Reviewed, UniProtKB/Swiss-Prot P19926 (AGP_ECOLI)

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) [Complete proteome] [HAMAP]

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
Gene Ontology (GO)
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acid phosphatase activity Inferred from electronic annotation. Source: InterPro glucose-1-phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.1 Ref.5

Chain

23 – 413

391

Glucose-1-phosphatase

PRO_0000023948

Sites

Active site

40

1

Nucleophile

Active site

312

1

Proton donor

Secondary structure

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413

Helix Strand Turn

Details...

Beta strand

29 – 38

10

Helix

47 – 49

3

Helix

50 – 55

6

Helix

73 – 92

20

Beta strand

98 – 100

3

Beta strand

106 – 111

6

Helix

115 – 128

14

Turn

147 – 149

3

Helix

159 – 174

16

Helix

178 – 188

11

Helix

190 – 192

3

Turn

194 – 199

6

Turn

204 – 206

3

Beta strand

210 – 212

3

Beta strand

220 – 223

4

Helix

224 – 240

17

Turn

245 – 247

3

Helix

248 – 251

4

Helix

258 – 274

17

Helix

277 – 283

7

Helix

285 – 294

10

Turn

295 – 301

7

Beta strand

304 – 309

6

Helix

312 – 321

10

Beta strand

333 – 336

4

Beta strand

341 – 349

9

Turn

350 – 353

4

Beta strand

354 – 363

10

Helix

366 – 371

6

Beta strand

377 – 379

3

Beta strand

382 – 385

4

Helix

401 – 411

11

Sequences

	Sequence		Length	Mass (Da)
	P19926-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: ADADAD3639D0D6AB	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

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. , 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: 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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M33807 Genomic DNA. Translation: AAA23426.1.
U00096 Genomic DNA. Translation: AAC74087.1.
AP009048 Genomic DNA. Translation: BAA35769.1.

PIR

JV0087.

RefSeq

AP_001633.1.
NP_415522.1.

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2905N.

STRING

P19926.

Genome annotation databases

GeneID

945773.

GenomeReviews

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

KEGG

ecj:JW0987.
eco:b1002.

Organism-specific databases

EchoBASE

EB0032.

EcoGene

EG10033. agp.

CMR

Search...

Phylogenomic databases

HOGENOM

P19926.

OMA

LLVGHDS

Enzyme and pathway databases

BioCyc

EcoCyc:GLUCOSE-1-PHOSPHAT-MON.
ECOL168927:B1002-MON.
MetaCyc:GLUCOSE-1-PHOSPHAT-MON.

Gene expression databases

Genevestigator

P19926.

Family and domain databases

InterPro

IPR000560. Histidine_acid_Pase.
[Graphical view]

Pfam

PF00328. Acid_phosphat_A. 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:	November 24, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)