SitesBLAST
Comparing GFF1134 FitnessBrowser__Marino:GFF1134 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)
1iunB Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant hexagonal (see paper)
65% identity, 95% coverage: 9:279/286 of query aligns to 4:273/276 of 1iunB
- active site: S33 (= S39), G34 (= G40), G36 (= G42), N101 (= N107), A102 (≠ S108), F103 (= F109), G126 (= G132), V141 (= V147), R173 (= R179), F186 (= F192), D223 (= D229), H251 (= H257), W252 (= W258)
- binding acetate ion: H244 (= H250), R260 (= R266)
1ukaA Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with (s)-2-methylbutyrate (see paper)
65% identity, 94% coverage: 9:278/286 of query aligns to 3:271/271 of 1ukaA
- active site: S32 (= S39), G33 (= G40), G35 (= G42), N100 (= N107), A101 (≠ S108), F102 (= F109), G125 (= G132), V140 (= V147), R172 (= R179), F185 (= F192), D222 (= D229), H250 (= H257), W251 (= W258)
- binding 2-methylbutanoic acid: S32 (= S39), A101 (≠ S108), F102 (= F109), W141 (= W148), V224 (= V231), H250 (= H257)
1uk9A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with isovalerate (see paper)
65% identity, 94% coverage: 9:278/286 of query aligns to 3:271/271 of 1uk9A
- active site: S32 (= S39), G33 (= G40), G35 (= G42), N100 (= N107), A101 (≠ S108), F102 (= F109), G125 (= G132), V140 (= V147), R172 (= R179), F185 (= F192), D222 (= D229), H250 (= H257), W251 (= W258)
- binding isovaleric acid: S32 (= S39), A101 (≠ S108), F102 (= F109), W141 (= W148), H250 (= H257)
1uk8A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-valerate (see paper)
65% identity, 94% coverage: 9:278/286 of query aligns to 3:271/271 of 1uk8A
- active site: S32 (= S39), G33 (= G40), G35 (= G42), N100 (= N107), A101 (≠ S108), F102 (= F109), G125 (= G132), V140 (= V147), R172 (= R179), F185 (= F192), D222 (= D229), H250 (= H257), W251 (= W258)
- binding pentanoic acid: S32 (= S39), A101 (≠ S108), F102 (= F109), L137 (= L144), W141 (= W148), L231 (= L238), G234 (≠ A241), E235 (= E242), H250 (= H257)
1uk7A Crystal structure of a meta-cleavage product hydrolase (cumd) complexed with n-butyrate (see paper)
65% identity, 94% coverage: 9:278/286 of query aligns to 3:271/271 of 1uk7A
- active site: S32 (= S39), G33 (= G40), G35 (= G42), N100 (= N107), A101 (≠ S108), F102 (= F109), G125 (= G132), V140 (= V147), R172 (= R179), F185 (= F192), D222 (= D229), H250 (= H257), W251 (= W258)
- binding butanoic acid: S32 (= S39), A101 (≠ S108), F102 (= F109), L137 (= L144), H250 (= H257)
1iupA Meta-cleavage product hydrolase from pseudomonas fluorescens ip01 (cumd) s103a mutant complexed with isobutyrates (see paper)
65% identity, 94% coverage: 9:278/286 of query aligns to 3:271/271 of 1iupA
- active site: S32 (= S39), G33 (= G40), G35 (= G42), N100 (= N107), A101 (≠ S108), F102 (= F109), G125 (= G132), V140 (= V147), R172 (= R179), F185 (= F192), D222 (= D229), H250 (= H257), W251 (= W258)
- binding 2-methyl-propionic acid: S32 (= S39), A40 (= A47), N41 (= N48), Y74 (= Y81), W79 (= W86), A101 (≠ S108), F102 (= F109), L137 (= L144), W141 (= W148), R172 (= R179), M188 (= M195), W196 (= W203), V224 (= V231), H250 (= H257), W251 (= W258)
2d0dA Crystal structure of a meta-cleavage product hydrolase (cumd) a129v mutant (see paper)
65% identity, 94% coverage: 9:278/286 of query aligns to 3:271/271 of 2d0dA
- active site: S32 (= S39), G33 (= G40), G35 (= G42), N100 (= N107), S101 (= S108), F102 (= F109), G125 (= G132), V140 (= V147), R172 (= R179), F185 (= F192), D222 (= D229), H250 (= H257), W251 (= W258)
- binding chloride ion: S32 (= S39), S101 (= S108), F102 (= F109)
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)
36% identity, 90% coverage: 20:275/286 of query aligns to 25:287/291 of P9WNH5
- S114 (= S108) mutation to A: Reduces the hydrolase activity.
7zm4A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclipostin-like inhibitor cyc31 (see paper)
36% identity, 90% coverage: 20:275/286 of query aligns to 19:281/284 of 7zm4A
7zm3A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclipostin-like inhibitor cyc17 (see paper)
36% identity, 90% coverage: 20:275/286 of query aligns to 19:281/284 of 7zm3A
7zm2A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclophostin-like inhibitor cyc8b (see paper)
36% identity, 90% coverage: 20:275/286 of query aligns to 19:281/284 of 7zm2A
7zm1A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclophostin-like inhibitor cyc7b (see paper)
36% identity, 90% coverage: 20:275/286 of query aligns to 19:281/284 of 7zm1A
5jzsB Hsad bound to 3,5-dichloro-4-hydroxybenzoic acid (see paper)
36% identity, 90% coverage: 20:275/286 of query aligns to 19:281/284 of 5jzsB
- active site: G39 (≠ S39), G40 (= G40), G42 (= G42), N107 (= N107), S108 (= S108), L109 (≠ F109), R186 (= R179), D235 (= D229), H263 (= H257), W264 (= W258)
- binding 3,5-dichloro-4-hydroxybenzoic acid: G39 (≠ S39), S108 (= S108), G148 (= G143), V149 (≠ L144), L152 (≠ V147), V237 (= V231)
5jz9A Crystal structure of hsad bound to 3,5-dichloro-4- hydroxybenzenesulphonic acid (see paper)
36% identity, 90% coverage: 20:275/286 of query aligns to 19:281/284 of 5jz9A
- active site: G39 (≠ S39), G40 (= G40), G42 (= G42), N107 (= N107), S108 (= S108), L109 (≠ F109), R186 (= R179), D235 (= D229), H263 (= H257), W264 (= W258)
- binding 3,5-dichloro-4-hydroxybenzene-1-sulfonic acid: G38 (= G38), G39 (≠ S39), G40 (= G40), S108 (= S108), G148 (= G143), L152 (≠ V147), F167 (≠ L160), M171 (≠ F164), V237 (= V231), H263 (= H257), W264 (= W258)
5jzbA Crystal structure of hsad bound to 3,5-dichlorobenzene sulphonamide (see paper)
36% identity, 90% coverage: 20:275/286 of query aligns to 19:281/282 of 5jzbA
- active site: G39 (≠ S39), G40 (= G40), G42 (= G42), N107 (= N107), S108 (= S108), L109 (≠ F109), R186 (= R179), D235 (= D229), H263 (= H257), W264 (= W258)
- binding 3,5-dichlorobenzene-1-sulfonamide: G39 (≠ S39), G40 (= G40), S108 (= S108), L109 (≠ F109), G134 (≠ A134), L152 (≠ V147), N238 (≠ I232)
2wugA Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with hopda (see paper)
36% identity, 90% coverage: 20:275/286 of query aligns to 19:281/283 of 2wugA
- active site: G39 (≠ S39), G40 (= G40), G42 (= G42), N107 (= N107), A108 (≠ S108), L109 (≠ F109), R186 (= R179), D235 (= D229), H263 (= H257), W264 (= W258)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G38 (= G38), G39 (≠ S39), G40 (= G40), A108 (≠ S108), L109 (≠ F109), M202 (≠ F188), H263 (= H257), W264 (= W258)
2wufB Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with 4,9dsha (see paper)
36% identity, 90% coverage: 20:275/286 of query aligns to 19:281/282 of 2wufB
- active site: G39 (≠ S39), G40 (= G40), G42 (= G42), N107 (= N107), A108 (≠ S108), L109 (≠ F109), R186 (= R179), D235 (= D229), H263 (= H257), W264 (= W258)
- 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 (= G38), G39 (≠ S39), G40 (= G40), A108 (≠ S108), L109 (≠ F109), L152 (≠ V147), F206 (= F192), H263 (= H257), W264 (= W258)
2wueB Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with hopoda (see paper)
36% identity, 90% coverage: 20:275/286 of query aligns to 19:281/282 of 2wueB
- active site: G39 (≠ S39), G40 (= G40), G42 (= G42), N107 (= N107), A108 (≠ S108), L109 (≠ F109), R186 (= R179), D235 (= D229), H263 (= H257), W264 (= W258)
- binding (3e,5r)-8-(2-chlorophenyl)-5-methyl-2,6-dioxooct-3-enoate: G38 (= G38), G39 (≠ S39), G40 (= G40), A108 (≠ S108), L109 (≠ F109), V149 (≠ L144), L152 (≠ V147), M202 (≠ F188), F206 (= F192), V237 (= V231), H263 (= H257)
Q9AQM4 2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid hydrolase; HOPDA; EC 3.7.1.13 from Pseudomonas resinovorans (see paper)
32% identity, 95% coverage: 5:276/286 of query aligns to 12:280/290 of Q9AQM4
- S114 (= S108) mutation to A: 40-fold decrease in reduction in hydrolase activity.
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)
35% identity, 90% coverage: 20:275/286 of query aligns to 25:285/288 of P77044
- S44 (= S39) mutation to A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate.
- N113 (= N107) 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 (= S108) 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 (≠ G112) mutation to A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity.
- F177 (= F164) 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 (= R179) 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 (= C255) mutation to A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- H267 (= H257) active site, Proton acceptor; mutation to A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage.
- W268 (= W258) 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
Query Sequence
>GFF1134 FitnessBrowser__Marino:GFF1134
MTVPEKSPEIGREITAAGYRTNVHDHGEGGVPVMMIHGSGPGVTAWANWRLVIPELAKNR
RVVAPDMLGFGYSERPEDQIYNRERWVKHAIGVMDELGLEQVDLVGNSFGGGLALALAIE
HPKRIRRLVLMGSAGVRFPITEGLDEVWGYEPSLDNMRRLMDVFAFNKGLLTDELAEMRY
EASIRPGFQESFAAMFPAPRQRWVDNLASNEDDIRALTHETLIIHGREDEVIPLEASLRL
AELIDRAQLHVFGRCGHWTQIEHADRFARLVNDFLTEADQAAVGGN
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