ID Y427_MYCPN Reviewed; 290 AA. AC P75360; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Putative phosphatase MPN_427; DE EC=3.1.3.-; GN OrderedLocusNames=MPN_427; ORFNames=A05_orf290, MP414; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasmoides pneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family. CC {ECO:0000305}. 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; U00089; AAB96062.1; -; Genomic_DNA. DR PIR; S73740; S73740. DR RefSeq; NP_110115.1; NC_000912.1. DR RefSeq; WP_010874783.1; NZ_OU342337.1. DR AlphaFoldDB; P75360; -. DR SMR; P75360; -. DR STRING; 272634.MPN_427; -. DR EnsemblBacteria; AAB96062; AAB96062; MPN_427. DR KEGG; mpn:MPN_427; -. DR PATRIC; fig|272634.6.peg.462; -. DR HOGENOM; CLU_044146_0_1_14; -. DR OrthoDB; 9810101at2; -. DR BioCyc; MPNE272634:G1GJ3-691-MONOMER; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016791; F:phosphatase activity; IEA:UniProt. DR Gene3D; 3.30.1240.10; -; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR000150; Cof. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR006379; HAD-SF_hydro_IIB. DR InterPro; IPR023214; HAD_sf. DR NCBIfam; TIGR00099; Cof-subfamily; 1. DR NCBIfam; TIGR01484; HAD-SF-IIB; 1. DR PANTHER; PTHR10000:SF8; PHOSPHOGLYCOLATE PHOSPHATASE 1; 1. DR PANTHER; PTHR10000; PHOSPHOSERINE PHOSPHATASE; 1. DR Pfam; PF08282; Hydrolase_3; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 3: Inferred from homology; KW Hydrolase; Magnesium; Metal-binding; Reference proteome. FT CHAIN 1..290 FT /note="Putative phosphatase MPN_427" FT /id="PRO_0000054441" FT ACT_SITE 16 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT BINDING 16 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 17 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250" FT BINDING 18 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 53..54 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250" FT BINDING 216 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250" FT BINDING 239 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 240 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 242 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250" SQ SEQUENCE 290 AA; 33216 MW; FCA0416EDEEE48CA CRC64; MTKTSKASGL SWFFCDLDGT LLRYQNNQHL IEPTTKRAVA QLVESGANFV VATGRKPSDV RNIYKELGIE QASPYLIANN GAVVWDLKRN SYLNKQTLSL SDFDLIDHIN QTLNQLNHEY GCILYGLNDQ VYFYHIHAPD SQAFKQYFAF YEGEFVQNQY LEIDGLKTEY NLVKAIWFFK EVHQQKAVIA QHFTNQERLV ITSAHSFELV PLNVSKGHAI NLIKQQVKIT DNQIMVLGDS YNDLPMFQHG VVKVTNHLAP DNLKQLATRV YELPASLFVG QALNDYFKFD //