ID   AGP_PRORE               Reviewed;         417 AA.
AC   Q52309;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Glucose-1-phosphatase;
DE            Short=G1Pase;
DE            EC=3.1.3.10;
DE   Flags: Precursor;
GN   Name=agp;
OS   Providencia rettgeri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PV7;
RA   Riccio M.L., Chiesurin A., Lombardi G., Satta G.;
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
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; X68201; CAA48288.1; -; Genomic_DNA.
DR   PIR; S25627; S25627.
DR   AlphaFoldDB; Q52309; -.
DR   SMR; Q52309; -.
DR   STRING; 1141663.OOC_08548; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008877; F:glucose-1-phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; -; 2.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; SSF53254; 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; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..417
FT                   /note="Glucose-1-phosphatase"
FT                   /id="PRO_0000023950"
FT   ACT_SITE        42
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        315
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  46941 MW;  8CC4CA4F55DBFB90 CRC64;
     MKYKVLTLCL SAALFAPIAP TMASTDNQAD MVLDQVLVLS RHNLRTPIVN TGILTEVTDK
     KWPDWDAKSG YLTTQGGALE VYMGHYFREW IDQNKLLADE LCPTSNEDIY LYTNSLQRTI
     ATAQFFAAGA FPGCKVNIHH QPEIGKMDPV FNPIITNGSP EFKQKALAAM DDYLKGLSLK
     AGYEELDTVL NIKDSQKCKT DKLCNLDSQK NSFIIEADKE PGVSGPLKIA NSAVDAIDLQ
     YYEGFPADQV AWGLVDTPEK WKKLNTLKNA YQETLFTPKI IAKNVAHPIL NYIDKGFVSV
     DKGETAKFIF LVGHDSNIAS LMSAMDFKPY QLAQQYEHTP IGGKLVFQRW TDKQTKKDFM
     KVEYVYQTAD QLRDNAYLSL ETPPKHVTLE LKDCPVDKNG YCSWEDFQKV MAKALEQ