YCDX_ECO27
ID YCDX_ECO27 Reviewed; 245 AA.
AC B7UP48;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Probable phosphatase YcdX {ECO:0000255|HAMAP-Rule:MF_01561};
DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01561};
GN Name=ycdX {ECO:0000255|HAMAP-Rule:MF_01561}; OrderedLocusNames=E2348C_1124;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01561};
CC Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01561};
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01561}.
CC -!- SIMILARITY: Belongs to the PHP family. {ECO:0000255|HAMAP-
CC Rule:MF_01561}.
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DR EMBL; FM180568; CAS08672.1; -; Genomic_DNA.
DR RefSeq; WP_000283657.1; NC_011601.1.
DR AlphaFoldDB; B7UP48; -.
DR SMR; B7UP48; -.
DR EnsemblBacteria; CAS08672; CAS08672; E2348C_1124.
DR KEGG; ecg:E2348C_1124; -.
DR HOGENOM; CLU_061999_0_1_6; -.
DR OMA; SEPNCRA; -.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01561; YcdX_phosphat; 1.
DR InterPro; IPR023710; Phosphatase_YcdX_put.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..245
FT /note="Probable phosphatase YcdX"
FT /id="PRO_1000185430"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
SQ SEQUENCE 245 AA; 26921 MW; CC6443B8DC961841 CRC64;
MYPVDLHMHT VASTHAYSTL SDYIAQAKQK GIKLFAITDH GPDMEDAPHH WHFINMRIWP
RVVDGVGILR GIEANIKNVD GEIDCSGKMF DSLDLIIAGF HEPVFAPHDK ATNTKAMIAT
IASGNVHIIS HPGNPRYPID FKAVSEAAVK HQVALEINNS SFLHSRKGSE DNCRAVAAAV
RDAGGWVALG SDSHTAFTMG EFEECLKILD AVDFPPERIL NVSPRRLLNF LESRGMAPIA
EFADL
