ID A0A013S3A9_9GAMM Unreviewed; 386 AA. AC A0A013S3A9; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 13-SEP-2023, entry version 24. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JFYC01000005; EXS28834.1; -; Genomic_DNA. DR AlphaFoldDB; A0A013S3A9; -. DR EnsemblBacteria; EXS28834; EXS28834; J690_1670. DR PATRIC; fig|1310791.3.peg.1639; -. DR UniPathway; UPA00135; UER00198. DR Proteomes; UP000020888; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1. 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; PF12710; HAD; 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 //