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Database: UniProt
Entry: U3GW37_9CORY
LinkDB: U3GW37_9CORY
Original site: U3GW37_9CORY 
ID   U3GW37_9CORY            Unreviewed;       429 AA.
AC   U3GW37;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00012640};
DE            EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
DE   AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000256|ARBA:ARBA00031693};
GN   ORFNames=CARG_08175 {ECO:0000313|EMBL:AGU15750.1};
OS   Corynebacterium argentoratense DSM 44202.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU15750.1, ECO:0000313|Proteomes:UP000016943};
RN   [1] {ECO:0000313|EMBL:AGU15750.1, ECO:0000313|Proteomes:UP000016943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU15750.1};
RX   PubMed=24092787;
RA   Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K.,
RA   Ruckert C., Tauch A.;
RT   "Whole-Genome Sequence of the Clinical Strain Corynebacterium
RT   argentoratense DSM 44202, Isolated from a Human Throat Specimen.";
RL   Genome Announc. 1:e00793-13(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC         Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001197};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC         Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000860};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 3/3. {ECO:0000256|ARBA:ARBA00005135}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {ECO:0000256|ARBA:ARBA00009184}.
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DR   EMBL; CP006365; AGU15750.1; -; Genomic_DNA.
DR   RefSeq; WP_021012142.1; NC_022198.1.
DR   AlphaFoldDB; U3GW37; -.
DR   STRING; 1348662.CARG_08175; -.
DR   GeneID; 78250380; -.
DR   KEGG; caz:CARG_08175; -.
DR   PATRIC; fig|1348662.3.peg.1618; -.
DR   eggNOG; COG0560; Bacteria.
DR   eggNOG; COG3830; Bacteria.
DR   HOGENOM; CLU_036368_1_2_11; -.
DR   OrthoDB; 9792539at2; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000016943; Chromosome.
DR   GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd04870; ACT_PSP_1; 1.
DR   CDD; cd04871; ACT_PSP_2; 1.
DR   CDD; cd07500; HAD_PSP; 1.
DR   Gene3D; 3.30.70.260; -; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004469; PSP.
DR   InterPro; IPR049148; PSP_ACT.
DR   NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR   NCBIfam; TIGR00338; serB; 1.
DR   PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1.
DR   PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1.
DR   Pfam; PF13740; ACT_6; 1.
DR   Pfam; PF21086; ACT_PSP_2; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016943};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          23..97
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        201
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ   SEQUENCE   429 AA;  45591 MW;  31A2EFCF1A22E3EA CRC64;
     MNSSTSLASD ITVNLSPGLV PAVVIVSGAD RPGVSGAFFR VLASHQVQLL DVEQSQFRGR
     LNLASLIGVD PARVETLKEG LSETLRGYGQ SVSVEVQETL HSTRPLSTHA VVVLGDPVTA
     SHVSRIGQTL ADYGANIDTI RGIADYPLTG LELSVTVADP TPGGGVAMRK ALAELTRQIG
     VDIAIERAGL QRRSKRLICF DCDSTLITGE VIEMLAARAG REAEVAEVTA RAMRGELDFE
     ESLRERVQAL AGLDASVIDD VAAEIELTPG ARTTIRTLKR MGYKAAVVSG GFIQVLEDLA
     QELDLDYVRA NTLEIVDGKL TGRVVGKVVD RAAKAEFLSE FAADSGLKMH QTVAVGDGAN
     DIDMLSAAGL GIAFNAKPAL REVADASVNH PFLDEVLYIL GISRTEIDNE DLSDGSFRRV
     PLTTSETNT
//
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