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P19926 (AGP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-1-phosphatase

Short name=G1Pase
EC=3.1.3.10
Gene names
Name:agp
Ordered Locus Names:b1002, JW0987
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Absolutely required for the growth of E.coli in a high-phosphate medium containing G-1-P as the sole carbon source.

Catalytic activity

Alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate.

Enzyme regulation

Independent from inorganic phosphate availability, and apparently submitted to catabolite repression, it is positively controlled by cAMP and the cAMP receptor protein.

Subunit structure

Homodimer.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Biophysicochemical properties

pH dependence:

Optimum pH is about 4.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.1 Ref.5
Chain23 – 413391Glucose-1-phosphatase
PRO_0000023948

Regions

Region311 – 3133Substrate binding

Sites

Active site401Nucleophile
Active site3121Proton donor
Binding site391Substrate
Binding site431Substrate
Binding site1161Substrate
Binding site2181Substrate

Secondary structure

........................................................... 413
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19926 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: ADADAD3639D0D6AB

FASTA41345,683
        10         20         30         40         50         60 
MNKTLIAAAV AGIVLLASNA QAQTVPEGYQ LQQVLMMSRH NLRAPLANNG SVLEQSTPNK 

        70         80         90        100        110        120 
WPEWDVPGGQ LTTKGGVLEV YMGHYMREWL AEQGMVKSGE CPPPYTVYAY ANSLQRTVAT 

       130        140        150        160        170        180 
AQFFITGAFP GCDIPVHHQE KMGTMDPTFN PVITDDSAAF SEQAVAAMEK ELSKLQLTDS 

       190        200        210        220        230        240 
YQLLEKIVNY KDSPACKEKQ QCSLVDGKNT FSAKYQQEPG VSGPLKVGNS LVDAFTLQYY 

       250        260        270        280        290        300 
EGFPMDQVAW GEIKSDQQWK VLSKLKNGYQ DSLFTSPEVA RNVAKPLVSY IDKALVTDRT 

       310        320        330        340        350        360 
SAPKITVLVG HDSNIASLLT ALDFKPYQLH DQNERTPIGG KIVFQRWHDS KANRDLMKIE 

       370        380        390        400        410 
YVYQSAEQLR NADALTLQAP AQRVTLELSG CPIDADGFCP MDKFDSVLNE AVK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and transcriptional analysis of the Escherichia coli agp gene encoding periplasmic acid glucose-1-phosphatase."
Pradel E., Marck C., Boquet P.L.
J. Bacteriol. 172:802-807(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-31.
Strain: K12.
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-34.
Strain: K12 / EMG2.
[6]"Functional insights revealed by the crystal structures of Escherichia coli glucose-1-phosphatase."
Lee D.C., Cottrill M.A., Forsberg C.W., Jia Z.
J. Biol. Chem. 278:31412-31418(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-413 IN COMPLEX WITH GLUCOSE 1-PHOSPHATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33807 Genomic DNA. Translation: AAA23426.1.
U00096 Genomic DNA. Translation: AAC74087.1.
AP009048 Genomic DNA. Translation: BAA35769.1.
PIRJV0087.
RefSeqNP_415522.1. NC_000913.3.
YP_489275.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NT4X-ray2.40A/B23-413[»]
ProteinModelPortalP19926.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-2905N.
IntActP19926. 3 interactions.
STRING511145.b1002.

Proteomic databases

PaxDbP19926.
PRIDEP19926.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74087; AAC74087; b1002.
BAA35769; BAA35769; BAA35769.
GeneID12930557.
945773.
KEGGecj:Y75_p0975.
eco:b1002.
PATRIC32117229. VBIEscCol129921_1038.

Organism-specific databases

EchoBASEEB0032.
EcoGeneEG10033. agp.

Phylogenomic databases

eggNOGNOG28269.
HOGENOMHOG000118851.
KOK01085.
OMAFQRWHDK.
OrthoDBEOG64N9T2.

Enzyme and pathway databases

BioCycEcoCyc:GLUCOSE-1-PHOSPHAT-MONOMER.
ECOL316407:JW0987-MONOMER.
MetaCyc:GLUCOSE-1-PHOSPHAT-MONOMER.

Gene expression databases

GenevestigatorP19926.

Family and domain databases

Gene3D3.40.50.1240. 3 hits.
InterProIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 1 hit.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19926.
PROP19926.

Entry information

Entry nameAGP_ECOLI
AccessionPrimary (citable) accession number: P19926
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 11, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene