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Protein

Glucose-1-phosphatase

Gene

agp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei39Substrate1
Active sitei40Nucleophile1
Binding sitei43Substrate1
Binding sitei116Substrate1
Binding sitei218Substrate1
Active sitei312Proton donor1

GO - Molecular functioni

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

GO - Biological processi

  • glucose catabolic 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10033. agp.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 222 PublicationsAdd BLAST22
ChainiPRO_000002394823 – 413Glucose-1-phosphataseAdd BLAST391

Proteomic databases

EPDiP19926.
PaxDbiP19926.
PRIDEiP19926.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4259551. 10 interactors.
DIPiDIP-2905N.
IntActiP19926. 3 interactors.
STRINGi511145.b1002.

Structurei

Secondary structure

1413
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 38Combined sources10
Helixi47 – 49Combined sources3
Helixi50 – 55Combined sources6
Helixi73 – 92Combined sources20
Beta strandi98 – 100Combined sources3
Beta strandi106 – 111Combined sources6
Helixi115 – 128Combined sources14
Turni147 – 149Combined sources3
Helixi159 – 174Combined sources16
Helixi178 – 188Combined sources11
Helixi190 – 192Combined sources3
Turni194 – 199Combined sources6
Turni204 – 206Combined sources3
Beta strandi210 – 212Combined sources3
Beta strandi220 – 223Combined sources4
Helixi224 – 240Combined sources17
Turni245 – 247Combined sources3
Helixi248 – 251Combined sources4
Helixi258 – 274Combined sources17
Helixi277 – 283Combined sources7
Helixi285 – 294Combined sources10
Turni295 – 301Combined sources7
Beta strandi304 – 309Combined sources6
Helixi312 – 321Combined sources10
Beta strandi333 – 336Combined sources4
Beta strandi341 – 349Combined sources9
Turni350 – 353Combined sources4
Beta strandi354 – 363Combined sources10
Helixi366 – 371Combined sources6
Beta strandi377 – 379Combined sources3
Beta strandi382 – 385Combined sources4
Helixi401 – 411Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP19926.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni311 – 313Substrate binding3

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105D6F. Bacteria.
ENOG410XRK8. LUCA.
HOGENOMiHOG000118851.
InParanoidiP19926.
KOiK01085.
OMAiAWGEIKT.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 3 hits.
InterProiIPR033379. Acid_Pase_AS.
IPR000560. His_Pase_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.
WP_001044279.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74087; AAC74087; b1002.
BAA35769; BAA35769; BAA35769.
GeneIDi945773.
KEGGiecj:JW0987.
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.
PIRiJV0087.
RefSeqiNP_415522.1. NC_000913.3.
WP_001044279.1. NZ_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4259551. 10 interactors.
DIPiDIP-2905N.
IntActiP19926. 3 interactors.
STRINGi511145.b1002.

Proteomic databases

EPDiP19926.
PaxDbiP19926.
PRIDEiP19926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74087; AAC74087; b1002.
BAA35769; BAA35769; BAA35769.
GeneIDi945773.
KEGGiecj:JW0987.
eco:b1002.
PATRICi32117229. VBIEscCol129921_1038.

Organism-specific databases

EchoBASEiEB0032.
EcoGeneiEG10033. agp.

Phylogenomic databases

eggNOGiENOG4105D6F. Bacteria.
ENOG410XRK8. LUCA.
HOGENOMiHOG000118851.
InParanoidiP19926.
KOiK01085.
OMAiAWGEIKT.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP19926.
PROiP19926.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 3 hits.
InterProiIPR033379. Acid_Pase_AS.
IPR000560. His_Pase_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]
ProtoNetiSearch...

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 2, 2016
This is version 136 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.