SitesBLAST
Comparing Ac3H11_413 FitnessBrowser__acidovorax_3H11:Ac3H11_413 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)
6i8wB Crystal structure of a membrane phospholipase a, a novel bacterial virulence factor (see paper)
37% identity, 90% coverage: 22:319/331 of query aligns to 20:307/310 of 6i8wB
Q9BV23 Monoacylglycerol lipase ABHD6; 2-arachidonoylglycerol hydrolase; Abhydrolase domain-containing protein 6; EC 3.1.1.23 from Homo sapiens (Human) (see 2 papers)
30% identity, 73% coverage: 75:316/331 of query aligns to 74:324/337 of Q9BV23
- F80 (≠ I81) binding
- R113 (= R114) to H: decreased bis(monoacylglycero)phosphate (BMP) hydrolase activity; dbSNP:rs200333190
- S148 (= S147) to C: loss of bis(monoacylglycero)phosphate (BMP) hydrolase activity; dbSNP:rs11544004; mutation to A: Loss of 2-arachidonoyglycerol hydrolase activity.
- M149 (= M148) binding
- P204 (≠ A197) to L: loss of bis(monoacylglycero)phosphate (BMP) hydrolase activity; dbSNP:rs199678322
- T206 (≠ D199) to P: loss of lipase activity; dbSNP:rs199696239
- G231 (≠ A224) to V: decreased bis(monoacylglycero)phosphate (BMP) hydrolase activity; dbSNP:rs745824058
- H306 (= H298) binding
Q8R2Y0 Monoacylglycerol lipase ABHD6; 2-arachidonoylglycerol hydrolase; Abhydrolase domain-containing protein 6; EC 3.1.1.23 from Mus musculus (Mouse) (see paper)
27% identity, 73% coverage: 75:316/331 of query aligns to 74:324/336 of Q8R2Y0
- S148 (= S147) mutation to A: Loss of the lipid hydrolase activity.
4lyeA Crystal structure of the s105a mutant of a c-c hydrolase, dxnb2 from sphingomonas wittichii rw1, in complex with substrate hopda (see paper)
29% identity, 80% coverage: 55:319/331 of query aligns to 18:276/276 of 4lyeA
- active site: G34 (≠ I81), G37 (≠ E84), N104 (= N146), A105 (≠ S147), M106 (= M148), M128 (≠ I170), R180 (≠ K213), D227 (= D270), H255 (= H298), W256 (≠ L299)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G33 (= G80), G34 (≠ I81), G35 (≠ F82), N104 (= N146), A105 (≠ S147), L146 (vs. gap), L166 (≠ D199), R180 (≠ K213), M229 (≠ V272), H255 (= H298), W256 (≠ L299)
4lxiA Crystal structure of the s105a mutant of a carbon-carbon bond hydrolase, dxnb2 from sphingomonas wittichii rw1, in complex with 5, 8-dif hopda (see paper)
29% identity, 80% coverage: 55:319/331 of query aligns to 18:276/276 of 4lxiA
- active site: G34 (≠ I81), G37 (≠ E84), N104 (= N146), A105 (≠ S147), M106 (= M148), M128 (≠ I170), R180 (≠ K213), D227 (= D270), H255 (= H298), W256 (≠ L299)
- binding (3E,5R)-5-fluoro-6-(2-fluorophenyl)-2,6-dioxohex-3-enoic acid: G33 (= G80), G34 (≠ I81), G35 (≠ F82), A38 (≠ K85), N43 (≠ D90), N104 (= N146), A105 (≠ S147), M106 (= M148), V149 (vs. gap), M150 (vs. gap), L166 (≠ D199), R180 (≠ K213), M229 (≠ V272), W256 (≠ L299)
4lxhA Crystal structure of the s105a mutant of a carbon-carbon bond hydrolase, dxnb2 from sphingomonas wittichii rw1, in complex with 3- cl hopda (see paper)
29% identity, 80% coverage: 55:319/331 of query aligns to 18:276/276 of 4lxhA
- active site: G34 (≠ I81), G37 (≠ E84), N104 (= N146), A105 (≠ S147), M106 (= M148), M128 (≠ I170), R180 (≠ K213), D227 (= D270), H255 (= H298), W256 (≠ L299)
- binding (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid: G33 (= G80), G34 (≠ I81), G35 (≠ F82), N104 (= N146), A105 (≠ S147), M106 (= M148), L166 (≠ D199), W256 (≠ L299)
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)
29% identity, 80% coverage: 54:318/331 of query aligns to 26:289/291 of P9WNH5
- S114 (= S147) mutation to A: Reduces the hydrolase activity.
7zm4A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclipostin-like inhibitor cyc31 (see paper)
29% identity, 80% coverage: 54:318/331 of query aligns to 20:283/284 of 7zm4A
7zm3A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclipostin-like inhibitor cyc17 (see paper)
29% identity, 80% coverage: 54:318/331 of query aligns to 20:283/284 of 7zm3A
7zm2A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclophostin-like inhibitor cyc8b (see paper)
29% identity, 80% coverage: 54:318/331 of query aligns to 20:283/284 of 7zm2A
7zm1A Crystal structure of hsad from mycobacterium tuberculosis in complex with cyclophostin-like inhibitor cyc7b (see paper)
29% identity, 80% coverage: 54:318/331 of query aligns to 20:283/284 of 7zm1A
5jzsB Hsad bound to 3,5-dichloro-4-hydroxybenzoic acid (see paper)
29% identity, 80% coverage: 54:318/331 of query aligns to 20:283/284 of 5jzsB
- active site: G39 (≠ I81), G40 (≠ F82), G42 (≠ E84), N107 (= N146), S108 (= S147), L109 (≠ M148), R186 (≠ A224), D235 (= D270), H263 (= H298), W264 (≠ L299)
- binding 3,5-dichloro-4-hydroxybenzoic acid: G39 (≠ I81), S108 (= S147), G148 (vs. gap), V149 (≠ M184), L152 (= L187), V237 (= V272)
5jz9A Crystal structure of hsad bound to 3,5-dichloro-4- hydroxybenzenesulphonic acid (see paper)
29% identity, 80% coverage: 54:318/331 of query aligns to 20:283/284 of 5jz9A
- active site: G39 (≠ I81), G40 (≠ F82), G42 (≠ E84), N107 (= N146), S108 (= S147), L109 (≠ M148), R186 (≠ A224), D235 (= D270), H263 (= H298), W264 (≠ L299)
- binding 3,5-dichloro-4-hydroxybenzene-1-sulfonic acid: G38 (= G80), G39 (≠ I81), G40 (≠ F82), S108 (= S147), G148 (vs. gap), L152 (= L187), F167 (≠ T202), M171 (= M206), V237 (= V272), H263 (= H298), W264 (≠ L299)
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)
26% identity, 79% coverage: 54:316/331 of query aligns to 26:285/288 of P77044
- S44 (≠ I81) mutation to A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate.
- N113 (= N146) 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 (= S147) 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 (≠ T151) mutation to A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity.
- F177 (≠ V210) 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 (≠ A229) 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 (≠ V296) mutation to A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity.
- H267 (= H298) active site, Proton acceptor; mutation to A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage.
- W268 (≠ L299) 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
5jzbA Crystal structure of hsad bound to 3,5-dichlorobenzene sulphonamide (see paper)
29% identity, 76% coverage: 54:303/331 of query aligns to 20:268/282 of 5jzbA
- active site: G39 (≠ I81), G40 (≠ F82), G42 (≠ E84), N107 (= N146), S108 (= S147), L109 (≠ M148), R186 (≠ A224), D235 (= D270), H263 (= H298), W264 (≠ L299)
- binding 3,5-dichlorobenzene-1-sulfonamide: G39 (≠ I81), G40 (≠ F82), S108 (= S147), L109 (≠ M148), G134 (≠ H174), L152 (= L187), N238 (≠ F273)
2wugA Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with hopda (see paper)
28% identity, 80% coverage: 54:318/331 of query aligns to 20:283/283 of 2wugA
- active site: G39 (≠ I81), G40 (≠ F82), G42 (≠ E84), N107 (= N146), A108 (≠ S147), L109 (≠ M148), R186 (≠ A224), D235 (= D270), H263 (= H298), W264 (≠ L299)
- binding (3e)-2,6-dioxo-6-phenylhex-3-enoate: G38 (= G80), G39 (≠ I81), G40 (≠ F82), A108 (≠ S147), L109 (≠ M148), M202 (≠ W240), H263 (= H298), W264 (≠ L299)
2wufB Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with 4,9dsha (see paper)
29% identity, 76% coverage: 54:303/331 of query aligns to 20:268/282 of 2wufB
- active site: G39 (≠ I81), G40 (≠ F82), G42 (≠ E84), N107 (= N146), A108 (≠ S147), L109 (≠ M148), R186 (≠ A224), D235 (= D270), H263 (= H298), W264 (≠ L299)
- 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 (= G80), G39 (≠ I81), G40 (≠ F82), A108 (≠ S147), L109 (≠ M148), L152 (= L187), F206 (≠ L244), H263 (= H298), W264 (≠ L299)
2wueB Crystal structure of s114a mutant of hsad from mycobacterium tuberculosis in complex with hopoda (see paper)
29% identity, 76% coverage: 54:303/331 of query aligns to 20:268/282 of 2wueB
- active site: G39 (≠ I81), G40 (≠ F82), G42 (≠ E84), N107 (= N146), A108 (≠ S147), L109 (≠ M148), R186 (≠ A224), D235 (= D270), H263 (= H298), W264 (≠ L299)
- binding (3e,5r)-8-(2-chlorophenyl)-5-methyl-2,6-dioxooct-3-enoate: G38 (= G80), G39 (≠ I81), G40 (≠ F82), A108 (≠ S147), L109 (≠ M148), V149 (≠ M184), L152 (= L187), M202 (≠ W240), F206 (≠ L244), V237 (= V272), H263 (= H298)
7c4dA Marine microorganism esterase (see paper)
28% identity, 73% coverage: 74:316/331 of query aligns to 15:261/261 of 7c4dA
2d0dA Crystal structure of a meta-cleavage product hydrolase (cumd) a129v mutant (see paper)
28% identity, 69% coverage: 74:303/331 of query aligns to 25:255/271 of 2d0dA
- active site: S32 (≠ I81), G33 (vs. gap), G35 (vs. gap), N100 (= N146), S101 (= S147), F102 (≠ M148), G125 (= G171), V140 (vs. gap), R172 (≠ T202), F185 (vs. gap), D222 (= D270), H250 (= H298), W251 (≠ L299)
- binding chloride ion: S32 (≠ I81), S101 (= S147), F102 (≠ M148)
Query Sequence
>Ac3H11_413 FitnessBrowser__acidovorax_3H11:Ac3H11_413
LKRIAFFSVAAALALGGVGLYYGAPSLLKEPLLHLNRSLSGMEEKTTTAALHTIHYLDSG
APSQPAPTNPDTTPLVLLHGIFAEKDHWVDFARPLTAQYRVVAPDFPGFGESTRLDDQPY
DYAAHTQRLGALLDALGIEKAHLAGNSMGGTIAALFALQHPEHVASVAFIGAPHGIHSPK
PSTMDRLIDAGQRPLVAHDAATFSAMMDLVFEKRPFLPYPILHATEQAALGNAASNTRLW
DAQLKDRYLLEQRLGGLQQHPVLALWGDSDRVFDRSGLLPLQKLLPQAQLEALPGVGHLP
MMEAPADTAQRYARFLEGLAPSSALASQKIQ
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