ID A0A085ZQQ9_9FLAO Unreviewed; 409 AA.
AC A0A085ZQQ9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-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=IW19_15225 {ECO:0000313|EMBL:KFF06773.1};
OS Flavobacterium reichenbachii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=362418 {ECO:0000313|EMBL:KFF06773.1, ECO:0000313|Proteomes:UP000028715};
RN [1] {ECO:0000313|EMBL:KFF06773.1, ECO:0000313|Proteomes:UP000028715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25512 {ECO:0000313|EMBL:KFF06773.1,
RC ECO:0000313|Proteomes:UP000028715};
RA Stropko S.J., Pipes S.E., Newman J.D.;
RT "Genome of Flavobacterium reichenbachii LMG 25512.";
RL Submitted (JUL-2014) 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:KFF06773.1}.
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DR EMBL; JPRL01000001; KFF06773.1; -; Genomic_DNA.
DR RefSeq; WP_035685585.1; NZ_MUHF01000001.1.
DR AlphaFoldDB; A0A085ZQQ9; -.
DR STRING; 362418.IW19_15225; -.
DR eggNOG; COG0560; Bacteria.
DR eggNOG; COG3830; Bacteria.
DR OrthoDB; 9790031at2; -.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000028715; 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; 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; 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; 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 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; 45195 MW; 74DEFE037C158318 CRC64;
MAAEDKEIIL LKVSGHDKIG VTAGLTSVLA AYDAMILDIG QADIHDTLSL GILFEIKAGS
TSGPVLKDLL FKAYELEIKV KFIPISIDDY EKWVKSQSKQ RYIINILGEQ LAASQLAAVT
KIMSDQNLNI DSIIRLTGRT SIVEKEEYPR SCIQLSVTGE IVNKIVMTAS FMEISRTLDV
DISFQEDNIY RRNRRLVCFD MDSTLIQTEV IDELAELNGV GAQVRAITES AMNGEIDFNE
SFKQRMALLE GLSEEVLHNV AINLPITKGA RRLMKALKYY GYKTAILSGG FTYFGDYLQK
ELGIDYVHAN QLEIIDGKLT GKYLGEIVDG QKKAELLRAI AEKEGIHINQ TIAVGDGAND
LPMLNLAGLG IAFHAKPKVK ESASTSISSL GLDGVLYLLG YHDRYIDMM
//
