SitesBLAST
Comparing PP_0553 FitnessBrowser__Putida:PP_0553 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)
31% identity, 58% coverage: 153:366/368 of query aligns to 58:284/286 of P47229
- S112 (= S206) mutation to A: Catalyzes the tautomerisation of HOPDA. Extremely low hydrolase activity; when associated with A-265.
- H265 (= H347) 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)
31% identity, 58% coverage: 153:366/368 of query aligns to 57:283/285 of 2og1A
Sites not aligning to the query:
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)
31% identity, 58% coverage: 153:366/368 of query aligns to 55:281/283 of 2rhwA
- active site: N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D324), H262 (= H347), W263 (≠ M348)
- binding 3-fluoro-6-(4-fluorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid: A109 (≠ S206), M110 (= M207), G135 (≠ A232), I150 (vs. gap), F172 (= F263), L210 (vs. gap), F236 (≠ I326), V237 (≠ I327), H262 (= H347)
Sites not aligning to the query:
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)
31% identity, 58% coverage: 153:366/368 of query aligns to 55:281/283 of 2rhtA
- active site: N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D324), H262 (= H347), W263 (≠ M348)
- binding (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: A109 (≠ S206), M110 (= M207), I150 (vs. gap), L153 (= L243), F172 (= F263), R187 (= R282), F236 (≠ I326), V237 (≠ I327), H262 (= H347)
Sites not aligning to the query:
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)
31% identity, 58% coverage: 153:366/368 of query aligns to 55:281/283 of 2puhA
- active site: N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D324), H262 (= H347), W263 (≠ M348)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: N108 (≠ H205), A109 (≠ S206), M110 (= M207), I150 (vs. gap), F172 (= F263), R187 (= R282), L210 (vs. gap), W213 (≠ H305), V237 (≠ I327), H262 (= H347), W263 (≠ M348)
Sites not aligning to the query:
6i8wB Crystal structure of a membrane phospholipase a, a novel bacterial virulence factor (see paper)
30% identity, 65% coverage: 125:365/368 of query aligns to 54:304/310 of 6i8wB
Sites not aligning to the query:
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)
28% identity, 69% coverage: 115:367/368 of query aligns to 16:287/288 of P77044
- S44 (≠ F141) mutation to A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate.
- N113 (≠ H205) 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 (= S206) 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 (≠ A210) mutation to A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity.
- F177 (≠ L278) 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 (vs. gap) 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 (≠ A345) mutation to A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- H267 (= H347) active site, Proton acceptor; mutation to A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage.
- W268 (≠ M348) 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
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)
30% identity, 58% coverage: 153:366/368 of query aligns to 55:281/283 of 2pujA
- active site: N108 (≠ H205), A109 (≠ S206), M110 (= M207), R187 (= R282), D234 (= D324), A262 (≠ H347), W263 (≠ M348)
- binding (2e,4e)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: A109 (≠ S206), M110 (= M207), G135 (≠ A232), I150 (vs. gap), L153 (= L243), F172 (= F263), R187 (= R282), V237 (≠ I327)
Sites not aligning to the query:
4uhdA Structural studies of a thermophilic esterase from thermogutta terrifontis (acetate bound) (see paper)
28% identity, 66% coverage: 126:367/368 of query aligns to 19:269/274 of 4uhdA
- active site: F34 (= F141), L99 (≠ H205), S100 (= S206), M101 (= M207), D124 (≠ A230), E164 (vs. gap), D221 (= D324), H249 (= H347), L250 (≠ M348)
- binding acetate ion: G33 (= G140), F34 (= F141), S100 (= S206), Y104 (≠ A210), R138 (≠ A254), H249 (= H347)
- binding magnesium ion: A233 (vs. gap), I236 (vs. gap), S239 (≠ A337)
4uheA Structural studies of a thermophilic esterase from thermogutta terrifontis (malate bound) (see paper)
28% identity, 66% coverage: 126:367/368 of query aligns to 19:269/272 of 4uheA
- active site: F34 (= F141), L99 (≠ H205), S100 (= S206), M101 (= M207), D124 (≠ A230), E164 (vs. gap), D221 (= D324), H249 (= H347), L250 (≠ M348)
- binding d-malate: F34 (= F141), S100 (= S206), M101 (= M207), Y104 (≠ A210), R138 (≠ A254), H249 (= H347)
4uhfA Structural studies of a thermophilic esterase from thermogutta terrifontis (l37a mutant with butyrate bound) (see paper)
28% identity, 66% coverage: 126:367/368 of query aligns to 19:269/278 of 4uhfA
- active site: F34 (= F141), L99 (≠ H205), S100 (= S206), M101 (= M207), D124 (≠ A230), E164 (vs. gap), D221 (= D324), H249 (= H347), L250 (≠ M348)
- binding butanoic acid: G33 (= G140), F34 (= F141), S100 (= S206), H249 (= H347)
1iunB Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant hexagonal (see paper)
25% identity, 67% coverage: 120:367/368 of query aligns to 13:271/276 of 1iunB
- active site: S33 (≠ F141), G34 (= G142), G36 (≠ D144), N101 (≠ H205), A102 (≠ S206), F103 (≠ M207), G126 (≠ A230), V141 (≠ Q241), R173 (≠ K281), F186 (≠ A294), D223 (= D324), H251 (= H347), W252 (≠ M348)
- binding acetate ion: H244 (≠ Q340), R260 (≠ Q356)
1ukaA Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with (s)-2-methylbutyrate (see paper)
25% identity, 67% coverage: 120:367/368 of query aligns to 12:270/271 of 1ukaA
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), A101 (≠ S206), F102 (≠ M207), G125 (≠ A230), V140 (≠ Q241), R172 (≠ K281), F185 (≠ A294), D222 (= D324), H250 (= H347), W251 (≠ M348)
- binding 2-methylbutanoic acid: S32 (≠ F141), A101 (≠ S206), F102 (≠ M207), W141 (≠ Y242), V224 (≠ I326), H250 (= H347)
1uk9A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with isovalerate (see paper)
25% identity, 67% coverage: 120:367/368 of query aligns to 12:270/271 of 1uk9A
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), A101 (≠ S206), F102 (≠ M207), G125 (≠ A230), V140 (≠ Q241), R172 (≠ K281), F185 (≠ A294), D222 (= D324), H250 (= H347), W251 (≠ M348)
- binding isovaleric acid: S32 (≠ F141), A101 (≠ S206), F102 (≠ M207), W141 (≠ Y242), H250 (= H347)
1uk8A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-valerate (see paper)
25% identity, 67% coverage: 120:367/368 of query aligns to 12:270/271 of 1uk8A
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), A101 (≠ S206), F102 (≠ M207), G125 (≠ A230), V140 (≠ Q241), R172 (≠ K281), F185 (≠ A294), D222 (= D324), H250 (= H347), W251 (≠ M348)
- binding pentanoic acid: S32 (≠ F141), A101 (≠ S206), F102 (≠ M207), L137 (≠ I238), W141 (≠ Y242), L231 (≠ E333), G234 (vs. gap), E235 (vs. gap), H250 (= H347)
1uk7A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-butyrate (see paper)
25% identity, 67% coverage: 120:367/368 of query aligns to 12:270/271 of 1uk7A
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), A101 (≠ S206), F102 (≠ M207), G125 (≠ A230), V140 (≠ Q241), R172 (≠ K281), F185 (≠ A294), D222 (= D324), H250 (= H347), W251 (≠ M348)
- binding butanoic acid: S32 (≠ F141), A101 (≠ S206), F102 (≠ M207), L137 (≠ I238), H250 (= H347)
1iupA Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant complexed with isobutyrates (see paper)
25% identity, 67% coverage: 120:367/368 of query aligns to 12:270/271 of 1iupA
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), A101 (≠ S206), F102 (≠ M207), G125 (≠ A230), V140 (≠ Q241), R172 (≠ K281), F185 (≠ A294), D222 (= D324), H250 (= H347), W251 (≠ M348)
- binding 2-methyl-propionic acid: S32 (≠ F141), A40 (vs. gap), N41 (= N147), Y74 (vs. gap), W79 (≠ L184), A101 (≠ S206), F102 (≠ M207), L137 (≠ I238), W141 (≠ Y242), R172 (≠ K281), M188 (≠ L297), W196 (vs. gap), V224 (≠ I326), H250 (= H347), W251 (≠ M348)
2d0dA Crystal structure of a meta-cleavage product hydrolase (cumd) a129v mutant (see paper)
25% identity, 67% coverage: 120:367/368 of query aligns to 12:270/271 of 2d0dA
- active site: S32 (≠ F141), G33 (= G142), G35 (≠ D144), N100 (≠ H205), S101 (= S206), F102 (≠ M207), G125 (≠ A230), V140 (≠ Q241), R172 (≠ K281), F185 (≠ A294), D222 (= D324), H250 (= H347), W251 (≠ M348)
- binding chloride ion: S32 (≠ F141), S101 (= S206), F102 (≠ M207)
3heaA The l29p/l124i mutation of pseudomonas fluorescens esterase (see paper)
29% identity, 66% coverage: 125:367/368 of query aligns to 12:271/271 of 3heaA
- active site: W28 (≠ F141), S94 (= S206), M95 (= M207), L118 (≠ V229), G119 (≠ A230), D222 (= D324), H251 (= H347)
- binding ethyl acetate: G27 (= G140), W28 (≠ F141), S94 (= S206), M95 (= M207), H251 (= H347)
3hi4A Switching catalysis from hydrolysis to perhydrolysis in p. Fluorescens esterase (see paper)
28% identity, 66% coverage: 125:367/368 of query aligns to 12:271/271 of 3hi4A
Query Sequence
>PP_0553 FitnessBrowser__Putida:PP_0553
MSQIHTLTMPKWGLSMTEGRVDTWLKQEGDEISKGDEVLDVETDKISSSVEAPFSGVLRR
QVAKPDETLPVGALLAVVVEGEAEEAEIDAVVQRFQAEFVAEGGADQSQGPAPQKAEVGG
RLLRWFELGEGGTPLVLVHGFGGDLNNWLFNHPALAAERRVIALDLPGHGESAKALQRGD
LDELSETVLALLDHLDIAKAHLAGHSMGGAVSLNVARLAPQRVASLSLVASAGLGEAING
QYLQGFVTAANRNALKPQMVQLFADPALVTRQMLEDMLKFKRLEGVDQALQQLAGALADG
DRQRHDLRGVLGNHPALVVWGGKDAIIPASHAEGLEAEVQVLPEAGHMVQMEAAEQVNQQ
LLAFLRKH
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