (≠ F103), W88 (vs. gap), G109 (= G122), P131 (= P144), L135 (≠ I148), G140 (≠ D153)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
25% identity, 52% coverage: 5:197/368 of query aligns to 1:184/255 of 3q0jC
- active site: A65 (≠ G70), M70 (≠ L89), T80 (≠ R99), F84 (= F103), G108 (= G122), E111 (≠ G125), P130 (= P144), E131 (= E145), V136 (≠ L150), P138 (= P152), G139 (≠ D153)
- binding acetoacetyl-coenzyme a: Q23 (≠ A27), A24 (= A28), L25 (= L29), A27 (= A31), A63 (= A68), G64 (= G69), A65 (≠ G70), D66 (= D71), I67 (≠ V72), K68 (≠ R73), M70 (≠ L89), F84 (= F103), G107 (= G121), G108 (= G122), E111 (≠ G125), P130 (= P144), E131 (= E145), P138 (= P152), G139 (≠ D153), M140 (≠ V154)
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, 52% coverage: 5:197/368 of query aligns to 1:184/255 of 3q0gC
- active site: A65 (≠ G70), M70 (≠ L89), T80 (≠ R99), F84 (= F103), G108 (= G122), E111 (≠ G125), P130 (= P144), E131 (= E145), V136 (≠ L150), P138 (= P152), G139 (≠ D153)
- binding coenzyme a: L25 (= L29), A63 (= A68), I67 (≠ V72), K68 (≠ R73), Y104 (≠ I118), P130 (= P144), E131 (= E145), L134 (≠ I148)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
25% identity, 52% coverage: 6:197/368 of query aligns to 1:183/256 of 3h81A
- active site: A64 (≠ G70), M69 (≠ L89), T79 (≠ R99), F83 (= F103), G107 (= G122), E110 (≠ G125), P129 (= P144), E130 (= E145), V135 (≠ L150), P137 (= P152), G138 (≠ D153)
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: 20:251/368 of query aligns to 20:247/266 of O53561
- K135 (≠ R140) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 140:147, 13% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ T147) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
28% identity, 50% coverage: 3:187/368 of query aligns to 4:175/258 of 1mj3A
- active site: A68 (≠ G70), M73 (≠ T88), S83 (≠ Y98), L85 (= L100), G109 (= G122), E112 (≠ G125), P131 (= P144), E132 (= E145), T137 (≠ L150), P139 (= P152), G140 (≠ D153)
- binding hexanoyl-coenzyme a: K26 (≠ A27), A27 (= A28), L28 (= L29), A30 (= A31), A66 (= A68), G67 (= G69), A68 (≠ G70), D69 (= D71), I70 (≠ V72), G109 (= G122), P131 (= P144), E132 (= E145), L135 (≠ I148), G140 (≠ D153)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
25% identity, 52% coverage: 6:197/368 of query aligns to 1:179/250 of 3q0gD
- active site: A64 (≠ G70), M69 (≠ F93), T75 (≠ R99), F79 (= F103), G103 (= G122), E106 (≠ G125), P125 (= P144), E126 (= E145), V131 (≠ L150), P133 (= P152), G134 (≠ D153)
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)
29% identity, 46% coverage: 29:199/368 of query aligns to 21:179/723 of Q08426
- V40 (≠ Q48) to G: in dbSNP:rs1062551
- I41 (≠ A49) to R: in dbSNP:rs1062552
- T75 (≠ L89) to I: in dbSNP:rs1062553
- K165 (≠ Y185) 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 (≠ F191) 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
6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
28% identity, 41% coverage: 13:163/368 of query aligns to 862:1006/1804 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
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
30% identity, 33% coverage: 36:157/368 of query aligns to 35:136/692 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
Query Sequence
>6937209 FitnessBrowser__SB2B:6937209
MTQKVVFQTLGTASGKQIGVATLNVEAALNALDLDMVRALSAQLKAWQADSNIAMVLLDG
AGDKAFCAGGDVRALYQASKDAPGSTETLAKTFFEEEYRLDYFIHEFGKPFMVWGDGIVM
GGGLGLMAGASHRIATERSRIAMPEITIGLYPDVGGTFFLAHMPEKTGVFLGLTAFQMNG
ADALYAGTANFLLESDDKEPLLDALAEVAWDDHSEANHQRLSDVLGTRAVPEQASFLKDN
AELISELCSGDLDTVIERFKALPDDSHKSLLRARDTLLAGSPLSAHLVWHQAIIGEELSL
NDCFRWELGVSINCCAHGDFVEGVRALLIDKDRNPTWQYADVASVPAEAIGSLLSSPWQG
ELHPLQDL
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