ID   A0A013S3A9_9GAMM        Unreviewed;       386 AA.
AC   A0A013S3A9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   02-OCT-2024, entry version 28.
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:EXS28834.1};
GN   ORFNames=J690_1670 {ECO:0000313|EMBL:EXS28834.1};
OS   Acinetobacter sp. 742879.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=1310791 {ECO:0000313|EMBL:EXS28834.1, ECO:0000313|Proteomes:UP000020888};
RN   [1] {ECO:0000313|EMBL:EXS28834.1, ECO:0000313|Proteomes:UP000020888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=742879 {ECO:0000313|EMBL:EXS28834.1,
RC   ECO:0000313|Proteomes:UP000020888};
RA   Harris A.D., Johnson K.J., Nadendla S., Daugherty S.C., Parankush S.,
RA   Sadzewicz L., Tallon L., Sengamalay N., Hazen T.H., Rasko D.A.;
RT   "Comparative genomics and transcriptomics to identify genetic mechanisms
RT   underlying the emergence of carbapenem resistant Acinetobacter baumannii
RT   (CRAb).";
RL   Submitted (MAR-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:EXS28834.1}.
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DR   EMBL; JFYC01000005; EXS28834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A013S3A9; -.
DR   PATRIC; fig|1310791.3.peg.1639; -.
DR   UniPathway; UPA00135; UER00198.
DR   Proteomes; UP000020888; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR050582; HAD-like_SerB.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004469; PSP.
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; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01136; C1.6:_Phosphoserine_Phosphatas; 1.
DR   SFLD; SFLDF00029; phosphoserine_phosphatase; 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:ARBA00022605};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EXS28834.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          247..279
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   ACT_SITE        177
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
FT   ACT_SITE        179
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604469-1"
SQ   SEQUENCE   386 AA;  41617 MW;  2513BEEA930FB782 CRC64;
     MQVLSVHSLQ ILDVGQAVIH NQLTLGIVVA SDNETATALA MKEILILAHD IGLTVRFKPI
     TGAEYDQWVS EGGRTRYIVT ALAPELTAAH LQAVTKIVSS QGFNIETVTR LSGRVDFEGD
     NKFPRRACVQ FGLSSGPTLD AQAMRAACLL LSSELNIDVA VQEDNAYRRN RRLVCFDMDS
     TLIEQEVIDE LAIEAGVGAQ VAEITERAMQ GELDFQQSFR ARVALLKGLD AAVLPKIAER
     LTITEGAERL ISTLKALGYK TAILSGGFQY FAEYLQGKLG IDEVHANILD VQDGFVTGEV
     KGAIVDGARK AELLRELANK MGISLEQAMA VGDGANDLPM LAIAGLGVAY RAKPLVRQNA
     NQAISSVGLD GVLYLLGMHD KDLNRA
//