Y125_MYCGE
ID Y125_MYCGE Reviewed; 285 AA.
AC P47371;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putative phosphatase MG125;
DE EC=3.1.3.-;
GN OrderedLocusNames=MG125;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
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; L43967; AAC71343.1; -; Genomic_DNA.
DR PIR; H64213; H64213.
DR RefSeq; WP_010869344.1; NC_000908.2.
DR AlphaFoldDB; P47371; -.
DR SMR; P47371; -.
DR STRING; 243273.MG_125; -.
DR PRIDE; P47371; -.
DR EnsemblBacteria; AAC71343; AAC71343; MG_125.
DR KEGG; mge:MG_125; -.
DR eggNOG; COG0561; Bacteria.
DR HOGENOM; CLU_044146_3_1_14; -.
DR OMA; IANIYPT; -.
DR OrthoDB; 1374424at2; -.
DR BioCyc; MGEN243273:G1GJ2-138-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR000150; Cof.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00099; Cof-subfamily; 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..285
FT /note="Putative phosphatase MG125"
FT /id="PRO_0000054435"
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 285 AA; 32877 MW; 05339705CA2C49D2 CRC64;
MIDLLGLDLD GTLLSKTKKI NNPSKLALTN LIAKKPSLKV MILTGRSVFS TLKHVEKLNS
LFKKPIVDYF CCYGGAKLYQ IEANKPQERY KFCLENSVVE TTFSIIKKHR GLCLAYLDSY
VSPYLCLAGN KLLGWFTKYF WYRKRCVFFN QNHLKQGILK ISVYFLSAKR CKKVYEILKN
TFQEKVNVLS FSNNLIEITH HDANKGYAIE YMAKREQLSL NRIAVIGDSW NDYAMFKKAK
YSFAMSKSPS QLKLIATNTS NKTNRYRFST LLNLISETII NQKAD
