SitesBLAST

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)
29% identity, 47% coverage: 108:246/293 of query aligns to 229:368/409 of O53289

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O53289

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S273 (≠ T151) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
K318 (= K196) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
D341 (= D219) 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 (= D223) 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.
185 D→G: Completely abolishes enzymatic activity.; D→N: Completely abolishes enzymatic activity.
186 V→Q: Decreases enzymatic activity by 50%.
187 D→N: Decreases enzymatic activity by 15%.
188 S→A: No effect on enzymatic activity.

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)
34% identity, 29% coverage: 161:246/293 of query aligns to 109:194/211 of Q58989

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Q58989

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K144 (= K196) binding
D167 (= D219) binding
N170 (= N222) binding

Sites not aligning to the query:

11 active site, Nucleophile; binding ; D→N: Loss of activity.
13 active site, Proton donor; binding
20 binding
56 binding
99:100 binding

1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
34% identity, 29% coverage: 161:246/293 of query aligns to 106:191/208 of 1l7pA

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1l7pA

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active site: K141 (= K196), D168 (= D223)
binding phosphoserine: K141 (= K196)

Sites not aligning to the query:

active site: 8, 9, 10, 97
binding phosphoserine: 8, 9, 10, 17, 40, 46, 53, 96, 97

1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
34% identity, 29% coverage: 161:246/293 of query aligns to 107:192/209 of 1l7nA

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active site: K142 (= K196), D169 (= D223)
binding aluminum fluoride: K142 (= K196)
binding tetrafluoroaluminate ion: K142 (= K196), N168 (= N222)
binding magnesium ion: D165 (= D219)

Sites not aligning to the query:

active site: 9, 10, 11, 98
binding aluminum fluoride: 9, 10, 11, 97
binding tetrafluoroaluminate ion: 9, 10, 11, 97, 98
binding magnesium ion: 9, 11

1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
34% identity, 29% coverage: 161:246/293 of query aligns to 108:193/210 of 1f5sA

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1f5sA

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active site: K143 (= K196), D170 (= D223)
binding magnesium ion: D166 (= D219)
binding phosphate ion: K143 (= K196)

Sites not aligning to the query:

active site: 10, 11, 12, 99
binding magnesium ion: 10, 12
binding phosphate ion: 10, 11, 12, 98, 99

1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
34% identity, 29% coverage: 161:246/293 of query aligns to 98:183/200 of 1l7oA

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1l7oA

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Sites not aligning to the query:

binding zinc ion: 186, 188

Query Sequence

>WP_041938828.1 NCBI__GCF_000058485.1:WP_041938828.1
MRVRRRGVAETRQAAEAAAIAALKVAAEEVPRPPLDESAAAFFDVDNTMMAGASIFYFAR
GLAARDFFDSRDLLRFGWQHVTYRLRGHENPDGMRDARETALAFVAGRSVAEIVRYGEEI
YDERMAEQIYSGAHALAQQHLDAGQRVWLVTATPVELASVIARRLSLTGALGTVSEVTDG
TYTGHLVGGLLHGQAKAEAVQALAEREGLDLSRCWAYSDSINDLPMLSLVGHPVAINPDP
DLKTVAREREWPIKDFRTARKAVRIGIPAAAGAGALAGGVAAGMALRRRVASV

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