ID   AGP_SALTY               Reviewed;         413 AA.
AC   O33921;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 2.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Glucose-1-phosphatase;
DE            Short=G1Pase;
DE            EC=3.1.3.10;
DE   Flags: Precursor;
GN   Name=agp; OrderedLocusNames=STM1117;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-249.
RC   STRAIN=TN1379;
RX   PubMed=9260936; DOI=10.1128/jb.179.16.4977-4984.1997;
RA   Gupta S.D., Wu H.C., Rick P.D.;
RT   "A Salmonella typhimurium genetic locus which confers copper tolerance on
RT   copper-sensitive mutants of Escherichia coli.";
RL   J. Bacteriol. 179:4977-4984(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate;
CC         Xref=Rhea:RHEA:19933, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=3.1.3.10;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase 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; AE006468; AAL20049.1; -; Genomic_DNA.
DR   EMBL; U75949; AAC45604.1; -; Genomic_DNA.
DR   RefSeq; NP_460090.1; NC_003197.2.
DR   RefSeq; WP_000749201.1; NC_003197.2.
DR   AlphaFoldDB; O33921; -.
DR   SMR; O33921; -.
DR   STRING; 99287.STM1117; -.
DR   PaxDb; 99287-STM1117; -.
DR   GeneID; 1252635; -.
DR   KEGG; stm:STM1117; -.
DR   PATRIC; fig|99287.12.peg.1182; -.
DR   HOGENOM; CLU_030561_2_1_6; -.
DR   OMA; IKTDQQW; -.
DR   PhylomeDB; O33921; -.
DR   BioCyc; SENT99287:STM1117-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0008877; F:glucose-1-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050308; F:sugar-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 2.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR11567:SF135; GLUCOSE-1-PHOSPHATASE; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..413
FT                   /note="Glucose-1-phosphatase"
FT                   /id="PRO_0000023949"
FT   ACT_SITE        40
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        312
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        57
FT                   /note="T -> P (in Ref. 2; AAC45604)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60..63
FT                   /note="AWPA -> TCPP (in Ref. 2; AAC45604)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="K -> T (in Ref. 2; AAC45604)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   413 AA;  45559 MW;  E057667CF8A7244C CRC64;
     MKKSLLAVAV AGAVLLSSAV QAQTTPEGYQ LQQVLMMSRH NLRAPLANNG SVLAQSTPNA
     WPAWDVPGGQ LTTKGGVLEV YMGHYTREWL VAQGLIPSGE CPAPDTVYAY ANSLQRTVAT
     AQFFITGAFP GCDIPVHHQE KMGTMDPTFN PVITDDSAAF RQQAVQAMEK ARSQLHLDES
     YKLLEQITHY QDSPSCKEKH QCSLIDAKDT FSANYQQEPG VQGPLKVGNS LVDAFTLQYY
     EGFPMDQVAW GGIHTDRQWK VLSKLKNGYQ DSLFTSPTVA RNVAAPLVKY IDKVLVADRV
     SAPKVTVLVG HDSNIASLLT ALDFKPYQLH DQYERTPIGG QLVFQRWHDG NANRDLMKIE
     YVYQSARQLR NAEALTLKSP AQRVTLELKG CPVDANGFCP LDKFDNVMNT AAK
//