SitesBLAST
Comparing PP_4909 FitnessBrowser__Putida:PP_4909 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)
O53289 Phosphoserine phosphatase SerB2; PSP; PSPase; O-phosphoserine phosphohydrolase; Protein-serine/threonine phosphatase; EC 3.1.3.3; EC 3.1.3.16 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
41% identity, 95% coverage: 16:408/415 of query aligns to 7:386/409 of O53289
- G18 (= G27) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- G108 (≠ E121) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- D185 (= D207) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M208) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D209) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S210) mutation to A: No effect on enzymatic activity.
- S273 (= S295) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K340) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D363) mutation to G: Decreases enzymatic activity by 80%.; mutation to N: Decreases enzymatic activity by 85%. Completely abolishes enzymatic activity, does not elicit cytoskeletal rearrangements, and does not suppress IL-8 production after TNF-alpha stimulation; when associated with N-345.
- D345 (= D367) mutation to N: Decreases enzymatic activity by 55%. Completely abolishes enzymatic activity, does not elicit cytoskeletal rearrangements, and does not suppress IL-8 production after TNF-alpha stimulation; when associated with N-341.
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
40% identity, 95% coverage: 16:408/415 of query aligns to 5:384/396 of 8a21A
- binding magnesium ion: D183 (= D207), D185 (= D209), D339 (= D363)
- binding 4-phenyl-1h-imidazole: D13 (= D24), T18 (= T29), Q37 (≠ L48), D185 (= D209), E192 (= E216), V193 (= V217), I194 (= I218), T211 (= T235), M215 (= M239), F221 (= F245), R228 (= R252), G273 (= G297)
8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
40% identity, 95% coverage: 16:408/415 of query aligns to 5:384/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D209), E192 (= E216), M215 (= M239), F221 (= F245), L225 (≠ F249), R228 (= R252), G272 (= G296), F274 (= F298), D339 (= D363)
- binding magnesium ion: D183 (= D207), D185 (= D209), D339 (= D363)
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
40% identity, 95% coverage: 16:408/415 of query aligns to 5:384/396 of 5jlpA
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
40% identity, 95% coverage: 16:408/415 of query aligns to 9:388/411 of A0QJI1
- D187 (= D207) binding
- D189 (= D209) binding
- D343 (= D363) binding
Q58989 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see 3 papers)
43% identity, 50% coverage: 197:403/415 of query aligns to 1:207/211 of Q58989
- D11 (= D207) active site, Nucleophile; binding ; mutation to N: Loss of activity.
- D13 (= D209) active site, Proton donor; binding
- E20 (= E216) binding
- R56 (= R252) binding
- SG 99:100 (= SG 295:296) binding
- K144 (= K340) binding
- D167 (= D363) binding
- N170 (= N366) binding
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
43% identity, 49% coverage: 199:403/415 of query aligns to 1:205/209 of 1l7nA
- active site: D9 (= D207), F10 (≠ M208), D11 (= D209), G98 (= G296), K142 (= K340), D169 (= D367)
- binding aluminum fluoride: D9 (= D207), F10 (≠ M208), D11 (= D209), S97 (= S295), K142 (= K340)
- binding tetrafluoroaluminate ion: D9 (= D207), F10 (≠ M208), D11 (= D209), S97 (= S295), G98 (= G296), K142 (= K340), N168 (= N366)
- binding magnesium ion: D9 (= D207), D11 (= D209), D165 (= D363)
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
43% identity, 49% coverage: 199:403/415 of query aligns to 2:206/210 of 1f5sA
- active site: D10 (= D207), F11 (≠ M208), D12 (= D209), G99 (= G296), K143 (= K340), D170 (= D367)
- binding magnesium ion: D10 (= D207), D12 (= D209), D166 (= D363)
- binding phosphate ion: D10 (= D207), F11 (≠ M208), D12 (= D209), S98 (= S295), G99 (= G296), K143 (= K340)
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
43% identity, 49% coverage: 201:403/415 of query aligns to 2:204/208 of 1l7pA
- active site: N8 (≠ D207), F9 (≠ M208), D10 (= D209), G97 (= G296), K141 (= K340), D168 (= D367)
- binding phosphoserine: N8 (≠ D207), F9 (≠ M208), D10 (= D209), E17 (= E216), M40 (= M239), F46 (= F245), R53 (= R252), S96 (= S295), G97 (= G296), K141 (= K340)
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
44% identity, 55% coverage: 186:412/415 of query aligns to 67:292/295 of 7qplA
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
41% identity, 49% coverage: 201:403/415 of query aligns to 2:196/200 of 1l7oA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
37% identity, 47% coverage: 201:395/415 of query aligns to 3:196/208 of 3m1yC
6hyjB Psph human phosphoserine phosphatase (see paper)
33% identity, 45% coverage: 205:391/415 of query aligns to 18:206/223 of 6hyjB
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
33% identity, 45% coverage: 205:391/415 of query aligns to 18:206/225 of P78330
- D20 (= D207) binding
- DVD 20:22 (≠ DMD 207:209) binding
- D22 (= D209) binding
- S23 (= S210) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E216) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D219) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A222) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M239) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ R240) binding
- R65 (= R252) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 295:297) binding ; binding
- N133 (= N317) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K340) binding ; binding
- D179 (= D363) binding
- T182 (≠ N366) binding ; binding ; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.
- R202 (= R387) mutation to A: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to K: Reduces L-phosphoserine phosphatase activity by about 95%.
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
33% identity, 45% coverage: 205:391/415 of query aligns to 15:203/222 of 1l8oA
- active site: D17 (= D207), V18 (≠ M208), D19 (= D209), G107 (= G296), K155 (= K340), D180 (= D367)
- binding phosphate ion: D17 (= D207), D19 (= D209), S106 (= S295), K155 (= K340)
- binding serine: G177 (= G364), T179 (≠ N366), R199 (= R387)
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
33% identity, 45% coverage: 205:391/415 of query aligns to 15:203/222 of 1l8lA
- active site: D17 (= D207), V18 (≠ M208), D19 (= D209), G107 (= G296), K155 (= K340), D180 (= D367)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D207), D19 (= D209), G107 (= G296), K155 (= K340), D176 (= D363), G177 (= G364), T179 (≠ N366)
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
33% identity, 45% coverage: 205:391/415 of query aligns to 14:202/217 of 6q6jB
- binding calcium ion: D16 (= D207), D18 (= D209), D175 (= D363)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D207), V17 (≠ M208), D18 (= D209), F54 (= F245), S105 (= S295), G106 (= G296), G107 (= G297), K154 (= K340), T178 (≠ N366)
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
33% identity, 45% coverage: 205:391/415 of query aligns to 14:202/221 of 6hyyA
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
31% identity, 40% coverage: 205:368/415 of query aligns to 18:180/585 of 6iuyA
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 233, 234, 235, 236, 268, 290, 321, 324, 349, 381, 382, 497, 529, 530, 532
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
27% identity, 43% coverage: 201:379/415 of query aligns to 9:174/200 of 4ap9A
- active site: D15 (= D207), I16 (≠ M208), E17 (≠ D209), G103 (= G296), K141 (= K340), D162 (= D367)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ K223), I32 (≠ A224), T33 (≠ A225), L46 (≠ M239), W52 (≠ F245), D140 (≠ R339), K141 (= K340), Y160 (≠ A365), A161 (≠ N366)
Query Sequence
>PP_4909 FitnessBrowser__Putida:PP_4909
MRIFHRSRSQVVREIVLINITGEDRPGLTAAITGVLLQGGVSILDIGLAVMHGTLSFGIL
VDIPDNEVATALLQSVQAKAHELNLQARYTPISEADYQHWADGHGEARHIVTLLSRKITP
EQLQRVSAVISQYGLTIERIERLSARVALDAEIDKGKAAVEISVRGVPSDAQALRADFFA
LAEELSVDIAFQKDDLFRRNRRLAVFDMDSTLIEAEVIDELAKAAGVGEQVAAITERAMR
GELDFRASFKERMALLKGLDVGVLDEIGASLRLTEGAENLFAELKRLGYKTAILSGGFTY
FARQVQARLGIDYVFANELEVVDGKVTGVAVEPIVDAQRKADLLKKLASDEGLQLEQTIA
VGDGANDLPMLSLAGLGVAFRAKPLVRQSAKQAISTLGLDGVLYLLGLRDRDARG
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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