SitesBLAST
Comparing BWI76_RS04160 FitnessBrowser__Koxy:BWI76_RS04160 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)
40% identity, 92% coverage: 19:316/323 of query aligns to 76:384/409 of O53289
- G108 (≠ H51) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- D185 (= D117) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M118) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D119) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S120) mutation to A: No effect on enzymatic activity.
- S273 (= S205) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K250) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D273) 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 (= D277) 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.
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
40% identity, 92% coverage: 19:316/323 of query aligns to 74:382/396 of 5jlpA
Sites not aligning to the query:
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
39% identity, 92% coverage: 19:316/323 of query aligns to 78:386/411 of A0QJI1
- D187 (= D117) binding
- D189 (= D119) binding
- D343 (= D273) binding
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
39% identity, 92% coverage: 19:316/323 of query aligns to 74:382/396 of 8a21A
- binding magnesium ion: D183 (= D117), D185 (= D119), D339 (= D273)
- binding 4-phenyl-1h-imidazole: D185 (= D119), E192 (= E126), V193 (≠ C127), I194 (= I128), T211 (= T145), M215 (= M149), F221 (= F155), R228 (= R162), G273 (= G207)
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)
39% identity, 92% coverage: 19:316/323 of query aligns to 74:382/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D119), E192 (= E126), M215 (= M149), F221 (= F155), L225 (= L159), R228 (= R162), G272 (= G206), F274 (= F208), D339 (= D273)
- binding magnesium ion: D183 (= D117), D185 (= D119), D339 (= D273)
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)
41% identity, 62% coverage: 109:309/323 of query aligns to 3:203/211 of Q58989
- D11 (= D117) active site, Nucleophile; binding ; mutation to N: Loss of activity.
- D13 (= D119) active site, Proton donor; binding
- E20 (= E126) binding
- R56 (= R162) binding
- SG 99:100 (= SG 205:206) binding
- K144 (= K250) binding
- D167 (= D273) binding
- N170 (= N276) binding
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
40% identity, 63% coverage: 109:313/323 of query aligns to 2:206/210 of 1f5sA
- active site: D10 (= D117), F11 (≠ M118), D12 (= D119), G99 (= G206), K143 (= K250), D170 (= D277)
- binding magnesium ion: D10 (= D117), D12 (= D119), D166 (= D273)
- binding phosphate ion: D10 (= D117), F11 (≠ M118), D12 (= D119), S98 (= S205), G99 (= G206), K143 (= K250)
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
41% identity, 62% coverage: 109:309/323 of query aligns to 1:201/209 of 1l7nA
- active site: D9 (= D117), F10 (≠ M118), D11 (= D119), G98 (= G206), K142 (= K250), D169 (= D277)
- binding aluminum fluoride: D9 (= D117), F10 (≠ M118), D11 (= D119), S97 (= S205), K142 (= K250)
- binding tetrafluoroaluminate ion: D9 (= D117), F10 (≠ M118), D11 (= D119), S97 (= S205), G98 (= G206), K142 (= K250), N168 (= N276)
- binding magnesium ion: D9 (= D117), D11 (= D119), D165 (= D273)
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
42% identity, 61% coverage: 113:309/323 of query aligns to 4:200/208 of 1l7pA
- active site: N8 (≠ D117), F9 (≠ M118), D10 (= D119), G97 (= G206), K141 (= K250), D168 (= D277)
- binding phosphoserine: N8 (≠ D117), F9 (≠ M118), D10 (= D119), E17 (= E126), M40 (= M149), F46 (= F155), R53 (= R162), S96 (= S205), G97 (= G206), K141 (= K250)
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
42% identity, 64% coverage: 109:315/323 of query aligns to 78:285/295 of 7qplA
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
40% identity, 61% coverage: 113:309/323 of query aligns to 4:192/200 of 1l7oA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
39% identity, 61% coverage: 113:309/323 of query aligns to 5:200/208 of 3m1yC
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
34% identity, 55% coverage: 114:290/323 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)
34% identity, 55% coverage: 114:290/323 of query aligns to 14:193/222 of 1l8lA
- active site: D17 (= D117), V18 (≠ M118), D19 (= D119), G107 (= G206), K155 (= K250), D180 (= D277)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D117), D19 (= D119), G107 (= G206), K155 (= K250), D176 (= D273), G177 (= G274), T179 (≠ N276)
6hyjB Psph human phosphoserine phosphatase (see paper)
34% identity, 55% coverage: 114:290/323 of query aligns to 17:196/223 of 6hyjB
Sites not aligning to the query:
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
34% identity, 55% coverage: 114:290/323 of query aligns to 17:196/225 of P78330
- D20 (= D117) binding
- DVD 20:22 (≠ DMD 117:119) binding
- D22 (= D119) binding
- S23 (= S120) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E126) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D129) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A132) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M149) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ R150) binding
- R65 (= R162) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 205:207) binding ; binding
- N133 (= N227) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K250) binding ; binding
- D179 (= D273) binding
- T182 (≠ N276) 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%.
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
34% identity, 55% coverage: 114:290/323 of query aligns to 13:192/217 of 6q6jB
- binding calcium ion: D16 (= D117), D18 (= D119), D175 (= D273)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D117), V17 (≠ M118), D18 (= D119), F54 (= F155), S105 (= S205), G106 (= G206), G107 (= G207), K154 (= K250), T178 (≠ N276)
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
34% identity, 55% coverage: 114:290/323 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: 115:289/323 of query aligns to 13:174/200 of 4ap9A
- active site: D15 (= D117), I16 (≠ M118), E17 (≠ D119), G103 (= G206), K141 (= K250), D162 (= D277)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ K133), I32 (≠ L134), T33 (≠ A135), L46 (≠ M149), W52 (≠ F155), D140 (≠ Y249), K141 (= K250), Y160 (≠ A275), A161 (≠ N276)
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
26% identity, 53% coverage: 114:284/323 of query aligns to 17:186/585 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
>BWI76_RS04160 FitnessBrowser__Koxy:BWI76_RS04160
MPNSLTWCDLPEDVSLWPGLPLSLSGDEVMPLDYHAGRSGWLLYGRGLNKHRLTEWQREL
GAALVIVASWAVDDYQVMRLAGSLTLRATRLAHEAGFDVAPLGKIPHLRTPGLLVMDMDS
TAIQIECIDEIAKLAGTGELVSEVTERAMRGELDFTASLRQRVATLKDADASILLQVRES
LPLMPGLTQLVLKLETLGWKVAIASGGFTFFAEYLRDKLHLDAVFANELEIRDGKLTGNV
IGDIVDAKYKANTLRKLAEKYEIPPAQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNELA
EVTIRHADLMGVFCILSGSMNQK
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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