AGP_ECOLI
ID AGP_ECOLI Reviewed; 413 AA.
AC P19926;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Glucose-1-phosphatase;
DE Short=G1Pase;
DE EC=3.1.3.10;
DE Flags: Precursor;
GN Name=agp; OrderedLocusNames=b1002, JW0987;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-31.
RC STRAIN=K12;
RX PubMed=2153660; DOI=10.1128/jb.172.2.802-807.1990;
RA Pradel E., Marck C., Boquet P.L.;
RT "Nucleotide sequence and transcriptional analysis of the Escherichia coli
RT agp gene encoding periplasmic acid glucose-1-phosphatase.";
RL J. Bacteriol. 172:802-807(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 23-34.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-413 IN COMPLEX WITH GLUCOSE
RP 1-PHOSPHATE.
RX PubMed=12782623; DOI=10.1074/jbc.m213154200;
RA Lee D.C., Cottrill M.A., Forsberg C.W., Jia Z.;
RT "Functional insights revealed by the crystal structures of Escherichia coli
RT glucose-1-phosphatase.";
RL J. Biol. Chem. 278:31412-31418(2003).
CC -!- FUNCTION: Absolutely required for the growth of E.coli in a high-
CC phosphate medium containing G-1-P as the sole carbon source.
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 -!- ACTIVITY REGULATION: Independent from inorganic phosphate availability,
CC and apparently submitted to catabolite repression, it is positively
CC controlled by cAMP and the cAMP receptor protein.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is about 4.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12782623}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; M33807; AAA23426.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74087.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35769.1; -; Genomic_DNA.
DR PIR; JV0087; JV0087.
DR RefSeq; NP_415522.1; NC_000913.3.
DR RefSeq; WP_001044279.1; NZ_SSZK01000002.1.
DR PDB; 1NT4; X-ray; 2.40 A; A/B=23-413.
DR PDB; 6RMR; X-ray; 2.50 A; A/B=23-413.
DR PDBsum; 1NT4; -.
DR PDBsum; 6RMR; -.
DR AlphaFoldDB; P19926; -.
DR SMR; P19926; -.
DR BioGRID; 4259551; 13.
DR DIP; DIP-2905N; -.
DR IntAct; P19926; 3.
DR STRING; 511145.b1002; -.
DR DrugBank; DB02843; alpha-D-glucose-1-phosphate.
DR jPOST; P19926; -.
DR PaxDb; P19926; -.
DR PRIDE; P19926; -.
DR EnsemblBacteria; AAC74087; AAC74087; b1002.
DR EnsemblBacteria; BAA35769; BAA35769; BAA35769.
DR GeneID; 945773; -.
DR KEGG; ecj:JW0987; -.
DR KEGG; eco:b1002; -.
DR PATRIC; fig|1411691.4.peg.1269; -.
DR EchoBASE; EB0032; -.
DR eggNOG; ENOG502Z7K9; Bacteria.
DR HOGENOM; CLU_030561_2_1_6; -.
DR InParanoid; P19926; -.
DR OMA; IKTDQQW; -.
DR PhylomeDB; P19926; -.
DR BioCyc; EcoCyc:GLUCOSE-1-PHOSPHAT-MON; -.
DR BioCyc; MetaCyc:GLUCOSE-1-PHOSPHAT-MON; -.
DR EvolutionaryTrace; P19926; -.
DR PRO; PR:P19926; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0016158; F:3-phytase activity; IDA:EcoCyc.
DR GO; GO:0008877; F:glucose-1-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0050308; F:sugar-phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006007; P:glucose catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:2153660,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 23..413
FT /note="Glucose-1-phosphatase"
FT /id="PRO_0000023948"
FT ACT_SITE 40
FT /note="Nucleophile"
FT ACT_SITE 312
FT /note="Proton donor"
FT BINDING 39
FT /ligand="substrate"
FT BINDING 43
FT /ligand="substrate"
FT BINDING 116
FT /ligand="substrate"
FT BINDING 218
FT /ligand="substrate"
FT BINDING 311..313
FT /ligand="substrate"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 73..92
FT /evidence="ECO:0007829|PDB:1NT4"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1NT4"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:1NT4"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1NT4"
FT TURN 194..199
FT /evidence="ECO:0007829|PDB:1NT4"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1NT4"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1NT4"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 224..240
FT /evidence="ECO:0007829|PDB:1NT4"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 258..274
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 277..283
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:1NT4"
FT TURN 295..301
FT /evidence="ECO:0007829|PDB:1NT4"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:1NT4"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:1NT4"
FT STRAND 341..349
FT /evidence="ECO:0007829|PDB:1NT4"
FT TURN 350..353
FT /evidence="ECO:0007829|PDB:1NT4"
FT STRAND 354..363
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:1NT4"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1NT4"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:1NT4"
FT HELIX 401..411
FT /evidence="ECO:0007829|PDB:1NT4"
SQ SEQUENCE 413 AA; 45683 MW; ADADAD3639D0D6AB CRC64;
MNKTLIAAAV AGIVLLASNA QAQTVPEGYQ LQQVLMMSRH NLRAPLANNG SVLEQSTPNK
WPEWDVPGGQ LTTKGGVLEV YMGHYMREWL AEQGMVKSGE CPPPYTVYAY ANSLQRTVAT
AQFFITGAFP GCDIPVHHQE KMGTMDPTFN PVITDDSAAF SEQAVAAMEK ELSKLQLTDS
YQLLEKIVNY KDSPACKEKQ QCSLVDGKNT FSAKYQQEPG VSGPLKVGNS LVDAFTLQYY
EGFPMDQVAW GEIKSDQQWK VLSKLKNGYQ DSLFTSPEVA RNVAKPLVSY IDKALVTDRT
SAPKITVLVG HDSNIASLLT ALDFKPYQLH DQNERTPIGG KIVFQRWHDS KANRDLMKIE
YVYQSAEQLR NADALTLQAP AQRVTLELSG CPIDADGFCP MDKFDSVLNE AVK
