ID A0A0Q7GMG0_9FLAO Unreviewed; 409 AA.
AC A0A0Q7GMG0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=ASC72_19770 {ECO:0000313|EMBL:KQX12073.1};
OS Flavobacterium sp. Root420.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736533 {ECO:0000313|EMBL:KQX12073.1, ECO:0000313|Proteomes:UP000051729};
RN [1] {ECO:0000313|EMBL:KQX12073.1, ECO:0000313|Proteomes:UP000051729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root420 {ECO:0000313|EMBL:KQX12073.1,
RC ECO:0000313|Proteomes:UP000051729};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQX12073.1}.
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DR EMBL; LMEF01000006; KQX12073.1; -; Genomic_DNA.
DR RefSeq; WP_056188153.1; NZ_LMEF01000006.1.
DR AlphaFoldDB; A0A0Q7GMG0; -.
DR STRING; 1736533.ASC72_19770; -.
DR OrthoDB; 9790031at2; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000051729; 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; cd04870; ACT_PSP_1; 1.
DR CDD; cd04871; ACT_PSP_2; 1.
DR CDD; cd07500; HAD_PSP; 1.
DR Gene3D; 3.30.70.260; -; 1.
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 InterPro; IPR001763; Rhodanese-like_dom.
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; PF12710; HAD; 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.
DR PROSITE; PS50206; RHODANESE_3; 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 Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 10..88
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 270..302
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT ACT_SITE 200
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ SEQUENCE 409 AA; 45232 MW; 1D744DAE8D1E938F CRC64;
MAIEDKEIIL LKVSGHDKIG VTAGLTAVLA TYDANILDIG QADIHDTLSL GILFEIEAGS
SSAPVLKDLL FKAYELEIKV KFIPISIEDY EVWVKSQSKQ RYIINILGEK LAASQLAAVT
KIMSDQNLNI DSIIRLTGRT SVVDLEEYPR SCIQLSVTGE IVNKILMTAS FMEISRTLNV
DISFQEDNIY RRNRRLVCFD MDSTLIQTEV IDELAELNGV GDQVRAITES AMNGEIDFNE
SFKQRMALLE GLSEEVLQKV AENLPITQGA HRLMKALKYY GYKTAILSGG FTYFGEYLQK
ELGIDYVHAN QLEIKDGKLT GKYIGDIVDG LKKAEHLKAI AEKEGIHINQ TIAVGDGAND
LPMLNLAGLG IAFHAKPKVK ESASTSISSL GLDGVLYLLG YHDRYIDMM
//
