SitesBLAST
Comparing 18409 FitnessBrowser__Keio:18409 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
47% identity, 73% coverage: 81:315/322 of query aligns to 150:384/409 of O53289
- D185 (= D116) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M117) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D118) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S119) mutation to A: No effect on enzymatic activity.
- S273 (= S204) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K249) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D272) 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 (= D276) 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.
Sites not aligning to the query:
- 18 G→A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- 108 G→A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
44% identity, 76% coverage: 71:315/322 of query aligns to 132:386/411 of A0QJI1
- D187 (= D116) binding
- D189 (= D118) binding
- D343 (= D272) binding
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
44% identity, 76% coverage: 71:315/322 of query aligns to 128:382/396 of 5jlpA
Sites not aligning to the query:
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
46% identity, 71% coverage: 88:315/322 of query aligns to 155:382/396 of 8a21A
- binding magnesium ion: D183 (= D116), D185 (= D118), D339 (= D272)
- binding 4-phenyl-1h-imidazole: D185 (= D118), E192 (= E125), V193 (≠ C126), I194 (= I127), T211 (= T144), M215 (= M148), F221 (= F154), R228 (= R161), G273 (= G206)
Sites not aligning to the query:
8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
46% identity, 71% coverage: 88:315/322 of query aligns to 155:382/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D118), E192 (= E125), M215 (= M148), F221 (= F154), L225 (= L158), R228 (= R161), G272 (= G205), F274 (= F207), D339 (= D272)
- binding magnesium ion: D183 (= D116), D185 (= D118), D339 (= D272)
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
39% identity, 64% coverage: 108:312/322 of query aligns to 2:206/210 of 1f5sA
- active site: D10 (= D116), F11 (≠ M117), D12 (= D118), G99 (= G205), K143 (= K249), D170 (= D276)
- binding magnesium ion: D10 (= D116), D12 (= D118), D166 (= D272)
- binding phosphate ion: D10 (= D116), F11 (≠ M117), D12 (= D118), S98 (= S204), G99 (= G205), K143 (= K249)
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
39% identity, 64% coverage: 108:312/322 of query aligns to 1:205/209 of 1l7nA
- active site: D9 (= D116), F10 (≠ M117), D11 (= D118), G98 (= G205), K142 (= K249), D169 (= D276)
- binding aluminum fluoride: D9 (= D116), F10 (≠ M117), D11 (= D118), S97 (= S204), K142 (= K249)
- binding tetrafluoroaluminate ion: D9 (= D116), F10 (≠ M117), D11 (= D118), S97 (= S204), G98 (= G205), K142 (= K249), N168 (= N275)
- binding magnesium ion: D9 (= D116), D11 (= D118), D165 (= D272)
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)
40% identity, 62% coverage: 108:308/322 of query aligns to 3:203/211 of Q58989
- D11 (= D116) active site, Nucleophile; binding ; mutation to N: Loss of activity.
- D13 (= D118) active site, Proton donor; binding
- E20 (= E125) binding
- R56 (= R161) binding
- SG 99:100 (= SG 204:205) binding
- K144 (= K249) binding
- D167 (= D272) binding
- N170 (= N275) binding
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
39% identity, 62% coverage: 112:312/322 of query aligns to 4:204/208 of 1l7pA
- active site: N8 (≠ D116), F9 (≠ M117), D10 (= D118), G97 (= G205), K141 (= K249), D168 (= D276)
- binding phosphoserine: N8 (≠ D116), F9 (≠ M117), D10 (= D118), E17 (= E125), M40 (= M148), F46 (= F154), R53 (= R161), S96 (= S204), G97 (= G205), K141 (= K249)
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
40% identity, 69% coverage: 94:314/322 of query aligns to 61:285/295 of 7qplA
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
37% identity, 62% coverage: 112:312/322 of query aligns to 4:196/200 of 1l7oA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
36% identity, 61% coverage: 112:308/322 of query aligns to 5:200/208 of 3m1yC
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
32% identity, 55% coverage: 113:289/322 of query aligns to 14:193/222 of 1l8oA
Sites not aligning to the query:
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
32% identity, 55% coverage: 113:289/322 of query aligns to 14:193/222 of 1l8lA
- active site: D17 (= D116), V18 (≠ M117), D19 (= D118), G107 (= G205), K155 (= K249), D180 (= D276)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D116), D19 (= D118), G107 (= G205), K155 (= K249), D176 (= D272), G177 (= G273), T179 (≠ N275)
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
32% identity, 55% coverage: 113:289/322 of query aligns to 13:192/217 of 6q6jB
- binding calcium ion: D16 (= D116), D18 (= D118), D175 (= D272)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D116), V17 (≠ M117), D18 (= D118), F54 (= F154), S105 (= S204), G106 (= G205), G107 (= G206), K154 (= K249), T178 (≠ N275)
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
32% identity, 55% coverage: 113:289/322 of query aligns to 17:196/225 of P78330
- D20 (= D116) binding
- DVD 20:22 (≠ DMD 116:118) binding
- D22 (= D118) binding
- S23 (= S119) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E125) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D128) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A131) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M148) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ R149) binding
- R65 (= R161) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 204:206) binding ; binding
- N133 (= N226) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K249) binding ; binding
- D179 (= D272) binding
- T182 (≠ N275) binding ; binding ; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.
Sites not aligning to the query:
- 202 R→A: Reduces L-phosphoserine phosphatase activity by about 99%.; R→K: Reduces L-phosphoserine phosphatase activity by about 95%.
6hyjB Psph human phosphoserine phosphatase (see paper)
32% identity, 55% coverage: 113:289/322 of query aligns to 17:196/223 of 6hyjB
Sites not aligning to the query:
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
32% identity, 55% coverage: 113:289/322 of query aligns to 13:192/221 of 6hyyA
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
29% identity, 54% coverage: 114:288/322 of query aligns to 13:174/200 of 4ap9A
- active site: D15 (= D116), I16 (≠ M117), E17 (≠ D118), G103 (= G205), K141 (= K249), D162 (= D276)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ K132), I32 (≠ L133), T33 (≠ A134), L46 (≠ M148), W52 (≠ F154), D140 (≠ Y248), K141 (= K249), Y160 (≠ A274), A161 (≠ N275)
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
25% identity, 61% coverage: 113:307/322 of query aligns to 17:217/585 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
Query Sequence
>18409 FitnessBrowser__Keio:18409
MPNITWCDLPEDVSLWPGLPLSLSGDEVMPLDYHAGRSGWLLYGRGLDKQRLTQYQSKLG
AAMVIVAAWCVEDYQVIRLAGSLTARATRLAHEAQLDVAPLGKIPHLRTPGLLVMDMDST
AIQIECIDEIAKLAGTGEMVAEVTERAMRGELDFTASLRSRVATLKGADANILQQVRENL
PLMPGLTQLVLKLETLGWKVAIASGGFTFFAEYLRDKLRLTAVVANELEIMDGKFTGNVI
GDIVDAQYKAKTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEKAE
VTIRHADLMGVFCILSGSLNQK
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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