SitesBLAST
Comparing 14487 FitnessBrowser__Keio:14487 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)
P77044 2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase; 2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase; 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase; 2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase; EC 3.7.1.14 from Escherichia coli (strain K12) (see 3 papers)
100% identity, 98% coverage: 6:293/293 of query aligns to 1:288/288 of P77044
- M1 (= M6) modified: Initiator methionine, Removed
- S44 (= S49) mutation to A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate.
- N113 (= N118) mutation to A: 200-fold decrease in catalytic activity and almost 2-fold increase in affinity.; mutation to H: 350-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- S114 (= S119) Transition state stabilizer; mutation to A: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage.; mutation to G: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage.
- H118 (= H123) mutation to A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity.
- F177 (= F182) mutation to D: 100-fold decrease in catalytic activity.; mutation to G: 4-fold and 8-fold decrease in catalytic activity and affinity, respectively.
- R192 (= R197) Catalytic role in ketonization of the dienol substrate (substrate destabilization); mutation to K: 40-fold and 5-fold decrease in catalytic activity and affinity, respectively.; mutation to Q: 280-fold and 10-fold decrease in catalytic activity and affinity, respectively.
- C265 (= C270) mutation to A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- H267 (= H272) active site, Proton acceptor; mutation to A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage.
- W268 (= W273) mutation to G: 10-fold and 20-fold decrease in catalytic activity and affinity, respectively.
P47229 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase; HOPDA hydrolase; 2,6-dioxo-6-phenylhexa-3-enoate hydrolase; EC 3.7.1.8 from Paraburkholderia xenovorans (strain LB400) (see paper)
52% identity, 95% coverage: 12:290/293 of query aligns to 5:283/286 of P47229
- S112 (= S119) mutation to A: Catalyzes the tautomerisation of HOPDA. Extremely low hydrolase activity; when associated with A-265.
- H265 (= H272) mutation to A: Unable to catalyze the tautomerisation of HOPDA. Extremely low hydrolase activity; when associated with A-112.
2og1A Crystal structure of bphd, a c-c hydrolase from burkholderia xenovorans lb400 (see paper)
52% identity, 95% coverage: 12:290/293 of query aligns to 4:282/285 of 2og1A
- active site: G41 (≠ S49), G42 (= G50), G44 (= G52), N110 (= N118), S111 (= S119), M112 (= M120), L155 (= L163), R189 (= R197), A207 (≠ L215), D236 (= D244), H264 (= H272), W265 (= W273)
- binding glycerol: Y52 (≠ S60), E184 (≠ A192)
2rhwA Crystal structure of the s112a mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with 3,10-di-fluoro hopda (see paper)
51% identity, 95% coverage: 12:290/293 of query aligns to 2:280/283 of 2rhwA
- active site: G39 (≠ S49), G40 (= G50), G42 (= G52), N108 (= N118), A109 (≠ S119), M110 (= M120), R187 (= R197), D234 (= D244), H262 (= H272), W263 (= W273)
- binding 3-fluoro-6-(4-fluorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid: G38 (= G48), G39 (≠ S49), G40 (= G50), A109 (≠ S119), M110 (= M120), G135 (= G145), I150 (= I160), F172 (= F182), L210 (≠ K220), F236 (= F246), V237 (= V247), H262 (= H272)
2rhtA Crystal structure of the s112a mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with 3-cl hopda (see paper)
51% identity, 95% coverage: 12:290/293 of query aligns to 2:280/283 of 2rhtA
- active site: G39 (≠ S49), G40 (= G50), G42 (= G52), N108 (= N118), A109 (≠ S119), M110 (= M120), R187 (= R197), D234 (= D244), H262 (= H272), W263 (= W273)
- binding (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G38 (= G48), G39 (≠ S49), G40 (= G50), A109 (≠ S119), M110 (= M120), I150 (= I160), L153 (= L163), F172 (= F182), R187 (= R197), F236 (= F246), V237 (= V247), H262 (= H272)
2puhA Crystal structure of the s112a mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with its substrate hopda (see paper)
51% identity, 95% coverage: 12:290/293 of query aligns to 2:280/283 of 2puhA
- active site: G39 (≠ S49), G40 (= G50), G42 (= G52), N108 (= N118), A109 (≠ S119), M110 (= M120), R187 (= R197), D234 (= D244), H262 (= H272), W263 (= W273)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G38 (= G48), G39 (≠ S49), G40 (= G50), N108 (= N118), A109 (≠ S119), M110 (= M120), I150 (= I160), F172 (= F182), R187 (= R197), L210 (≠ K220), W213 (≠ P223), V237 (= V247), H262 (= H272), W263 (= W273)
2pujA Crystal structure of the s112a/h265a double mutant of a c-c hydrolase, bphd from burkholderia xenovorans lb400, in complex with its substrate hopda (see paper)
51% identity, 95% coverage: 12:290/293 of query aligns to 2:280/283 of 2pujA
- active site: G39 (≠ S49), G40 (= G50), G42 (= G52), N108 (= N118), A109 (≠ S119), M110 (= M120), R187 (= R197), D234 (= D244), A262 (≠ H272), W263 (= W273)
- binding (2e,4e)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G38 (= G48), G39 (≠ S49), G40 (= G50), A109 (≠ S119), M110 (= M120), G135 (= G145), I150 (= I160), L153 (= L163), F172 (= F182), R187 (= R197), V237 (= V247)
P9WNH5 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase; 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase; HOPDA hydrolase; Meta-cleavage product hydrolase; MCP hydrolase; EC 3.7.1.17; EC 3.7.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 98% coverage: 5:290/293 of query aligns to 1:287/291 of P9WNH5
- S114 (= S119) mutation to A: Reduces the hydrolase activity.
5jzbA Crystal structure of hsad bound to 3,5-dichlorobenzene sulphonamide (see paper)
40% identity, 95% coverage: 12:290/293 of query aligns to 2:281/282 of 5jzbA
- active site: G39 (≠ S49), G40 (= G50), G42 (= G52), N107 (= N118), S108 (= S119), L109 (≠ M120), R186 (= R197), D235 (= D244), H263 (= H272), W264 (= W273)
- binding 3,5-dichlorobenzene-1-sulfonamide: G39 (≠ S49), G40 (= G50), S108 (= S119), L109 (≠ M120), G134 (= G145), L152 (= L163), N238 (≠ V247)
7zm4A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclipostin-like inhibitor cyc31 (see paper)
40% identity, 95% coverage: 12:290/293 of query aligns to 2:281/284 of 7zm4A
7zm3A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclipostin-like inhibitor cyc17 (see paper)
40% identity, 95% coverage: 12:290/293 of query aligns to 2:281/284 of 7zm3A
7zm2A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclophostin-like inhibitor cyc8b (see paper)
40% identity, 95% coverage: 12:290/293 of query aligns to 2:281/284 of 7zm2A
7zm1A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclophostin-like inhibitor cyc7b (see paper)
40% identity, 95% coverage: 12:290/293 of query aligns to 2:281/284 of 7zm1A
5jzsB Hsad bound to 3,5-dichloro-4-hydroxybenzoic acid (see paper)
40% identity, 95% coverage: 12:290/293 of query aligns to 2:281/284 of 5jzsB
- active site: G39 (≠ S49), G40 (= G50), G42 (= G52), N107 (= N118), S108 (= S119), L109 (≠ M120), R186 (= R197), D235 (= D244), H263 (= H272), W264 (= W273)
- binding 3,5-dichloro-4-hydroxybenzoic acid: G39 (≠ S49), S108 (= S119), G148 (= G159), V149 (≠ I160), L152 (= L163), V237 (≠ F246)
5jz9A Crystal structure of hsad bound to 3,5-dichloro-4- hydroxybenzenesulphonic acid (see paper)
40% identity, 95% coverage: 12:290/293 of query aligns to 2:281/284 of 5jz9A
- active site: G39 (≠ S49), G40 (= G50), G42 (= G52), N107 (= N118), S108 (= S119), L109 (≠ M120), R186 (= R197), D235 (= D244), H263 (= H272), W264 (= W273)
- binding 3,5-dichloro-4-hydroxybenzene-1-sulfonic acid: G38 (= G48), G39 (≠ S49), G40 (= G50), S108 (= S119), G148 (= G159), L152 (= L163), F167 (≠ M178), M171 (≠ F182), V237 (≠ F246), H263 (= H272), W264 (= W273)
2wufB Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with 4,9dsha (see paper)
40% identity, 95% coverage: 12:290/293 of query aligns to 2:281/282 of 2wufB
- active site: G39 (≠ S49), G40 (= G50), G42 (= G52), N107 (= N118), A108 (≠ S119), L109 (≠ M120), R186 (= R197), D235 (= D244), H263 (= H272), W264 (= W273)
- binding (3e,5r)-8-[(1s,3ar,4r,7as)-1-hydroxy-7a-methyl-5-oxooctahydro-1h-inden-4-yl]-5-methyl-2,6-dioxooct-3-enoate: G38 (= G48), G39 (≠ S49), G40 (= G50), A108 (≠ S119), L109 (≠ M120), L152 (= L163), F206 (= F222), H263 (= H272), W264 (= W273)
2wueB Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with hopoda (see paper)
40% identity, 95% coverage: 12:290/293 of query aligns to 2:281/282 of 2wueB
- active site: G39 (≠ S49), G40 (= G50), G42 (= G52), N107 (= N118), A108 (≠ S119), L109 (≠ M120), R186 (= R197), D235 (= D244), H263 (= H272), W264 (= W273)
- binding (3e,5r)-8-(2-chlorophenyl)-5-methyl-2,6-dioxooct-3-enoate: G38 (= G48), G39 (≠ S49), G40 (= G50), A108 (≠ S119), L109 (≠ M120), V149 (≠ I160), L152 (= L163), M202 (≠ N218), F206 (= F222), V237 (≠ F246), H263 (= H272)
2wugA Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with hopda (see paper)
40% identity, 95% coverage: 12:290/293 of query aligns to 2:281/283 of 2wugA
- active site: G39 (≠ S49), G40 (= G50), G42 (= G52), N107 (= N118), A108 (≠ S119), L109 (≠ M120), R186 (= R197), D235 (= D244), H263 (= H272), W264 (= W273)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G38 (= G48), G39 (≠ S49), G40 (= G50), A108 (≠ S119), L109 (≠ M120), M202 (≠ N218), H263 (= H272), W264 (= W273)
1ukaA Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with (s)-2-methylbutyrate (see paper)
35% identity, 88% coverage: 32:290/293 of query aligns to 16:268/271 of 1ukaA
- active site: S32 (= S49), G33 (= G50), G35 (= G52), N100 (= N118), A101 (≠ S119), F102 (≠ M120), G125 (= G143), V140 (≠ L166), R172 (≠ N199), F185 (≠ V212), D222 (= D244), H250 (= H272), W251 (= W273)
- binding 2-methylbutanoic acid: S32 (= S49), A101 (≠ S119), F102 (≠ M120), W141 (≠ Y167), V224 (≠ F246), H250 (= H272)
1uk9A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with isovalerate (see paper)
35% identity, 88% coverage: 32:290/293 of query aligns to 16:268/271 of 1uk9A
- active site: S32 (= S49), G33 (= G50), G35 (= G52), N100 (= N118), A101 (≠ S119), F102 (≠ M120), G125 (= G143), V140 (≠ L166), R172 (≠ N199), F185 (≠ V212), D222 (= D244), H250 (= H272), W251 (= W273)
- binding isovaleric acid: S32 (= S49), A101 (≠ S119), F102 (≠ M120), W141 (≠ Y167), H250 (= H272)
Query Sequence
>14487 FitnessBrowser__Keio:14487
MQEKMMSYQPQTEAATSRFLNVEEAGKTLRIHFNDCGQGDETVVLLHGSGPGATGWANFS
RNIDPLVEAGYRVILLDCPGWGKSDSVVNSGSRSDLNARILKSVVDQLDIAKIHLLGNSM
GGHSSVAFTLKWPERVGKLVLMGGGTGGMSLFTPMPTEGIKRLNQLYRQPTIENLKLMMD
IFVFDTSDLTDALFEARLNNMLSRRDHLENFVKSLEANPKQFPDFGPRLAEIKAQTLIVW
GRNDRFVPMDAGLRLLSGIAGSELHIFRDCGHWAQWEHADAFNQLVLNFLARP
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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