SitesBLAST
Comparing WP_086511903.1 NCBI__GCF_002151265.1:WP_086511903.1 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)
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)
38% identity, 98% coverage: 5:400/406 of query aligns to 7:392/409 of O53289
- G18 (= G16) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- G108 (= G107) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- D185 (= D193) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M194) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D195) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S196) mutation to A: No effect on enzymatic activity.
- S273 (= S281) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K326) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D349) 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 (= D353) 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.
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
39% identity, 98% coverage: 5:400/406 of query aligns to 5:390/396 of 8a21A
- binding magnesium ion: D183 (= D193), D185 (= D195), D339 (= D349)
- binding 4-phenyl-1h-imidazole: D13 (≠ A13), T18 (≠ L18), Q37 (= Q37), D185 (= D195), E192 (= E202), V193 (= V203), I194 (= I204), T211 (= T221), M215 (= M225), F221 (= F231), R228 (= R238), G273 (= G283)
8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
39% identity, 98% coverage: 5:400/406 of query aligns to 5:390/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D195), E192 (= E202), M215 (= M225), F221 (= F231), L225 (≠ F235), R228 (= R238), G272 (= G282), F274 (= F284), D339 (= D349)
- binding magnesium ion: D183 (= D193), D185 (= D195), D339 (= D349)
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
39% identity, 98% coverage: 5:400/406 of query aligns to 5:390/396 of 5jlpA
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
39% identity, 98% coverage: 5:400/406 of query aligns to 9:394/411 of A0QJI1
- D187 (= D193) binding
- D189 (= D195) binding
- D343 (= D349) binding
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
46% identity, 56% coverage: 173:399/406 of query aligns to 68:293/295 of 7qplA
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
44% identity, 47% coverage: 185:376/406 of query aligns to 2:193/210 of 1f5sA
- active site: D10 (= D193), F11 (≠ M194), D12 (= D195), G99 (= G282), K143 (= K326), D170 (= D353)
- binding magnesium ion: D10 (= D193), D12 (= D195), D166 (= D349)
- binding phosphate ion: D10 (= D193), F11 (≠ M194), D12 (= D195), S98 (= S281), G99 (= G282), K143 (= K326)
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
44% identity, 47% coverage: 185:376/406 of query aligns to 1:192/209 of 1l7nA
- active site: D9 (= D193), F10 (≠ M194), D11 (= D195), G98 (= G282), K142 (= K326), D169 (= D353)
- binding aluminum fluoride: D9 (= D193), F10 (≠ M194), D11 (= D195), S97 (= S281), K142 (= K326)
- binding tetrafluoroaluminate ion: D9 (= D193), F10 (≠ M194), D11 (= D195), S97 (= S281), G98 (= G282), K142 (= K326), N168 (= N352)
- binding magnesium ion: D9 (= D193), D11 (= D195), D165 (= D349)
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)
44% identity, 47% coverage: 185:376/406 of query aligns to 3:194/211 of Q58989
- D11 (= D193) active site, Nucleophile; binding ; mutation to N: Loss of activity.
- D13 (= D195) active site, Proton donor; binding
- E20 (= E202) binding
- R56 (= R238) binding
- SG 99:100 (= SG 281:282) binding
- K144 (= K326) binding
- D167 (= D349) binding
- N170 (= N352) binding
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
43% identity, 47% coverage: 186:376/406 of query aligns to 1:191/208 of 1l7pA
- active site: N8 (≠ D193), F9 (≠ M194), D10 (= D195), G97 (= G282), K141 (= K326), D168 (= D353)
- binding phosphoserine: N8 (≠ D193), F9 (≠ M194), D10 (= D195), E17 (= E202), M40 (= M225), F46 (= F231), R53 (= R238), S96 (= S281), G97 (= G282), K141 (= K326)
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
41% identity, 47% coverage: 186:376/406 of query aligns to 1:183/200 of 1l7oA
Sites not aligning to the query:
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
37% identity, 48% coverage: 187:381/406 of query aligns to 3:196/208 of 3m1yC
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
31% identity, 52% coverage: 190:401/406 of query aligns to 14:222/222 of 1l8oA
- active site: D17 (= D193), V18 (≠ M194), D19 (= D195), G107 (= G282), K155 (= K326), D180 (= D353)
- binding phosphate ion: D17 (= D193), D19 (= D195), S106 (= S281), K155 (= K326)
- binding serine: G177 (= G350), T179 (≠ N352), R199 (= R373)
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
31% identity, 52% coverage: 190:401/406 of query aligns to 14:222/222 of 1l8lA
- active site: D17 (= D193), V18 (≠ M194), D19 (= D195), G107 (= G282), K155 (= K326), D180 (= D353)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D193), D19 (= D195), G107 (= G282), K155 (= K326), D176 (= D349), G177 (= G350), T179 (≠ N352)
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
31% identity, 52% coverage: 190:401/406 of query aligns to 13:221/221 of 6hyyA
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
31% identity, 49% coverage: 190:388/406 of query aligns to 13:213/217 of 6q6jB
- binding calcium ion: D16 (= D193), D18 (= D195), D175 (= D349)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D193), V17 (≠ M194), D18 (= D195), F54 (= F231), S105 (= S281), G106 (= G282), G107 (= G283), K154 (= K326), T178 (≠ N352)
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
31% identity, 52% coverage: 190:401/406 of query aligns to 17:225/225 of P78330
- D20 (= D193) binding
- DVD 20:22 (≠ DMD 193:195) binding
- D22 (= D195) binding
- S23 (= S196) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E202) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D205) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A208) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M225) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ R226) binding
- R65 (= R238) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 281:283) binding ; binding
- N133 (= N303) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K326) binding ; binding
- D179 (= D349) binding
- T182 (≠ N352) binding ; binding ; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.
- R202 (= R373) mutation to A: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to K: Reduces L-phosphoserine phosphatase activity by about 95%.
6hyjB Psph human phosphoserine phosphatase (see paper)
32% identity, 47% coverage: 190:379/406 of query aligns to 17:208/223 of 6hyjB
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
30% identity, 46% coverage: 190:376/406 of query aligns to 17:209/585 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
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
30% identity, 44% coverage: 187:365/406 of query aligns to 9:174/200 of 4ap9A
- active site: D15 (= D193), I16 (≠ M194), E17 (≠ D195), G103 (= G282), K141 (= K326), D162 (= D353)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (= R209), I32 (≠ R210), T33 (≠ H211), L46 (≠ M225), W52 (≠ F231), D140 (= D322), K141 (= K326), Y160 (≠ A351), A161 (≠ N352)
Query Sequence
>WP_086511903.1 NCBI__GCF_002151265.1:WP_086511903.1
MTRRLLIRATGAARPGQLAGLGQALARSGARLLDINQSVTFGMVSLEALVGLEHDSDLEG
ALNEVGDSLGLDVQAIQVSAEDYQRWSSQASEPRLILTLLAPHLPAGILAEVGALTAEHG
LTVELIHRLSGREPLDGGVPRFGSCVECWLRGEEIDLDSLREKALALGAMHGVDIAIQED
SIWRRHRRLVCFDMDSTLIQAEVIDELARRHGVYEEVAAVTERAMRGELDFQQSFRERMA
KLKGLDEAVLAEIAEELPLMDGVERLMKHLKRLGYRTAILSGGFTYFARHLQETLGFDEI
HANELVIENGKVTGEVREPILDASRKAELLREIAAREGLAMEQTIAVGDGANDLKMLAAA
GLGIAFRAKPLVRSQARQSISTLGIDAVLYLMGYREGDLEDDSRAG
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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