ID A0A347UCA7_9RHOB Unreviewed; 290 AA.
AC A0A347UCA7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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:AXX96485.1};
GN ORFNames=BAR1_00170 {ECO:0000313|EMBL:AXX96485.1};
OS Profundibacter amoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Profundibacter.
OX NCBI_TaxID=2171755 {ECO:0000313|EMBL:AXX96485.1, ECO:0000313|Proteomes:UP000261704};
RN [1] {ECO:0000313|EMBL:AXX96485.1, ECO:0000313|Proteomes:UP000261704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAR1 {ECO:0000313|EMBL:AXX96485.1,
RC ECO:0000313|Proteomes:UP000261704};
RA Le Moine Bauer S., Sjoeberg A.G., L'Haridon S., Stokke R., Roalkvam I.,
RA Steen I.H., Dahle H.;
RT "Profundibacter amoris BAR1 gen. nov., sp. nov., a new member of the
RT Roseobacter clade isolated at Lokis Castle Vent Field on the Arctic Mid-
RT Oceanic Ridge.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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; CP032125; AXX96485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A347UCA7; -.
DR KEGG; pamo:BAR1_00170; -.
DR OrthoDB; 9792539at2; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000261704; 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; cd07500; HAD_PSP; 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; PF12710; HAD; 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:AXX96485.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000261704};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 84
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 290 AA; 30361 MW; 2B986E74F926C138 CRC64;
MFTVTLLSSP SNPVVGPAVV DSLRNAWGGG DALWLAPDVA AEFQVETVPA NRWAVWADLQ
GMGVDLVVQS CEGRRKKMLL ADMDSTMIQQ ECIDELAAEA GIGDHVAQIT ARAMNGELNF
EDALRERVGL LKGLDSAVIE TVLANRITLM PGGKALLATM KANGAYAALV SGGFTAFTGM
VAETLGFDEH RANTLIIADG KLTGEVGQPI LGRDAKVVAL NEITARLGLS TDQVMAVGDG
ANDLGMLGLA GAGVALHAKP SVAAECDIRI NHGDLTALLY IQGYSVEEFV
//
