Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P19926

- AGP_ECOLI

UniProt

P19926 - AGP_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glucose-1-phosphatase

Gene

agp

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

pH dependencei

Optimum pH is about 4.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391Substrate
Active sitei40 – 401Nucleophile
Binding sitei43 – 431Substrate
Binding sitei116 – 1161Substrate
Binding sitei218 – 2181Substrate
Active sitei312 – 3121Proton donor

GO - Molecular functioni

  1. 3-phytase activity Source: EcoCyc
  2. acid phosphatase activity Source: InterPro
  3. glucose-1-phosphatase activity Source: EcoCyc

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. glucose metabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-1-phosphatase (EC:3.1.3.10)
Short name:
G1Pase
Gene namesi
Name:agp
Ordered Locus Names:b1002, JW0987
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10033. agp.

Subcellular locationi

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22222 PublicationsAdd
BLAST
Chaini23 – 413391Glucose-1-phosphatasePRO_0000023948Add
BLAST

Proteomic databases

PaxDbiP19926.
PRIDEiP19926.

Expressioni

Gene expression databases

GenevestigatoriP19926.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-2905N.
IntActiP19926. 3 interactions.
STRINGi511145.b1002.

Structurei

Secondary structure

1
413
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 3810Combined sources
Helixi47 – 493Combined sources
Helixi50 – 556Combined sources
Helixi73 – 9220Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi106 – 1116Combined sources
Helixi115 – 12814Combined sources
Turni147 – 1493Combined sources
Helixi159 – 17416Combined sources
Helixi178 – 18811Combined sources
Helixi190 – 1923Combined sources
Turni194 – 1996Combined sources
Turni204 – 2063Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi220 – 2234Combined sources
Helixi224 – 24017Combined sources
Turni245 – 2473Combined sources
Helixi248 – 2514Combined sources
Helixi258 – 27417Combined sources
Helixi277 – 2837Combined sources
Helixi285 – 29410Combined sources
Turni295 – 3017Combined sources
Beta strandi304 – 3096Combined sources
Helixi312 – 32110Combined sources
Beta strandi333 – 3364Combined sources
Beta strandi341 – 3499Combined sources
Turni350 – 3534Combined sources
Beta strandi354 – 36310Combined sources
Helixi366 – 3716Combined sources
Beta strandi377 – 3793Combined sources
Beta strandi382 – 3854Combined sources
Helixi401 – 41111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NT4X-ray2.40A/B23-413[»]
ProteinModelPortaliP19926.
SMRiP19926. Positions 23-413.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19926.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni311 – 3133Substrate binding

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG28269.
HOGENOMiHOG000118851.
InParanoidiP19926.
KOiK01085.
OMAiFQRWHDK.
OrthoDBiEOG64N9T2.

Family and domain databases

Gene3Di3.40.50.1240. 3 hits.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19926-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKTLIAAAV AGIVLLASNA QAQTVPEGYQ LQQVLMMSRH NLRAPLANNG
60 70 80 90 100
SVLEQSTPNK WPEWDVPGGQ LTTKGGVLEV YMGHYMREWL AEQGMVKSGE
110 120 130 140 150
CPPPYTVYAY ANSLQRTVAT AQFFITGAFP GCDIPVHHQE KMGTMDPTFN
160 170 180 190 200
PVITDDSAAF SEQAVAAMEK ELSKLQLTDS YQLLEKIVNY KDSPACKEKQ
210 220 230 240 250
QCSLVDGKNT FSAKYQQEPG VSGPLKVGNS LVDAFTLQYY EGFPMDQVAW
260 270 280 290 300
GEIKSDQQWK VLSKLKNGYQ DSLFTSPEVA RNVAKPLVSY IDKALVTDRT
310 320 330 340 350
SAPKITVLVG HDSNIASLLT ALDFKPYQLH DQNERTPIGG KIVFQRWHDS
360 370 380 390 400
KANRDLMKIE YVYQSAEQLR NADALTLQAP AQRVTLELSG CPIDADGFCP
410
MDKFDSVLNE AVK
Length:413
Mass (Da):45,683
Last modified:February 1, 1991 - v1
Checksum:iADADAD3639D0D6AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33807 Genomic DNA. Translation: AAA23426.1.
U00096 Genomic DNA. Translation: AAC74087.1.
AP009048 Genomic DNA. Translation: BAA35769.1.
PIRiJV0087.
RefSeqiNP_415522.1. NC_000913.3.
YP_489275.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74087; AAC74087; b1002.
BAA35769; BAA35769; BAA35769.
GeneIDi12930557.
945773.
KEGGiecj:Y75_p0975.
eco:b1002.
PATRICi32117229. VBIEscCol129921_1038.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33807 Genomic DNA. Translation: AAA23426.1 .
U00096 Genomic DNA. Translation: AAC74087.1 .
AP009048 Genomic DNA. Translation: BAA35769.1 .
PIRi JV0087.
RefSeqi NP_415522.1. NC_000913.3.
YP_489275.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NT4 X-ray 2.40 A/B 23-413 [» ]
ProteinModelPortali P19926.
SMRi P19926. Positions 23-413.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-2905N.
IntActi P19926. 3 interactions.
STRINGi 511145.b1002.

Proteomic databases

PaxDbi P19926.
PRIDEi P19926.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74087 ; AAC74087 ; b1002 .
BAA35769 ; BAA35769 ; BAA35769 .
GeneIDi 12930557.
945773.
KEGGi ecj:Y75_p0975.
eco:b1002.
PATRICi 32117229. VBIEscCol129921_1038.

Organism-specific databases

EchoBASEi EB0032.
EcoGenei EG10033. agp.

Phylogenomic databases

eggNOGi NOG28269.
HOGENOMi HOG000118851.
InParanoidi P19926.
KOi K01085.
OMAi FQRWHDK.
OrthoDBi EOG64N9T2.

Enzyme and pathway databases

BioCyci EcoCyc:GLUCOSE-1-PHOSPHAT-MONOMER.
ECOL316407:JW0987-MONOMER.
MetaCyc:GLUCOSE-1-PHOSPHAT-MONOMER.

Miscellaneous databases

EvolutionaryTracei P19926.
PROi P19926.

Gene expression databases

Genevestigatori P19926.

Family and domain databases

Gene3Di 3.40.50.1240. 3 hits.
InterProi IPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view ]
Pfami PF00328. His_Phos_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

Entry informationi

Entry nameiAGP_ECOLI
AccessioniPrimary (citable) accession number: P19926
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 26, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3