Y1798_PECCP
ID Y1798_PECCP Reviewed; 245 AA.
AC C6DFD0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Probable phosphatase PC1_1798 {ECO:0000255|HAMAP-Rule:MF_01561};
DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01561};
GN OrderedLocusNames=PC1_1798;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT12839.1; -; Genomic_DNA.
DR RefSeq; WP_015840045.1; NC_012917.1.
DR AlphaFoldDB; C6DFD0; -.
DR SMR; C6DFD0; -.
DR STRING; 561230.PC1_1798; -.
DR EnsemblBacteria; ACT12839; ACT12839; PC1_1798.
DR KEGG; pct:PC1_1798; -.
DR eggNOG; COG1387; Bacteria.
DR HOGENOM; CLU_061999_0_1_6; -.
DR OMA; SEPNCRA; -.
DR OrthoDB; 1615112at2; -.
DR Proteomes; UP000002736; 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 PC1_1798"
FT /id="PRO_1000215509"
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; 27111 MW; ACE844183437D541 CRC64;
MYPVDLHMHT VASTHAYSTL HDYIAEAQQK NIRLFAITDH GPDMADAPHY WHFMNMRVWP
RLVDGVGILR GIEANIKNIE GDIDCTGPML DQVDVIIAGF HEPVFPPQDK DTHTAAMIAT
MARGDAHIIS HPGNPKYPVD IRAIAEAAAK YNVALELNNS SFMHSRKGSE PNCRAIAEAV
RDAGGLLSLG SDSHIAFSLG DFTHCERILQ EVNFPQDQIL NVSPRRVLDF LEQRGMPAIA
ELANL