Y427_MYCPN
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 03-AUG-2022, entry version 103.
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) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
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; AAB96062.1; -; Genomic_DNA.
DR PIR; S73740; S73740.
DR RefSeq; NP_110115.1; NC_000912.1.
DR RefSeq; WP_010874783.1; NC_000912.1.
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 OMA; ETTERFW; -.
DR BioCyc; MPNE272634:G1GJ3-691-MON; -.
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; 3.40.50.1000; -; 1.
DR InterPro; IPR000150; Cof.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00099; Cof-subfamily; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 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
