ID Y264_MYCPN Reviewed; 281 AA.
AC P75511;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Putative phosphatase MPN_264;
DE EC=3.1.3.-;
GN OrderedLocusNames=MPN_264; ORFNames=A65_orf281, MP569;
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}.
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DR EMBL; U00089; AAB96217.1; -; Genomic_DNA.
DR PIR; S73895; S73895.
DR RefSeq; NP_109952.1; NC_000912.1.
DR RefSeq; WP_010874621.1; NZ_OU342337.1.
DR AlphaFoldDB; P75511; -.
DR SMR; P75511; -.
DR IntAct; P75511; 3.
DR STRING; 272634.MPN_264; -.
DR EnsemblBacteria; AAB96217; AAB96217; MPN_264.
DR KEGG; mpn:MPN_264; -.
DR PATRIC; fig|272634.6.peg.283; -.
DR HOGENOM; CLU_044146_3_1_14; -.
DR OrthoDB; 9810101at2; -.
DR BioCyc; MPNE272634:G1GJ3-415-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:SF58; MANNOSYL-3-PHOSPHOGLYCERATE PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR10000; PHOSPHOSERINE PHOSPHATASE; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS01228; COF_1; 1.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..281
FT /note="Putative phosphatase MPN_264"
FT /id="PRO_0000054436"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 44..45
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
SQ SEQUENCE 281 AA; 32614 MW; BF44564E7C7FBF11 CRC64;
MIDLLGLDLD GTLLSRTRQI NDPTKQALAN LIQKKPSLKV MILTGRSLFS TLKYVQELNE
LCKKPLVEYF CCYGGAKLYQ LNNNQPQEQY KFLIDSRQVK TVFEIVEQHK GLFLAYLDKP
KAPYIILGAN QFYAWLIKQF WYKQRCEYFK NDHLTDGILK INVYFACPLR LKKVYQIIKR
QFQDTLNVVN FSKHLIEITH KDGNKGYAIE AIAKKQGLSL KRMAVIGDSL NDRSMFEKVQ
YSFAMSKSPD ELKLLATEIG TKTNRFRFSS LVDLITEKII N
//
