SitesBLAST
Comparing WP_020175090.1 NCBI__GCF_000385335.1:WP_020175090.1 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)
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
48% identity, 90% coverage: 4:296/324 of query aligns to 4:293/295 of 7qplA
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
41% identity, 65% coverage: 81:289/324 of query aligns to 2:210/210 of 1f5sA
- active site: D10 (= D89), F11 (≠ M90), D12 (= D91), G99 (= G180), K143 (= K223), D170 (= D250)
- binding magnesium ion: D10 (= D89), D12 (= D91), D166 (= D246)
- binding phosphate ion: D10 (= D89), F11 (≠ M90), D12 (= D91), S98 (= S179), G99 (= G180), K143 (= K223)
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, 65% coverage: 81:289/324 of query aligns to 3:211/211 of Q58989
- D11 (= D89) active site, Nucleophile; binding Mg(2+); mutation to N: Loss of activity.
- D13 (= D91) active site, Proton donor; binding Mg(2+)
- E20 (= E98) binding substrate
- R56 (= R134) binding substrate
- SG 99:100 (= SG 179:180) binding substrate
- K144 (= K223) binding substrate
- D167 (= D246) binding Mg(2+)
- N170 (= N249) binding substrate
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
41% identity, 65% coverage: 81:289/324 of query aligns to 1:209/209 of 1l7nA
- active site: D9 (= D89), F10 (≠ M90), D11 (= D91), G98 (= G180), K142 (= K223), D169 (= D250)
- binding aluminum fluoride: D9 (= D89), F10 (≠ M90), D11 (= D91), S97 (= S179), K142 (= K223)
- binding tetrafluoroaluminate ion: D9 (= D89), F10 (≠ M90), D11 (= D91), S97 (= S179), G98 (= G180), K142 (= K223), N168 (= N249)
- binding magnesium ion: D9 (= D89), D11 (= D91), D165 (= D246)
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
40% identity, 64% coverage: 82:289/324 of query aligns to 1:208/208 of 1l7pA
- active site: N8 (≠ D89), F9 (≠ M90), D10 (= D91), G97 (= G180), K141 (= K223), D168 (= D250)
- binding phosphoserine: N8 (≠ D89), F9 (≠ M90), D10 (= D91), E17 (= E98), M40 (= M121), F46 (= F127), R53 (= R134), S96 (= S179), G97 (= G180), K141 (= K223)
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
34% identity, 79% coverage: 45:300/324 of query aligns to 140:393/396 of 8a21A
- binding magnesium ion: D183 (= D89), D185 (= D91), D339 (= D246)
- binding 4-phenyl-1h-imidazole: D185 (= D91), E192 (= E98), V193 (≠ C99), I194 (= I100), T211 (= T117), M215 (= M121), F221 (= F127), R228 (= R134), G273 (= G180)
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)
34% identity, 79% coverage: 45:300/324 of query aligns to 140:393/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D91), E192 (= E98), M215 (= M121), F221 (= F127), L225 (= L131), R228 (= R134), G272 (≠ S179), F274 (= F181), D339 (= D246)
- binding magnesium ion: D183 (= D89), D185 (= D91), D339 (= D246)
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
34% identity, 79% coverage: 45:300/324 of query aligns to 140:393/396 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)
34% identity, 79% coverage: 45:300/324 of query aligns to 144:397/411 of A0QJI1
- D187 (= D89) binding Mg(2+)
- D189 (= D91) binding Mg(2+)
- D343 (= D246) binding Mg(2+)
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)
35% identity, 68% coverage: 81:300/324 of query aligns to 177:395/409 of O53289
- D185 (= D89) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M90) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D91) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S92) mutation to A: No effect on enzymatic activity.
- S273 (≠ T178) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K223) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D246) 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 (= D250) 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.
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
39% identity, 64% coverage: 82:289/324 of query aligns to 1:200/200 of 1l7oA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
30% identity, 62% coverage: 83:282/324 of query aligns to 3:200/208 of 3m1yC
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
30% identity, 56% coverage: 83:262/324 of query aligns to 9:174/200 of 4ap9A
- active site: D15 (= D89), I16 (≠ M90), E17 (≠ D91), G103 (≠ S179), K141 (= K233), D162 (= D250)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ Q105), I32 (≠ E106), T33 (≠ M107), L46 (≠ M121), W52 (≠ F127), D140 (≠ E232), K141 (= K233), Y160 (≠ A248), A161 (≠ N249)
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
28% identity, 54% coverage: 89:263/324 of query aligns to 16:192/217 of 6q6jB
- binding calcium ion: D16 (= D89), D18 (= D91), D175 (= D246)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D89), V17 (≠ M90), D18 (= D91), F54 (= F127), S105 (≠ T178), G106 (≠ S179), G107 (= G180), K154 (= K223), T178 (≠ N249)
6hyjB Psph human phosphoserine phosphatase (see paper)
28% identity, 54% coverage: 89:263/324 of query aligns to 20:196/223 of 6hyjB
Sites not aligning to the query:
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
28% identity, 54% coverage: 89:263/324 of query aligns to 17:193/222 of 1l8oA
Sites not aligning to the query:
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
28% identity, 54% coverage: 89:263/324 of query aligns to 17:193/222 of 1l8lA
- active site: D17 (= D89), V18 (≠ M90), D19 (= D91), G107 (≠ S179), K155 (= K223), D180 (= D250)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D89), D19 (= D91), G107 (≠ S179), K155 (= K223), D176 (= D246), G177 (= G247), T179 (≠ N249)
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
28% identity, 54% coverage: 89:263/324 of query aligns to 20:196/225 of P78330
- D20 (= D89) binding Mg(2+)
- DVD 20:22 (≠ DMD 89:91) binding L-serine
- D22 (= D91) binding Mg(2+)
- S23 (= S92) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E98) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (≠ N101) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A104) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M121) binding O-phospho-L-serine; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ A122) binding phosphate
- R65 (= R134) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (≠ TSG 178:180) binding L-serine; binding O-phospho-L-serine
- N133 (≠ A199) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K223) binding L-serine; binding O-phospho-L-serine
- D179 (= D246) binding Mg(2+)
- T182 (≠ N249) 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%.
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
28% identity, 54% coverage: 89:263/324 of query aligns to 16:192/221 of 6hyyA
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
26% identity, 57% coverage: 89:274/324 of query aligns to 20:210/585 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
>WP_020175090.1 NCBI__GCF_000385335.1:WP_020175090.1
MTHVATLVCDPSFPIVQASHLELAAGFLPGAQAPQWLDQGVAADITFTPQAGTDLRALAD
QIRAGLHPWQIDVVLQPVEGRRKKLLLADMDSTVIGQECINELAQEMGKRAQVTKITEQA
MAGEIDFETSLRERVTVIKNLRADTVNRILGKKITITNGARVLVQTMRANRAYTVLVTSG
FSAFAAPVTEKVGFNEFQANVLGVAENRFTGLLEEPVLGTEAKRDILIRLREKEFLPKVQ
VMAVGDGANDLAMLAEAGLGVAFHAKPAVAAAADARIDHADLTALLYLQGYQRSQFWSEE
RKELDASEWMKRYGWMARENSRKN
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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