ID A0A4D6HAH5_9EURY Unreviewed; 210 AA.
AC A0A4D6HAH5;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 Name=serB {ECO:0000313|EMBL:QCC50993.1};
GN ORFNames=DV733_06925 {ECO:0000313|EMBL:QCC50993.1};
OS Halapricum salinum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halapricum.
OX NCBI_TaxID=1457250 {ECO:0000313|EMBL:QCC50993.1, ECO:0000313|Proteomes:UP000296706};
RN [1] {ECO:0000313|EMBL:QCC50993.1, ECO:0000313|Proteomes:UP000296706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA1105 {ECO:0000313|EMBL:QCC50993.1,
RC ECO:0000313|Proteomes:UP000296706};
RX PubMed=30975999; DOI=.1038/s41467-019-09390-9;
RA Xiong L., Liu S., Chen S., Xiao Y., Zhu B., Gao Y., Zhang Y., Chen B.,
RA Luo J., Deng Z., Chen X., Wang L., Chen S.;
RT "A new type of DNA phosphorothioation-based antiviral system in archaea.";
RL Nat. Commun. 10:1688-1688(2019).
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; CP031310; QCC50993.1; -; Genomic_DNA.
DR RefSeq; WP_049995454.1; NZ_CP031310.1.
DR AlphaFoldDB; A0A4D6HAH5; -.
DR STRING; 1457250.GCA_000755225_00097; -.
DR GeneID; 39847584; -.
DR KEGG; hsn:DV733_06925; -.
DR OrthoDB; 10041at2157; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000296706; 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 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; PF12710; HAD; 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:QCC50993.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000296706};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT ACT_SITE 6
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 8
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 210 AA; 22067 MW; A420C80DF965CF12 CRC64;
MLVAFDFDGT LSDSEMTVLL GEQCGVADEM AEITERAMND EIEYAESLRQ RCALLEGLDD
TRAETAFGEV LLRDGAADVI ADLNDAGVHT AILTGGFERG VEAALAKAGA SVDTIVANRL
PVENGALTGE VEGPLIEGTK DTALRNLASD LDLDLSETVA VGDGANDLPM LSVAGLSIGF
EPKPAVKDSC DIVVTSMPEL QIVLEEERVL
//
