Reviewed, UniProtKB/Swiss-Prot Q9N1E2 (G6PI_RABIT)

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

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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. Ref.5
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
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_0000180541

Sites

Active site

358

1

Proton donor Ref.3 Ref.4

Active site

389

1

Ref.3 Ref.4

Active site

519

1

Ref.3 Ref.4

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

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

223

1

E → K in AAF35988. Ref.2

Secondary structure

1

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558

Helix Strand Turn

Details...

Turn

3 – 6

4

Helix

8 – 20

13

Helix

21 – 23

3

Helix

26 – 31

6

Helix

36 – 39

4

Beta strand

41 – 45

5

Beta strand

50 – 54

5

Helix

62 – 74

13

Helix

77 – 85

9

Turn

92 – 95

4

Helix

100 – 103

4

Beta strand

112 – 118

7

Helix

119 – 137

19

Beta strand

151 – 155

5

Helix

158 – 160

3

Helix

162 – 170

9

Helix

172 – 174

3

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 – 232

17

Helix

239 – 241

3

Beta strand

243 – 248

6

Helix

250 – 255

6

Helix

260 – 262

3

Beta strand

263 – 265

3

Helix

272 – 274

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

404 – 411

8

Helix

416 – 419

4

Helix

420 – 438

19

Helix

442 – 450

9

Turn

451 – 453

3

Helix

458 – 462

5

Helix

463 – 466

4

Beta strand

474 – 481

8

Helix

484 – 505

22

Helix

513 – 525

13

Helix

526 – 529

4

Beta strand

530 – 533

4

Helix

540 – 552

13

Sequences

	Sequence		Length	Mass (Da)
	Q9N1E2-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: BB4E3AB31BBD55E4	FASTA	558	62,747
	10 20 30 40 50 60 MAALTRNPQF QKLQQWHREH GSELNLRHLF DTDKERFNHF SLTLNTNHGH ILLDYSKNLV 70 80 90 100 110 120 TEEVMHMLLD LAKSRGVEAA RESMFNGEKI NSTEDRAVLH VALRNRSNTP IVVDGKDVMP 130 140 150 160 170 180 EVNKVLDKMK AFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSGGPR 190 200 210 220 230 240 VWFVSNIDGT HIAKTLACLN PESSLFIIAS KTFTTQETIT NAETAKDWFL LSAKDPSTVA 250 260 270 280 290 300 KHFVALSTNT AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA 310 320 330 340 350 360 HWMDQHFRTT PLEKNAPVLL AMLGIWYINC FGCETQAVLP YDQYLHRFAA YFQQGDMESN 370 380 390 400 410 420 GKYITKSGAR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL 430 440 450 460 470 480 HHKILLANFL AQTEALMKGK STEEARKELQ AAGKSPEDLM KLLPHKVFEG NRPTNSIVFT 490 500 510 520 530 540 KLTPFILGAL IAMYEHKIFV QGVVWDINSF DQWGVELGKQ LAKKIEPELD GSSPVTSHDS 550 STNGLINFIK QQREAKIQ

References

[1]	"Rabbit phosphoglucose isomerase/neuroleukin/autocrine motility factor: cloning via interspecies identity." Li X., Chirgwin J.M. Biochim. Biophys. Acta 1476:363-367(2000) [PubMed: 10669800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: New Zealand white. Tissue: Fast-twitch skeletal muscle.
[2]	"Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator." Jeffery C.J., Bahnson B.J., Chien W., Ringe D., Petsko G.A. Biochemistry 39:955-964(2000) [PubMed: 10653639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). Strain: New Zealand white. Tissue: Muscle.
[3]	"Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonate identifies the role of Glu357 in catalysis." Jeffery C.J., Hardre R., Salmon L. Biochemistry 40:1560-1566(2001) [PubMed: 11327814] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH 5-PHOSPHO-D-ARABINONATE, ACTIVE SITE.
[4]	"Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate." Lee J.H., Chang K.Z., Patel V., Jeffery C.J. Biochemistry 40:7799-7805(2001) [PubMed: 11425306] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH F6P, ACTIVE SITE.
[5]	"Conformational changes in phosphoglucose isomerase induced by ligand binding." Arsenieva D., Jeffery C.J. J. Mol. Biol. 323:77-84(2002) [PubMed: 12368100] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT.
[6]	"The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid." Arsenieva D., Hardre R., Salmon L., Jeffery C.J. Proc. Natl. Acad. Sci. U.S.A. 99:5872-5877(2002) [PubMed: 11983887] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH 5-PHOSPHO-D-ARABINONOHYDROXAMIC ACID.
[7]	"Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function." Davies C., Muirhead H. Acta Crystallogr. D 59:453-465(2003) [PubMed: 12595702] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[8]	"The crystal structure of rabbit phosphoglucose isomerase complexed with D-sorbitol-6-phosphate, an analog of the open chain form of D-glucose-6-phosphate." Lee J.H., Jeffery C.J. Protein Sci. 14:727-734(2005) [PubMed: 15689508] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH D-SORBITOL-6-PHOSPHATE.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF199601 mRNA. Translation: AAF13713.2.
AF222069 mRNA. Translation: AAF35988.1.

RefSeq

NP_001075538.1.

UniGene

Ocu.278

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DQR	X-ray	2.50	A/B	2-558	[»]
1G98	X-ray	1.90	A/B	1-558	[»]
1HM5	X-ray	1.80	A/B	1-558	[»]
1HOX	X-ray	2.10	A/B	1-558	[»]
1KOJ	X-ray	1.90	A/B	2-557	[»]
1N8T	X-ray	2.50	A/B	2-557	[»]
1XTB	X-ray	2.00	A/B	1-558	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9N1E2.

Genome annotation databases

GeneID

100008744.

Organism-specific databases

CTD

100008744.

Phylogenomic databases

HOVERGEN

Q9N1E2.

Enzyme and pathway databases

BRENDA

5.3.1.9. 255.

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_RABIT

Accession

Primary (citable) accession number: Q9N1E2
Secondary accession number(s): Q9N184

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 62 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)