Reviewed, UniProtKB/Swiss-Prot P08059 (G6PI_PIG)

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
    Autocrine motility factor
      Short name=AMF
    Neuroleukin
      Short name=NLK

Gene names

Name:

GPI

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	558 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	Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons By similarity.
Catalytic activity	D-glucose 6-phosphate = D-fructose 6-phosphate.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
Subunit structure	Homodimer in the catalytically active form, monomer in the secreted form.
Subcellular location	Cytoplasm. Secreted.
Sequence similarities	Belongs to the GPI family.

Ontologies

Keywords
Biological process	Angiogenesis Gluconeogenesis Glycolysis
Cellular component	Cytoplasm Secreted
Molecular function	Cytokine Isomerase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cytokine activity Inferred from electronic annotation. Source: UniProtKB-KW glucose-6-phosphate isomerase 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

Initiator methionine

1

1

Removed

Chain

2 – 558

557

Glucose-6-phosphate isomerase

PRO_0000180540

Sites

Active site

358

1

Proton donor By similarity

Active site

389

1

By similarity

Active site

519

1

By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.1

Modified residue

12

1

N6-acetyllysine By similarity

Modified residue

109

1

Phosphothreonine By similarity

Modified residue

142

1

N6-acetyllysine By similarity

Modified residue

185

1

Phosphoserine; by CK2 By similarity

Experimental info

Sequence conflict

156 – 157

2

Missing Ref.3

Sequence conflict

344

1

Y → H in AAA31048. Ref.5

Sequence conflict

347 – 398

52

RFAAY…LIHQG → ALLPTSSRVTWSPTGSTSPS PAPVWTTRRAPLCGGSQGPM ASMPSTSSS in CAA82246. Ref.3

Sequence conflict

481 – 482

2

KL → NV in CAA82246. Ref.3

Sequence conflict

550

1

K → M in CAA82246. Ref.3

Secondary structure

1

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558

Helix Strand Turn

Details...

Helix

3 – 6

4

Helix

8 – 20

13

Helix

21 – 23

3

Helix

26 – 32

7

Helix

36 – 39

4

Beta strand

40 – 45

6

Beta strand

50 – 54

5

Helix

62 – 74

13

Helix

77 – 86

10

Turn

92 – 95

4

Helix

100 – 103

4

Beta strand

116 – 118

3

Helix

119 – 138

20

Beta strand

151 – 155

5

Helix

159 – 170

12

Helix

172 – 175

4

Beta strand

180 – 184

5

Helix

189 – 196

8

Helix

201 – 203

3

Beta strand

204 – 209

6

Beta strand

211 – 213

3

Helix

216 – 233

18

Helix

236 – 241

6

Beta strand

243 – 248

6

Helix

250 – 255

6

Helix

260 – 262

3

Beta strand

263 – 265

3

Helix

272 – 274

3

Turn

276 – 278

3

Helix

279 – 281

3

Helix

282 – 288

7

Helix

290 – 309

20

Helix

312 – 314

3

Helix

316 – 329

14

Beta strand

335 – 341

7

Helix

343 – 345

3

Helix

348 – 360

13

Beta strand

378 – 380

3

Helix

386 – 389

4

Helix

392 – 397

6

Beta strand

398 – 400

3

Beta strand

404 – 411

8

Helix

416 – 438

23

Helix

442 – 451

10

Helix

456 – 459

4

Turn

460 – 462

3

Helix

463 – 466

4

Beta strand

474 – 481

8

Helix

484 – 505

22

Helix

513 – 515

3

Helix

516 – 528

13

Beta strand

530 – 533

4

Helix

540 – 554

15

Sequences

	Sequence		Length	Mass (Da)
	P08059-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 84DA1B15CF0C702F	FASTA	558	63,126
	10 20 30 40 50 60 MAALTQNPQF KKLQTWYHEH RSDLNLRRLF EGDKDRFNHF SLNLNTNHGR ILLDYSKNLV 70 80 90 100 110 120 TEAVMQMLVD LAKSRGVEAA RERMFNGEKI NFTEDRAVLH VALRNRSNTP ILVDGKDVMP 130 140 150 160 170 180 EVNRVLEKMK SFCKRVRSGE WKGYSGKSIT DVINIGIGGS DLGPLMVTEA LKPYSAEGPR 190 200 210 220 230 240 VWFVSNIDGT HIAKTLATLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QSAKDPSAVA 250 260 270 280 290 300 KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA 310 320 330 340 350 360 HWMDQHFRTT PLEKNAPVLL ALLGIWYINF FGCETHAMLP YDQYLHRFAA YFQQGDMESN 370 380 390 400 410 420 GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL 430 440 450 460 470 480 HHKILLANFL AQTEALMKGK STEEARKELQ AAGKSPEDFE KLLPHKVFEG NRPTNSIVFT 490 500 510 520 530 540 KLTPFILGAL IAMYEHKIFV QGVIWDINSF DQWGVELGKQ LAKKIEPELD GSSPVTSHDS 550 STNGLINFIK QEREARSQ

References

[1]	"The neurotrophic factor neuroleukin is 90% homologous with phosphohexose isomerase." Chaput M., Claes V., Portetelle D., Clutdts I., Cravador A., Burny A., Gras H., Tartar A. Nature 332:454-455(1988) [PubMed: 3352744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Burny A. Submitted (AUG-1988) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Structure of the gene encoding pig phosphoglucose isomerase." Claes V., Kettmann R., Burny A. Gene 150:235-241(1994) [PubMed: 7821788] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Sequence analysis of the pig phosphoglucose isomerase gene promoter region." Claes V., Taquet A.N., Kettmann R., Burny A. Biochim. Biophys. Acta 1087:339-340(1990) [PubMed: 2248981] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-17. Strain: Belgian Landrace.
[5]	"A partial cDNA clone for porcine glucosephosphate isomerase: isolation, characterization and use in detection of restriction fragment length polymorphisms." Davies W., Harbitz I., Hauge J.G. Anim. Genet. 18:233-240(1987) [PubMed: 2889410] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 238-357.
[6]	"Three-dimensional structure of pig muscle phosphoglucose isomerase at 6-A resolution." Muirhead H., Shaw P.J. J. Mol. Biol. 89:195-203(1974) [PubMed: 4475113] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
[7]	"Glucose-6-phosphate isomerase." Achari A., Marshall S.E., Muirhead H., Palmieri R.H., Noltmann E.A. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 293:145-157(1981) [PubMed: 6115414] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), PROTEIN SEQUENCE OF 554-558.
[8]	"Crystal structure of phosphoglucose isomerase from pig muscle and its complex with 5-phosphoarabinonate." Davies C., Muirhead H. Proteins 49:577-579(2002) [PubMed: 12402366] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) ALONE AND IN COMPLEX WITH 5-PHOSPHOARABINONATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X07382 mRNA. Translation: CAA30295.1.
Z28396 , Z28397, Z28398, Z28399, Z28400, Z28401, Z28402, Z28403, Z28404 Genomic DNA. Translation: CAA82246.1.
X53719 mRNA. Translation: CAA37755.1.
M54975 mRNA. Translation: AAA31048.1.

PIR

I47142.
NUPG. S00895.

RefSeq

NP_999495.1.

UniGene

Ssc.2375

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GZD	X-ray	2.50	A	2-557	[»]
1GZV	X-ray	3.51	A	2-557	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSSSCT00000003175; ENSSSCP00000003094; ENSSSCG00000002873; Sus scrofa. [Genome view]

GeneID

397602.

KEGG

ssc:397602.

Organism-specific databases

CTD

397602.

Phylogenomic databases

HOVERGEN

P08059.

Enzyme and pathway databases

BRENDA

5.3.1.9. 249.

Family and domain databases

InterPro

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

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_PIG

Accession

Primary (citable) accession number: P08059
Secondary accession number(s): Q29556

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)