P0A6T1 (G6PI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucose-6-phosphate isomerase
Short name=GPI
EC=5.3.1.9

Alternative name(s):
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI

Gene names

Name:	pgi
Ordered Locus Names:	b4025, JW3985

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	549 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glucose 6-phosphate = D-fructose 6-phosphate. HAMAP MF_00473
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. HAMAP MF_00473
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP MF_00473.
Sequence similarities	Belongs to the GPI family.

Ontologies

Keywords
Biological process	Gluconeogenesis Glycolysis
Cellular component	Cytoplasm
Molecular function	Isomerase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to oxidative stress Inferred from expression pattern. Source: EcoCyc gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW glycolysis Inferred from mutant phenotype. Source: EcoCyc
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	glucose-6-phosphate isomerase activity Inferred from direct assay. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 549

549

Glucose-6-phosphate isomerase HAMAP MF_00473

PRO_0000180641

Sites

Active site

355

1

Proton donor By similarity

Active site

386

1

By similarity

Active site

514

1

By similarity

Amino acid modifications

Modified residue

80

1

N6-acetyllysine Ref.6

Modified residue

228

1

N6-acetyllysine Ref.6

Modified residue

234

1

N6-acetyllysine Ref.6

Experimental info

Sequence conflict

317

1

L → V Ref.1

Sequence conflict

317

1

L → V Ref.2

Secondary structure

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549

Helix Strand Turn

Details...

Helix

6 – 8

3

Helix

10 – 22

13

Helix

27 – 33

7

Helix

37 – 40

4

Beta strand

41 – 45

5

Turn

46 – 48

3

Beta strand

49 – 52

4

Beta strand

55 – 57

3

Helix

60 – 72

13

Helix

75 – 83

9

Turn

90 – 93

4

Helix

98 – 101

4

Beta strand

114 – 116

3

Helix

117 – 135

19

Beta strand

149 – 153

5

Helix

156 – 158

3

Helix

160 – 168

9

Helix

170 – 172

3

Beta strand

177 – 181

5

Helix

186 – 193

8

Helix

198 – 200

3

Beta strand

201 – 206

6

Beta strand

208 – 210

3

Helix

213 – 230

18

Helix

233 – 238

6

Beta strand

240 – 244

5

Helix

257 – 259

3

Beta strand

260 – 262

3

Helix

269 – 271

3

Helix

276 – 278

3

Helix

279 – 285

7

Helix

287 – 306

20

Helix

309 – 311

3

Helix

313 – 326

14

Beta strand

332 – 338

7

Helix

340 – 342

3

Helix

345 – 357

13

Beta strand

375 – 377

3

Turn

381 – 384

4

Helix

385 – 394

10

Beta strand

395 – 397

3

Beta strand

401 – 408

8

Helix

416 – 433

18

Helix

437 – 446

10

Helix

451 – 453

3

Turn

455 – 457

3

Helix

458 – 461

4

Beta strand

469 – 476

8

Helix

479 – 499

21

Helix

508 – 510

3

Helix

511 – 523

13

Helix

535 – 547

13

Sequences

	Sequence		Length	Mass (Da)
	P0A6T1 [UniParc]. Last modified March 29, 2005. Version 1. Checksum: 74AEDB670A068A01	FASTA	549	61,530
	10 20 30 40 50 60 MKNINPTQTA AWQALQKHFD EMKDVTIADL FAKDGDRFSK FSATFDDQML VDYSKNRITE 70 80 90 100 110 120 ETLAKLQDLA KECDLAGAIK SMFSGEKINR TENRAVLHVA LRNRSNTPIL VDGKDVMPEV 130 140 150 160 170 180 NAVLEKMKTF SEAIISGEWK GYTGKAITDV VNIGIGGSDL GPYMVTEALR PYKNHLNMHF 190 200 210 220 230 240 VSNVDGTHIA EVLKKVNPET TLFLVASKTF TTQETMTNAH SARDWFLKAA GDEKHVAKHF 250 260 270 280 290 300 AALSTNAKAV GEFGIDTANM FEFWDWVGGR YSLWSAIGLS IVLSIGFDNF VELLSGAHAM 310 320 330 340 350 360 DKHFSTTPAE KNLPVLLALI GIWYNNFFGA ETEAILPYDQ YMHRFAAYFQ QGNMESNGKY 370 380 390 400 410 420 VDRNGNVVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKMVP CDFIAPAITH NPLSDHHQKL 430 440 450 460 470 480 LSNFFAQTEA LAFGKSREVV EQEYRDQGKD PATLDYVVPF KVFEGNRPTN SILLREITPF 490 500 510 520 530 540 SLGALIALYE HKIFTQGVIL NIFTFDQWGV ELGKQLANRI LPELKDDKEI SSHDSSTNGL INRYKAWRG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the phosphoglucose isomerase gene from Escherichia coli." Froman B.E., Tait R.C., Gottlieb L.D. Mol. Gen. Genet. 217:126-131(1989) [PubMed: 2549364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926.
[2]	"Anomalous phylogeny involving the enzyme glucose-6-phosphate isomerase." Smith M.W., Doolittle R.F. J. Mol. Evol. 34:544-545(1992) [PubMed: 1593646] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PHYLOGENETIC STUDY. Strain: XL1 Blue 2.
[3]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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.
[5]	"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.
[6]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-228 AND LYS-234, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X15196 Genomic DNA. Translation: CAA33268.1.
U00006 Genomic DNA. Translation: AAC43119.1.
U00096 Genomic DNA. Translation: AAC76995.1.
AP009048 Genomic DNA. Translation: BAE78027.1.

PIR

NUEC. H65209.

RefSeq

NP_418449.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NBU	X-ray	2.05	A/B/C/D/E/F	1-549	[»]

ProteinModelPortal

P0A6T1.

SMR

P0A6T1. Positions 1-549.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35887N.

IntAct

P0A6T1. 9 interactions.

PTM databases

PhosSite

P0A6T1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000965; EBESCP00000000965; EBESCG00000000793.
EBESCT00000015863; EBESCP00000015154; EBESCG00000014923.

GeneID

948535.

GenomeReviews

Gene locus JW3985 in contig AP009048_GR.
Gene locus b4025 in contig U00096_GR.

KEGG

ecj:JW3985.
eco:b4025.

PATRIC

32123579. VBIEscCol129921_4138.

Organism-specific databases

EchoBASE

EB0696.

EcoGene

EG10702. pgi.

Phylogenomic databases

eggNOG

COG0166.

GeneTree

EBGT00050000009591.

HOGENOM

HBG352954.

OMA

GPKIVSQ.

PhylomeDB

P0A6T1.

ProtClustDB

PRK00179.

Enzyme and pathway databases

BioCyc

EcoCyc:PGLUCISOM.
MetaCyc:PGLUCISOM.

Gene expression databases

Genevestigator

P0A6T1.

Family and domain databases

HAMAP

MF_00473. G6P_isomerase.
[Tree]

InterPro

IPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]

Gene3D

G3DSA:1.10.1390.10. G6P_Isomerase_C. 1 hit.

KO

K01810.

PANTHER

PTHR11469. G6P_Isomerase. 1 hit.

Pfam

PF00342. PGI. 1 hit.
[Graphical view]

PRINTS

PR00662. G6PISOMERASE.

PROSITE

PS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

G6PI_ECOLI

Accession

Primary (citable) accession number: P0A6T1
Secondary accession number(s): P11537, Q2M6S9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 29, 2005
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program