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Comparing WP_011781568.1 NCBI__GCF_000015305.1:WP_011781568.1 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)
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)
42% identity, 98% coverage: 3:274/277 of query aligns to 2:283/286 of P47229
- S112 (= S104) mutation to A: Catalyzes the tautomerisation of HOPDA. Extremely low hydrolase activity; when associated with A-265.
- H265 (= H256) 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)
42% identity, 98% coverage: 3:274/277 of query aligns to 1:282/285 of 2og1A
- active site: G41 (≠ S38), G42 (= G39), G44 (= G41), N110 (= N103), S111 (= S104), M112 (= M105), L155 (= L149), R189 (= R183), A207 (≠ G201), D236 (= D228), H264 (= H256), W265 (= W257)
- binding glycerol: Y52 (≠ G49), E184 (= E178)
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)
41% identity, 97% coverage: 5:274/277 of query aligns to 1:280/283 of 2rhwA
- active site: G39 (≠ S38), G40 (= G39), G42 (= G41), N108 (= N103), A109 (≠ S104), M110 (= M105), R187 (= R183), D234 (= D228), H262 (= H256), W263 (= W257)
- binding 3-fluoro-6-(4-fluorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid: G38 (= G37), G39 (≠ S38), G40 (= G39), A109 (≠ S104), M110 (= M105), G135 (≠ R130), I150 (≠ L146), F172 (≠ M168), L210 (≠ Q207), F236 (≠ V230), V237 (= V231), H262 (= H256)
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)
41% identity, 97% coverage: 5:274/277 of query aligns to 1:280/283 of 2rhtA
- active site: G39 (≠ S38), G40 (= G39), G42 (= G41), N108 (= N103), A109 (≠ S104), M110 (= M105), R187 (= R183), D234 (= D228), H262 (= H256), W263 (= W257)
- binding (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G38 (= G37), G39 (≠ S38), G40 (= G39), A109 (≠ S104), M110 (= M105), I150 (≠ L146), L153 (= L149), F172 (≠ M168), R187 (= R183), F236 (≠ V230), V237 (= V231), H262 (= H256)
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)
41% identity, 97% coverage: 5:274/277 of query aligns to 1:280/283 of 2puhA
- active site: G39 (≠ S38), G40 (= G39), G42 (= G41), N108 (= N103), A109 (≠ S104), M110 (= M105), R187 (= R183), D234 (= D228), H262 (= H256), W263 (= W257)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G38 (= G37), G39 (≠ S38), G40 (= G39), N108 (= N103), A109 (≠ S104), M110 (= M105), I150 (≠ L146), F172 (≠ M168), R187 (= R183), L210 (≠ Q207), W213 (≠ V210), V237 (= V231), H262 (= H256), W263 (= W257)
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)
41% identity, 97% coverage: 5:274/277 of query aligns to 1:280/283 of 2pujA
- active site: G39 (≠ S38), G40 (= G39), G42 (= G41), N108 (= N103), A109 (≠ S104), M110 (= M105), R187 (= R183), D234 (= D228), A262 (≠ H256), W263 (= W257)
- binding (2e,4e)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G38 (= G37), G39 (≠ S38), G40 (= G39), A109 (≠ S104), M110 (= M105), G135 (≠ R130), I150 (≠ L146), L153 (= L149), F172 (≠ M168), R187 (= R183), V237 (= V231)
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)
38% identity, 97% coverage: 6:275/277 of query aligns to 7:286/288 of P77044
- S44 (= S38) mutation to A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate.
- N113 (= N103) 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 (= S104) 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 (≠ G108) mutation to A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity.
- F177 (≠ M168) 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 (= R183) 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 (= C254) mutation to A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- H267 (= H256) active site, Proton acceptor; mutation to A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage.
- W268 (= W257) mutation to G: 10-fold and 20-fold decrease in catalytic activity and affinity, respectively.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
37% identity, 99% coverage: 2:274/277 of query aligns to 4:287/291 of P9WNH5
- S114 (= S104) mutation to A: Reduces the hydrolase activity.
2d0dA Crystal structure of a meta-cleavage product hydrolase (cumd) a129v mutant (see paper)
37% identity, 92% coverage: 22:275/277 of query aligns to 16:269/271 of 2d0dA
- active site: S32 (= S38), G33 (= G39), G35 (= G41), N100 (= N103), S101 (= S104), F102 (≠ M105), G125 (= G128), V140 (≠ L149), R172 (= R183), F185 (= F197), D222 (= D228), H250 (= H256), W251 (= W257)
- binding chloride ion: S32 (= S38), S101 (= S104), F102 (≠ M105)
1ukaA Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with (s)-2-methylbutyrate (see paper)
37% identity, 92% coverage: 22:275/277 of query aligns to 16:269/271 of 1ukaA
- active site: S32 (= S38), G33 (= G39), G35 (= G41), N100 (= N103), A101 (≠ S104), F102 (≠ M105), G125 (= G128), V140 (≠ L149), R172 (= R183), F185 (= F197), D222 (= D228), H250 (= H256), W251 (= W257)
- binding 2-methylbutanoic acid: S32 (= S38), A101 (≠ S104), F102 (≠ M105), W141 (≠ L150), V224 (= V230), H250 (= H256)
1uk9A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with isovalerate (see paper)
37% identity, 92% coverage: 22:275/277 of query aligns to 16:269/271 of 1uk9A
- active site: S32 (= S38), G33 (= G39), G35 (= G41), N100 (= N103), A101 (≠ S104), F102 (≠ M105), G125 (= G128), V140 (≠ L149), R172 (= R183), F185 (= F197), D222 (= D228), H250 (= H256), W251 (= W257)
- binding isovaleric acid: S32 (= S38), A101 (≠ S104), F102 (≠ M105), W141 (≠ L150), H250 (= H256)
1uk8A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-valerate (see paper)
37% identity, 92% coverage: 22:275/277 of query aligns to 16:269/271 of 1uk8A
- active site: S32 (= S38), G33 (= G39), G35 (= G41), N100 (= N103), A101 (≠ S104), F102 (≠ M105), G125 (= G128), V140 (≠ L149), R172 (= R183), F185 (= F197), D222 (= D228), H250 (= H256), W251 (= W257)
- binding pentanoic acid: S32 (= S38), A101 (≠ S104), F102 (≠ M105), L137 (= L146), W141 (≠ L150), L231 (= L237), G234 (≠ V240), E235 (≠ S241), H250 (= H256)
1uk7A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-butyrate (see paper)
37% identity, 92% coverage: 22:275/277 of query aligns to 16:269/271 of 1uk7A
- active site: S32 (= S38), G33 (= G39), G35 (= G41), N100 (= N103), A101 (≠ S104), F102 (≠ M105), G125 (= G128), V140 (≠ L149), R172 (= R183), F185 (= F197), D222 (= D228), H250 (= H256), W251 (= W257)
- binding butanoic acid: S32 (= S38), A101 (≠ S104), F102 (≠ M105), L137 (= L146), H250 (= H256)
1iupA Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant complexed with isobutyrates (see paper)
37% identity, 92% coverage: 22:275/277 of query aligns to 16:269/271 of 1iupA
- active site: S32 (= S38), G33 (= G39), G35 (= G41), N100 (= N103), A101 (≠ S104), F102 (≠ M105), G125 (= G128), V140 (≠ L149), R172 (= R183), F185 (= F197), D222 (= D228), H250 (= H256), W251 (= W257)
- binding 2-methyl-propionic acid: S32 (= S38), A40 (≠ S46), N41 (= N47), Y74 (≠ H82), W79 (vs. gap), A101 (≠ S104), F102 (≠ M105), L137 (= L146), W141 (≠ L150), R172 (= R183), M188 (≠ L202), W196 (vs. gap), V224 (= V230), H250 (= H256), W251 (= W257)
1iunB Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant hexagonal (see paper)
37% identity, 92% coverage: 22:275/277 of query aligns to 17:270/276 of 1iunB
- active site: S33 (= S38), G34 (= G39), G36 (= G41), N101 (= N103), A102 (≠ S104), F103 (≠ M105), G126 (= G128), V141 (≠ L149), R173 (= R183), F186 (= F197), D223 (= D228), H251 (= H256), W252 (= W257)
- binding acetate ion: H244 (≠ V249), R260 (≠ E265)
5jzbA Crystal structure of hsad bound to 3,5-dichlorobenzene sulphonamide (see paper)
36% identity, 99% coverage: 1:274/277 of query aligns to 1:281/282 of 5jzbA
- active site: G39 (≠ S38), G40 (= G39), G42 (= G41), N107 (= N103), S108 (= S104), L109 (≠ M105), R186 (= R183), D235 (= D228), H263 (= H256), W264 (= W257)
- binding 3,5-dichlorobenzene-1-sulfonamide: G39 (≠ S38), G40 (= G39), S108 (= S104), L109 (≠ M105), G134 (≠ R130), L152 (= L149), N238 (≠ V231)
7zm4A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclipostin-like inhibitor cyc31 (see paper)
36% identity, 99% coverage: 1:274/277 of query aligns to 1:281/284 of 7zm4A
7zm3A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclipostin-like inhibitor cyc17 (see paper)
36% identity, 99% coverage: 1:274/277 of query aligns to 1:281/284 of 7zm3A
7zm2A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclophostin-like inhibitor cyc8b (see paper)
36% identity, 99% coverage: 1:274/277 of query aligns to 1:281/284 of 7zm2A
7zm1A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclophostin-like inhibitor cyc7b (see paper)
36% identity, 99% coverage: 1:274/277 of query aligns to 1:281/284 of 7zm1A
Query Sequence
>WP_011781568.1 NCBI__GCF_000015305.1:WP_011781568.1
MSSEITEQYTSRDIETKSGTIHYNEAGEGYPIVMLHGSGPGATGWSNFGSNIKGLADRFR
VIAADMPGWGQSEAVKPDARDHVAAALQLLDGLGIEKAAFVGNSMGGGTAIQFAVAHPDR
ISHLITMGSRAPGPTIIGPDGLTEGLKTLLKGYTDPSPTSMRELVEIMTYDSANATDELV
QQRYAAAIGRPDHLENFMIAGLLGIPQATVEEIAGIETPTLIFHGKDDRVVSYEAALKLV
SLIRDSRVVLINRCGHWLQTEHSDEFNRLVADFVSNR
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