Glucose-1-phosphatase precursor - Escherichia coli (strain K12)

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P19926 (AGP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glucose-1-phosphatase
Short name=G1Pase
EC=3.1.3.10

Gene names

Name:	agp
Ordered Locus Names:	b1002, JW0987

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	413 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from mutant phenotype. Source: EcoCyc
Cellular component	periplasmic space Inferred from physical interaction. Source: EcoCyc
Molecular function	3-phytase activity Inferred from direct assay. Source: EcoCyc acid phosphatase activity Inferred from electronic annotation. Source: InterPro glucose-1-phosphatase activity Inferred from direct assay. Source: EcoCyc protein homodimerization activity Inferred from physical interaction. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Ref.1 Ref.5

Chain

23 – 413

391

Glucose-1-phosphatase

PRO_0000023948

Sites

Active site

Nucleophile

Active site

312

Proton donor

Secondary structure

413

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P19926 [UniParc].

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

FASTA

413

45,683

        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' referencesShow '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: 2153660] [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. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 9298646] [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: 12782623] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-413.
+	Additional computationally mapped references.

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.

PIR

JV0087.

RefSeq

NP_415522.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NT4	X-ray	2.40	A/B	23-413	[»]

ProteinModelPortal

P19926.

SMR

P19926. Positions 23-413.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2905N.

IntAct

P19926. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003441; EBESCP00000003441; EBESCG00000002822.
EBESCT00000017532; EBESCP00000016823; EBESCG00000016588.

GeneID

945773.

GenomeReviews

Gene locus JW0987 in contig AP009048_GR.
Gene locus b1002 in contig U00096_GR.

KEGG

ecj:JW0987.
eco:b1002.

PATRIC

32117229. VBIEscCol129921_1038.

Organism-specific databases

EchoBASE

EB0032.

EcoGene

EG10033. agp.

Phylogenomic databases

eggNOG

NOG28269.

GeneTree

EBGT00050000009987.

HOGENOM

HBG751992.

OMA

LLVGHDS.

ProtClustDB

PRK10173.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUCOSE-1-PHOSPHAT-MONOMER.
MetaCyc:GLUCOSE-1-PHOSPHAT-MONOMER.

Gene expression databases

Genevestigator

P19926.

Family and domain databases

InterPro

IPR000560. His_Pase_superF_clade-2.
[Graphical view]

K01085.

Pfam

PF00328. His_Phos_2. 1 hit.
[Graphical view]

PROSITE

PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AGP_ECOLI

Accession

Primary (citable) accession number: P19926

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	January 25, 2012
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents