SitesBLAST
Comparing WP_007474112.1 NCBI__GCF_000170735.1:WP_007474112.1 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)
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
55% identity, 100% coverage: 2:206/206 of query aligns to 4:207/208 of 3m1yC
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)
50% identity, 100% coverage: 2:206/206 of query aligns to 6:210/211 of Q58989
- D11 (= D7) active site, Nucleophile; binding Mg(2+); mutation to N: Loss of activity.
- D13 (= D9) active site, Proton donor; binding Mg(2+)
- E20 (= E16) binding substrate
- R56 (= R52) binding substrate
- SG 99:100 (= SG 95:96) binding substrate
- K144 (= K140) binding substrate
- D167 (= D163) binding Mg(2+)
- N170 (= N166) binding substrate
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
50% identity, 100% coverage: 2:206/206 of query aligns to 5:209/210 of 1f5sA
- active site: D10 (= D7), F11 (= F8), D12 (= D9), G99 (= G96), K143 (= K140), D170 (= D167)
- binding magnesium ion: D10 (= D7), D12 (= D9), D166 (= D163)
- binding phosphate ion: D10 (= D7), F11 (= F8), D12 (= D9), S98 (= S95), G99 (= G96), K143 (= K140)
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
50% identity, 100% coverage: 2:206/206 of query aligns to 4:208/209 of 1l7nA
- active site: D9 (= D7), F10 (= F8), D11 (= D9), G98 (= G96), K142 (= K140), D169 (= D167)
- binding aluminum fluoride: D9 (= D7), F10 (= F8), D11 (= D9), S97 (= S95), K142 (= K140)
- binding tetrafluoroaluminate ion: D9 (= D7), F10 (= F8), D11 (= D9), S97 (= S95), G98 (= G96), K142 (= K140), N168 (= N166)
- binding magnesium ion: D9 (= D7), D11 (= D9), D165 (= D163)
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
50% identity, 100% coverage: 2:206/206 of query aligns to 3:207/208 of 1l7pA
- active site: N8 (≠ D7), F9 (= F8), D10 (= D9), G97 (= G96), K141 (= K140), D168 (= D167)
- binding phosphoserine: N8 (≠ D7), F9 (= F8), D10 (= D9), E17 (= E16), M40 (= M39), F46 (= F45), R53 (= R52), S96 (= S95), G97 (= G96), K141 (= K140)
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
48% identity, 100% coverage: 2:206/206 of query aligns to 3:199/200 of 1l7oA
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)
42% identity, 98% coverage: 2:203/206 of query aligns to 180:381/409 of O53289
- D185 (= D7) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ F8) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D9) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S10) mutation to A: No effect on enzymatic activity.
- S273 (= S95) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K140) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D163) 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 (= D167) 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.
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
41% identity, 98% coverage: 2:203/206 of query aligns to 178:379/396 of 8a21A
- binding magnesium ion: D183 (= D7), D185 (= D9), D339 (= D163)
- binding 4-phenyl-1h-imidazole: D185 (= D9), E192 (= E16), V193 (≠ T17), I194 (= I18), T211 (= T35), M215 (= M39), F221 (= F45), R228 (= R52), G273 (= G97)
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)
41% identity, 98% coverage: 2:203/206 of query aligns to 178:379/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D9), E192 (= E16), M215 (= M39), F221 (= F45), L225 (= L49), R228 (= R52), G272 (= G96), F274 (= F98), D339 (= D163)
- binding magnesium ion: D183 (= D7), D185 (= D9), D339 (= D163)
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
41% identity, 98% coverage: 2:203/206 of query aligns to 182:383/411 of A0QJI1
- D187 (= D7) binding Mg(2+)
- D189 (= D9) binding Mg(2+)
- D343 (= D163) binding Mg(2+)
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
41% identity, 98% coverage: 2:203/206 of query aligns to 178:379/396 of 5jlpA
Sites not aligning to the query:
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
37% identity, 98% coverage: 2:203/206 of query aligns to 81:283/295 of 7qplA
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
29% identity, 85% coverage: 6:180/206 of query aligns to 15:192/221 of 6hyyA
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
29% identity, 85% coverage: 6:180/206 of query aligns to 15:192/217 of 6q6jB
- binding calcium ion: D16 (= D7), D18 (= D9), D175 (= D163)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D7), V17 (≠ F8), D18 (= D9), F54 (= F45), S105 (= S95), G106 (= G96), G107 (= G97), K154 (= K140), T178 (≠ N166)
6hyjB Psph human phosphoserine phosphatase (see paper)
29% identity, 85% coverage: 6:180/206 of query aligns to 19:196/223 of 6hyjB
Sites not aligning to the query:
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
29% identity, 100% coverage: 2:206/206 of query aligns to 10:196/200 of 4ap9A
- active site: D15 (= D7), I16 (≠ F8), E17 (≠ D9), G103 (= G96), K141 (= K140), D162 (= D167)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ E23), I32 (≠ P24), T33 (≠ L25), L46 (≠ M39), W52 (≠ F45), D140 (≠ S139), K141 (= K140), Y160 (≠ A165), A161 (≠ N166)
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
29% identity, 85% coverage: 6:180/206 of query aligns to 19:196/225 of P78330
- D20 (= D7) binding Mg(2+)
- DVD 20:22 (≠ DFD 7:9) binding L-serine
- D22 (= D9) binding Mg(2+)
- S23 (= S10) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E16) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D19) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A22) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M39) binding O-phospho-L-serine; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ R40) binding phosphate
- R65 (= R52) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 95:97) binding L-serine; binding O-phospho-L-serine
- N133 (≠ S121) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K140) binding L-serine; binding O-phospho-L-serine
- D179 (= D163) binding Mg(2+)
- T182 (≠ N166) binding O-phospho-L-serine; binding phosphate; 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%.
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
29% identity, 85% coverage: 6:180/206 of query aligns to 16:193/222 of 1l8oA
Sites not aligning to the query:
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
29% identity, 85% coverage: 6:180/206 of query aligns to 16:193/222 of 1l8lA
- active site: D17 (= D7), V18 (≠ F8), D19 (= D9), G107 (= G96), K155 (= K140), D180 (= D167)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D7), D19 (= D9), G107 (= G96), K155 (= K140), D176 (= D163), G177 (= G164), T179 (≠ N166)
3kd3A Crystal structure of a phosphoserine phosphohydrolase-like protein from francisella tularensis subsp. Tularensis schu s4
28% identity, 87% coverage: 1:180/206 of query aligns to 1:188/216 of 3kd3A
Query Sequence
>WP_007474112.1 NCBI__GCF_000170735.1:WP_007474112.1
MKLAVFDFDSTLMDGETIDFLAEPLGFKDKVASITEMAMRGELDFFESLIMRVKLLEGLE
DKKVNEICHNLPYMPGADETIKALKKDGYKVVVFSGGFRNATSYAKEILGFDADFSNILH
SKNGRLTGLVGGEMMFSHSKGDMLKRLQAILGISIEDTLVVGDGANDLSMFKYAGTRIAF
CAKDVLKKEANVIIEEKDLTKILEFI
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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