SitesBLAST
Comparing WP_013835004.1 NCBI__GCF_000214825.1:WP_013835004.1 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
42% identity, 82% coverage: 48:273/277 of query aligns to 57:283/295 of 7qplA
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)
44% identity, 75% coverage: 71:277/277 of query aligns to 180:385/409 of O53289
- D185 (= D76) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M77) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D78) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S79) mutation to A: No effect on enzymatic activity.
- S273 (= S165) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K210) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D233) 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 (= D237) 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.
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
41% identity, 70% coverage: 71:263/277 of query aligns to 5:197/210 of 1f5sA
- active site: D10 (= D76), F11 (≠ M77), D12 (= D78), G99 (= G166), K143 (= K210), D170 (= D237)
- binding magnesium ion: D10 (= D76), D12 (= D78), D166 (= D233)
- binding phosphate ion: D10 (= D76), F11 (≠ M77), D12 (= D78), S98 (= S165), G99 (= G166), K143 (= K210)
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, 70% coverage: 71:263/277 of query aligns to 6:198/211 of Q58989
- D11 (= D76) active site, Nucleophile; binding Mg(2+); mutation to N: Loss of activity.
- D13 (= D78) active site, Proton donor; binding Mg(2+)
- E20 (= E85) binding substrate
- R56 (= R121) binding substrate
- SG 99:100 (= SG 165:166) binding substrate
- K144 (= K210) binding substrate
- D167 (= D233) binding Mg(2+)
- N170 (= N236) binding substrate
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
41% identity, 70% coverage: 71:263/277 of query aligns to 4:196/209 of 1l7nA
- active site: D9 (= D76), F10 (≠ M77), D11 (= D78), G98 (= G166), K142 (= K210), D169 (= D237)
- binding aluminum fluoride: D9 (= D76), F10 (≠ M77), D11 (= D78), S97 (= S165), K142 (= K210)
- binding tetrafluoroaluminate ion: D9 (= D76), F10 (≠ M77), D11 (= D78), S97 (= S165), G98 (= G166), K142 (= K210), N168 (= N236)
- binding magnesium ion: D9 (= D76), D11 (= D78), D165 (= D233)
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
44% identity, 75% coverage: 71:277/277 of query aligns to 182:387/411 of A0QJI1
- D187 (= D76) binding Mg(2+)
- D189 (= D78) binding Mg(2+)
- D343 (= D233) binding Mg(2+)
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
44% identity, 75% coverage: 71:277/277 of query aligns to 178:383/396 of 8a21A
- binding magnesium ion: D183 (= D76), D185 (= D78), D339 (= D233)
- binding 4-phenyl-1h-imidazole: D185 (= D78), E192 (= E85), V193 (≠ C86), I194 (= I87), T211 (= T104), M215 (= M108), F221 (= F114), R228 (= R121), G273 (= G167)
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)
44% identity, 75% coverage: 71:277/277 of query aligns to 178:383/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D78), E192 (= E85), M215 (= M108), F221 (= F114), L225 (= L118), R228 (= R121), G272 (= G166), F274 (= F168), D339 (= D233)
- binding magnesium ion: D183 (= D76), D185 (= D78), D339 (= D233)
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
44% identity, 75% coverage: 71:277/277 of query aligns to 178:383/396 of 5jlpA
Sites not aligning to the query:
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
41% identity, 70% coverage: 71:263/277 of query aligns to 3:195/208 of 1l7pA
- active site: N8 (≠ D76), F9 (≠ M77), D10 (= D78), G97 (= G166), K141 (= K210), D168 (= D237)
- binding phosphoserine: N8 (≠ D76), F9 (≠ M77), D10 (= D78), E17 (= E85), M40 (= M108), F46 (= F114), R53 (= R121), S96 (= S165), G97 (= G166), K141 (= K210)
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
39% identity, 70% coverage: 71:263/277 of query aligns to 3:187/200 of 1l7oA
Sites not aligning to the query:
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
35% identity, 70% coverage: 71:265/277 of query aligns to 4:196/208 of 3m1yC
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
31% identity, 60% coverage: 73:238/277 of query aligns to 14:181/222 of 1l8oA
Sites not aligning to the query:
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
31% identity, 60% coverage: 73:238/277 of query aligns to 14:181/222 of 1l8lA
- active site: D17 (= D76), V18 (≠ M77), D19 (= D78), G107 (= G166), K155 (≠ Q208), D180 (= D237)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D76), D19 (= D78), G107 (= G166), K155 (≠ Q208), D176 (= D233), G177 (= G234), T179 (≠ N236)
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
30% identity, 60% coverage: 73:238/277 of query aligns to 17:184/225 of P78330
- D20 (= D76) binding Mg(2+)
- DVD 20:22 (≠ DMD 76:78) binding L-serine
- D22 (= D78) binding Mg(2+)
- S23 (= S79) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E85) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D88) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A91) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M108) binding O-phospho-L-serine; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ R109) binding phosphate
- R65 (= R121) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 165:167) binding L-serine; binding O-phospho-L-serine
- N133 (= N187) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (≠ Q208) binding L-serine; binding O-phospho-L-serine
- D179 (= D233) binding Mg(2+)
- T182 (≠ N236) 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%.
6hyjB Psph human phosphoserine phosphatase (see paper)
30% identity, 60% coverage: 73:238/277 of query aligns to 17:184/223 of 6hyjB
Sites not aligning to the query:
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
30% identity, 60% coverage: 73:238/277 of query aligns to 13:180/221 of 6hyyA
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
30% identity, 60% coverage: 73:238/277 of query aligns to 13:180/217 of 6q6jB
- binding calcium ion: D16 (= D76), D18 (= D78), D175 (= D233)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D76), V17 (≠ M77), D18 (= D78), F54 (= F114), S105 (= S165), G106 (= G166), G107 (= G167), K154 (≠ Q208), T178 (≠ N236)
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
27% identity, 65% coverage: 71:249/277 of query aligns to 10:174/200 of 4ap9A
- active site: D15 (= D76), I16 (≠ M77), E17 (≠ D78), G103 (= G166), K141 (= K210), D162 (= D237)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ D92), I32 (≠ M93), T33 (≠ F94), L46 (≠ M108), W52 (≠ F114), D140 (≠ A209), K141 (= K210), Y160 (≠ A235), A161 (≠ N236)
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
30% identity, 39% coverage: 73:181/277 of query aligns to 17:127/585 of 6iuyA
Sites not aligning to the query:
- binding magnesium ion: 175
- binding nicotinamide-adenine-dinucleotide: 233, 234, 235, 236, 268, 290, 321, 324, 349, 381, 382, 497, 529, 530, 532
Query Sequence
>WP_013835004.1 NCBI__GCF_000214825.1:WP_013835004.1
MKHTLVIHHNQLDQVQKDQLSASIGEPFPHNNHWRIISEQTINAPDLAELRHQLQLDINI
LPNDFEPAEVKLVISDMDSTLISIECIDEIADMFHIKPQVAAITESAMRGELNFEQSLTQ
RVTLLRGLDEKALDRVYNERLQLNPGAETWISGLKARDIKFALVSGGFDFFTSRLANRLN
LDFSRANKLAIEQGVLTGSVVGSIVGAQAKADFLHELCQHLAITPKQVIAIGDGANDLLM
MKAAGLSMAYHAKPTVQAQANCVLNYIGLDAMLDLLA
Or try a new SitesBLAST search
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