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Database: UniProt
Entry: K6Z4R5_9ALTE
LinkDB: K6Z4R5_9ALTE
Original site: K6Z4R5_9ALTE 
ID   K6Z4R5_9ALTE            Unreviewed;       354 AA.
AC   K6Z4R5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Phosphoserine phosphatase {ECO:0000256|ARBA:ARBA00015196};
DE            EC=3.1.3.3 {ECO:0000256|ARBA:ARBA00012640};
DE   AltName: Full=O-phosphoserine phosphohydrolase {ECO:0000256|ARBA:ARBA00031693};
GN   Name=serB {ECO:0000313|EMBL:GAC18405.1};
GN   ORFNames=GARC_1430 {ECO:0000313|EMBL:GAC18405.1};
OS   Paraglaciecola arctica BSs20135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC18405.1, ECO:0000313|Proteomes:UP000006327};
RN   [1] {ECO:0000313|EMBL:GAC18405.1, ECO:0000313|Proteomes:UP000006327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSs20135 {ECO:0000313|EMBL:GAC18405.1,
RC   ECO:0000313|Proteomes:UP000006327};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAC18405.1}.
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DR   EMBL; BAEO01000017; GAC18405.1; -; Genomic_DNA.
DR   RefSeq; WP_007618210.1; NZ_BAEO01000017.1.
DR   AlphaFoldDB; K6Z4R5; -.
DR   STRING; 493475.GARC_1430; -.
DR   eggNOG; COG0560; Bacteria.
DR   OrthoDB; 9792539at2; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000006327; Unassembled WGS sequence.
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; cd07500; HAD_PSP; 1.
DR   Gene3D; 3.30.70.2020; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004469; PSP.
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; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAC18405.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006327};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   ACT_SITE        150
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        152
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ   SEQUENCE   354 AA;  38117 MW;  FA243876B162D46A CRC64;
     MFEIKTTDKN LLSHLYLNDL VCQQGLSDFT LTDGLLCSVE ALKGAQQIPS ESSSFMDQSK
     LNKLVIFTEG LHLLQLTQVT QAFADYLEFA FFRVIKVDGV SGFAICAFVA LKTQEHLNSH
     LEDVANRFSV ELCLVDKTPS LTQPGLLLMD MDSTVIAVEC IDEIAELAGV GEEVSAVTGL
     AMQGKLDFAQ SLRTRVACLA NADESILHQV RDALPLMPGV ANLVEILKSY NWKVAIASGG
     FSYFADYLQD RLNLDAAVAN DLAIENGKLT GEVQGSIVDA NVKAQTLKTL AEQWSILPSQ
     TIAMGDGAND LVMMNAAALG VALHAKPIVR QQADIAIRRG GLDTLLWVLA AGAA
//
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