SitesBLAST
Comparing AO353_13070 FitnessBrowser__pseudo3_N2E3:AO353_13070 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)
41% identity, 97% coverage: 5:396/404 of query aligns to 7:385/409 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 (≠ E110) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- D185 (= D196) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M197) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D198) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S199) mutation to A: No effect on enzymatic activity.
- S273 (= S284) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K329) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D352) 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 (= D356) 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)
41% identity, 97% coverage: 5:396/404 of query aligns to 5:383/396 of 8a21A
- binding magnesium ion: D183 (= D196), D185 (= D198), D339 (= D352)
- binding 4-phenyl-1h-imidazole: D13 (= D13), T18 (= T18), Q37 (= Q37), D185 (= D198), E192 (= E205), V193 (= V206), I194 (= I207), T211 (= T224), M215 (= M228), F221 (= F234), R228 (= R241), G273 (= G286)
8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
41% identity, 97% coverage: 5:396/404 of query aligns to 5:383/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D198), E192 (= E205), M215 (= M228), F221 (= F234), L225 (≠ F238), R228 (= R241), G272 (= G285), F274 (= F287), D339 (= D352)
- binding magnesium ion: D183 (= D196), D185 (= D198), D339 (= D352)
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
41% identity, 97% coverage: 5:396/404 of query aligns to 5:383/396 of 5jlpA
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
41% identity, 97% coverage: 5:396/404 of query aligns to 9:387/411 of A0QJI1
- D187 (= D196) binding
- D189 (= D198) binding
- D343 (= D352) binding
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
44% identity, 51% coverage: 188:392/404 of query aligns to 2:206/210 of 1f5sA
- active site: D10 (= D196), F11 (≠ M197), D12 (= D198), G99 (= G285), K143 (= K329), D170 (= D356)
- binding magnesium ion: D10 (= D196), D12 (= D198), D166 (= D352)
- binding phosphate ion: D10 (= D196), F11 (≠ M197), D12 (= D198), S98 (= S284), G99 (= G285), K143 (= K329)
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)
43% identity, 51% coverage: 186:392/404 of query aligns to 1:207/211 of Q58989
- D11 (= D196) active site, Nucleophile; binding ; mutation to N: Loss of activity.
- D13 (= D198) active site, Proton donor; binding
- E20 (= E205) binding
- R56 (= R241) binding
- SG 99:100 (= SG 284:285) binding
- K144 (= K329) binding
- D167 (= D352) binding
- N170 (= N355) binding
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
44% identity, 51% coverage: 188:392/404 of query aligns to 1:205/209 of 1l7nA
- active site: D9 (= D196), F10 (≠ M197), D11 (= D198), G98 (= G285), K142 (= K329), D169 (= D356)
- binding aluminum fluoride: D9 (= D196), F10 (≠ M197), D11 (= D198), S97 (= S284), K142 (= K329)
- binding tetrafluoroaluminate ion: D9 (= D196), F10 (≠ M197), D11 (= D198), S97 (= S284), G98 (= G285), K142 (= K329), N168 (= N355)
- binding magnesium ion: D9 (= D196), D11 (= D198), D165 (= D352)
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
44% identity, 56% coverage: 176:401/404 of query aligns to 68:292/295 of 7qplA
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
44% identity, 50% coverage: 190:392/404 of query aligns to 2:204/208 of 1l7pA
- active site: N8 (≠ D196), F9 (≠ M197), D10 (= D198), G97 (= G285), K141 (= K329), D168 (= D356)
- binding phosphoserine: N8 (≠ D196), F9 (≠ M197), D10 (= D198), E17 (= E205), M40 (= M228), F46 (= F234), R53 (= R241), S96 (= S284), G97 (= G285), K141 (= K329)
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
42% identity, 50% coverage: 190:392/404 of query aligns to 2:196/200 of 1l7oA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
37% identity, 48% coverage: 190:384/404 of query aligns to 3:196/208 of 3m1yC
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
35% identity, 47% coverage: 194:384/404 of query aligns to 15:211/222 of 1l8oA
- active site: D17 (= D196), V18 (≠ M197), D19 (= D198), G107 (= G285), K155 (= K329), D180 (= D356)
- binding phosphate ion: D17 (= D196), D19 (= D198), S106 (= S284), K155 (= K329)
- binding serine: G177 (= G353), T179 (≠ N355), R199 (vs. gap)
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
35% identity, 47% coverage: 194:384/404 of query aligns to 15:211/222 of 1l8lA
- active site: D17 (= D196), V18 (≠ M197), D19 (= D198), G107 (= G285), K155 (= K329), D180 (= D356)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D196), D19 (= D198), G107 (= G285), K155 (= K329), D176 (= D352), G177 (= G353), T179 (≠ N355)
6hyjB Psph human phosphoserine phosphatase (see paper)
35% identity, 47% coverage: 194:384/404 of query aligns to 18:214/223 of 6hyjB
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
35% identity, 47% coverage: 194:384/404 of query aligns to 18:214/225 of P78330
- D20 (= D196) binding
- DVD 20:22 (≠ DMD 196:198) binding
- D22 (= D198) binding
- S23 (= S199) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E205) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D208) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A211) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M228) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ A229) binding
- R65 (= R241) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 284:286) binding ; binding
- N133 (= N306) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K329) binding ; binding
- D179 (= D352) binding
- T182 (≠ N355) 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 (vs. gap) mutation to A: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to K: Reduces L-phosphoserine phosphatase activity by about 95%.
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
35% identity, 47% coverage: 194:384/404 of query aligns to 14:210/221 of 6hyyA
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
35% identity, 47% coverage: 194:384/404 of query aligns to 14:210/217 of 6q6jB
- binding calcium ion: D16 (= D196), D18 (= D198), D175 (= D352)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D196), V17 (≠ M197), D18 (= D198), F54 (= F234), S105 (= S284), G106 (= G285), G107 (= G286), K154 (= K329), T178 (≠ N355)
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
27% identity, 44% coverage: 190:368/404 of query aligns to 9:174/200 of 4ap9A
- active site: D15 (= D196), I16 (≠ M197), E17 (≠ D198), G103 (= G285), K141 (= K329), D162 (= D356)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ K212), I32 (≠ A213), T33 (≠ A214), L46 (≠ M228), W52 (≠ F234), D140 (≠ R328), K141 (= K329), Y160 (≠ A354), A161 (≠ N355)
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
30% identity, 41% coverage: 194:357/404 of query aligns to 18:180/585 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
>AO353_13070 FitnessBrowser__pseudo3_N2E3:AO353_13070
LREIVLINITGVDRPGLTAAITGVLAQGGVNILDIGQAVIHDTLSFGILVEIPDTEQGSS
VLKDILFKAYELGQQVRFTPVSEEDYQLWVGAQGKKRHIVTLLTRKVTAEQLQRVSSITA
KYGLNIDHIDRLSGRMPLDTPADKGKGCIEFSVRGEAADPQALRAEFLSVAQELNVDIAF
QEDSLFRRNRRLAVFDMDSTLIEAEVIDELAKAAGVGEKVSEITERAMAGELDFRASFKE
RLALLKGLDVSVLDSIGASLRLTEGAETLFAELKRLGYKTAILSGGFTYFAKQLQAKLGI
DYVFANELEVVDGKVTGVAVEPIVDAQRKADLLRELAHKEGLRLEQTIAVGDGANDLPML
AIAGLGVAFRAKPLVKQSAKQAISTLGLDGVLYLLGFRDRDGQL
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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