SitesBLAST
Comparing WP_012708549.1 NCBI__GCF_000018545.1:WP_012708549.1 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
69% identity, 99% coverage: 1:293/295 of query aligns to 1:293/295 of 7qplA
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
44% identity, 71% coverage: 78:286/295 of query aligns to 2:210/210 of 1f5sA
- active site: D10 (= D86), F11 (≠ M87), D12 (= D88), G99 (= G176), K143 (= K220), D170 (= D247)
- binding magnesium ion: D10 (= D86), D12 (= D88), D166 (= D243)
- binding phosphate ion: D10 (= D86), F11 (≠ M87), D12 (= D88), S98 (= S175), G99 (= G176), K143 (= K220)
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, 71% coverage: 78:286/295 of query aligns to 3:211/211 of Q58989
- D11 (= D86) active site, Nucleophile; binding Mg(2+); mutation to N: Loss of activity.
- D13 (= D88) active site, Proton donor; binding Mg(2+)
- E20 (= E95) binding substrate
- R56 (= R131) binding substrate
- SG 99:100 (= SG 175:176) binding substrate
- K144 (= K220) binding substrate
- D167 (= D243) binding Mg(2+)
- N170 (= N246) binding substrate
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
44% identity, 71% coverage: 78:286/295 of query aligns to 1:209/209 of 1l7nA
- active site: D9 (= D86), F10 (≠ M87), D11 (= D88), G98 (= G176), K142 (= K220), D169 (= D247)
- binding aluminum fluoride: D9 (= D86), F10 (≠ M87), D11 (= D88), S97 (= S175), K142 (= K220)
- binding tetrafluoroaluminate ion: D9 (= D86), F10 (≠ M87), D11 (= D88), S97 (= S175), G98 (= G176), K142 (= K220), N168 (= N246)
- binding magnesium ion: D9 (= D86), D11 (= D88), D165 (= D243)
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
44% identity, 71% coverage: 79:286/295 of query aligns to 1:208/208 of 1l7pA
- active site: N8 (≠ D86), F9 (≠ M87), D10 (= D88), G97 (= G176), K141 (= K220), D168 (= D247)
- binding phosphoserine: N8 (≠ D86), F9 (≠ M87), D10 (= D88), E17 (= E95), M40 (= M118), F46 (= F124), R53 (= R131), S96 (= S175), G97 (= G176), K141 (= K220)
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
41% identity, 93% coverage: 22:295/295 of query aligns to 114:391/396 of 8a21A
- binding magnesium ion: D183 (= D86), D185 (= D88), D339 (= D243)
- binding 4-phenyl-1h-imidazole: D185 (= D88), E192 (= E95), V193 (≠ C96), I194 (= I97), T211 (= T114), M215 (= M118), F221 (= F124), R228 (= R131), G273 (= G177)
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, 93% coverage: 22:295/295 of query aligns to 114:391/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D88), E192 (= E95), M215 (= M118), F221 (= F124), L225 (= L128), R228 (= R131), G272 (= G176), F274 (= F178), D339 (= D243)
- binding magnesium ion: D183 (= D86), D185 (= D88), D339 (= D243)
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
41% identity, 93% coverage: 22:295/295 of query aligns to 118:395/411 of A0QJI1
- D187 (= D86) binding Mg(2+)
- D189 (= D88) binding Mg(2+)
- D343 (= D243) binding Mg(2+)
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
41% identity, 93% coverage: 22:295/295 of query aligns to 114:391/396 of 5jlpA
Sites not aligning to the query:
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, 77% coverage: 68:295/295 of query aligns to 165:393/409 of O53289
- D185 (= D86) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M87) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D88) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S89) mutation to A: No effect on enzymatic activity.
- S273 (= S175) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K220) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D243) 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 (= D247) 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)
43% identity, 71% coverage: 79:286/295 of query aligns to 1:200/200 of 1l7oA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
35% identity, 68% coverage: 80:280/295 of query aligns to 3:201/208 of 3m1yC
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
34% identity, 55% coverage: 86:248/295 of query aligns to 17:181/222 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: 86:248/295 of query aligns to 17:181/222 of 1l8lA
- active site: D17 (= D86), V18 (≠ M87), D19 (= D88), G107 (= G176), K155 (= K220), D180 (= D247)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D86), D19 (= D88), G107 (= G176), K155 (= K220), D176 (= D243), G177 (= G244), T179 (≠ N246)
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: 86:248/295 of query aligns to 20:184/225 of P78330
- D20 (= D86) binding Mg(2+)
- DVD 20:22 (≠ DMD 86:88) binding L-serine
- D22 (= D88) binding Mg(2+)
- S23 (= S89) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E95) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D98) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A101) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M118) binding O-phospho-L-serine; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ N119) binding phosphate
- R65 (= R131) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 175:177) binding L-serine; binding O-phospho-L-serine
- N133 (= N197) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K220) binding L-serine; binding O-phospho-L-serine
- D179 (= D243) binding Mg(2+)
- T182 (≠ N246) 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%.
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
34% identity, 55% coverage: 86:248/295 of query aligns to 16:180/217 of 6q6jB
- binding calcium ion: D16 (= D86), D18 (= D88), D175 (= D243)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D86), V17 (≠ M87), D18 (= D88), F54 (= F124), S105 (= S175), G106 (= G176), G107 (= G177), K154 (= K220), T178 (≠ N246)
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
34% identity, 55% coverage: 86:248/295 of query aligns to 16:180/221 of 6hyyA
6hyjB Psph human phosphoserine phosphatase (see paper)
34% identity, 55% coverage: 86:248/295 of query aligns to 20:184/223 of 6hyjB
Sites not aligning to the query:
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
28% identity, 61% coverage: 80:260/295 of query aligns to 9:175/200 of 4ap9A
- active site: D15 (= D86), I16 (≠ M87), E17 (≠ D88), G103 (= G176), K141 (≠ I227), D162 (= D247)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ A102), I32 (≠ E103), T33 (≠ V104), L46 (≠ M118), W52 (≠ F124), D140 (= D226), K141 (≠ I227), Y160 (≠ A245), A161 (≠ N246)
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
29% identity, 63% coverage: 86:270/295 of query aligns to 20:209/585 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
Query Sequence
>WP_012708549.1 NCBI__GCF_000018545.1:WP_012708549.1
MALVATLIANPSNPVLTPALAEAAAEAVQASGLYWLADGIACDLALRDGTDPNDAEARLR
AAINGAAIDVAVQEAETRRKKFLIADMDSTMIGQECIDELAAEVGLKEKVAAITARAMNG
EIAFEPALIERVALLKGLPTTVIAEVIAKRITLTPGGRELIATMKAKGHYTALVSGGFTV
FTGPIAEKLGFDENRANELLEENGALTGDVARPILGRQAKVDALIDISERLGISTADVIA
VGDGANDLGMLQLAGSGVALHAKPVVAEQAKIRIDHGDLSALLYLQGYRKTDFAA
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