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Protein

Glucose-6-phosphate isomerase

Gene

GPI

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

D-glucose 6-phosphate = D-fructose 6-phosphate.

Pathwayi: glycolysis

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI)
  3. ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKM)
  4. Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase A (ALDOA)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei358Proton donor1
Active sitei3891
Active sitei5191

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Isomerase

Keywords - Biological processi

Angiogenesis, Gluconeogenesis, Glycolysis

Enzyme and pathway databases

BRENDAi5.3.1.9. 1749.
SABIO-RKQ9N1E2.
UniPathwayiUPA00109; UER00181.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate isomerase (EC:5.3.1.9)
Short name:
GPI
Alternative name(s):
Autocrine motility factor
Short name:
AMF
Neuroleukin
Short name:
NLK
Phosphoglucose isomerase
Short name:
PGI
Phosphohexose isomerase
Short name:
PHI
Gene namesi
Name:GPI
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1770045.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001805412 – 558Glucose-6-phosphate isomeraseAdd BLAST557

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei12N6-acetyllysineBy similarity1
Modified residuei107PhosphoserineBy similarity1
Modified residuei109PhosphothreonineBy similarity1
Modified residuei142N6-acetyllysineBy similarity1
Modified residuei185Phosphoserine; by CK2By similarity1
Modified residuei250PhosphothreonineBy similarity1
Modified residuei454N6-acetyllysine; alternateBy similarity1
Modified residuei454N6-malonyllysine; alternateBy similarity1
Modified residuei454N6-succinyllysine; alternateBy similarity1
Modified residuei455PhosphoserineBy similarity1

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ9N1E2.

Interactioni

Subunit structurei

Homodimer in the catalytically active form, monomer in the secreted form.5 Publications

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000001250.

Chemistry databases

BindingDBiQ9N1E2.

Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Helixi8 – 20Combined sources13
Helixi21 – 23Combined sources3
Helixi26 – 31Combined sources6
Helixi36 – 39Combined sources4
Beta strandi41 – 45Combined sources5
Beta strandi50 – 54Combined sources5
Beta strandi57 – 59Combined sources3
Helixi62 – 74Combined sources13
Helixi77 – 85Combined sources9
Turni92 – 95Combined sources4
Helixi100 – 103Combined sources4
Beta strandi112 – 118Combined sources7
Helixi119 – 138Combined sources20
Beta strandi151 – 155Combined sources5
Helixi158 – 160Combined sources3
Helixi162 – 170Combined sources9
Helixi172 – 174Combined sources3
Beta strandi180 – 184Combined sources5
Helixi189 – 196Combined sources8
Helixi201 – 203Combined sources3
Beta strandi204 – 209Combined sources6
Beta strandi211 – 213Combined sources3
Helixi216 – 233Combined sources18
Helixi236 – 238Combined sources3
Helixi239 – 242Combined sources4
Beta strandi243 – 248Combined sources6
Helixi250 – 256Combined sources7
Helixi260 – 262Combined sources3
Beta strandi263 – 265Combined sources3
Helixi272 – 274Combined sources3
Turni276 – 278Combined sources3
Helixi279 – 281Combined sources3
Helixi282 – 288Combined sources7
Helixi290 – 309Combined sources20
Helixi312 – 314Combined sources3
Helixi316 – 329Combined sources14
Beta strandi335 – 341Combined sources7
Helixi343 – 345Combined sources3
Helixi348 – 360Combined sources13
Beta strandi378 – 380Combined sources3
Turni384 – 386Combined sources3
Helixi387 – 389Combined sources3
Helixi392 – 397Combined sources6
Beta strandi398 – 400Combined sources3
Beta strandi404 – 411Combined sources8
Helixi417 – 419Combined sources3
Helixi420 – 438Combined sources19
Helixi442 – 451Combined sources10
Helixi456 – 462Combined sources7
Helixi463 – 466Combined sources4
Beta strandi474 – 481Combined sources8
Helixi484 – 504Combined sources21
Helixi513 – 515Combined sources3
Helixi516 – 529Combined sources14
Beta strandi530 – 533Combined sources4
Helixi540 – 552Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DQRX-ray2.50A/B2-558[»]
1G98X-ray1.90A/B1-558[»]
1HM5X-ray1.80A/B1-558[»]
1HOXX-ray2.10A/B1-558[»]
1KOJX-ray1.90A/B2-558[»]
1N8TX-ray2.50A/B2-558[»]
1XTBX-ray2.00A/B1-558[»]
ProteinModelPortaliQ9N1E2.
SMRiQ9N1E2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9N1E2.

Family & Domainsi

Sequence similaritiesi

Belongs to the GPI family.Curated

Phylogenomic databases

eggNOGiKOG2446. Eukaryota.
COG0166. LUCA.
HOGENOMiHOG000261370.
HOVERGENiHBG002877.
InParanoidiQ9N1E2.
KOiK01810.

Family and domain databases

Gene3Di1.10.1390.10. 1 hit.
HAMAPiMF_00473. G6P_isomerase. 1 hit.
InterProiIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERiPTHR11469. PTHR11469. 1 hit.
PfamiPF00342. PGI. 1 hit.
[Graphical view]
PRINTSiPR00662. G6PISOMERASE.
PROSITEiPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9N1E2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALTRNPQF QKLQQWHREH GSELNLRHLF DTDKERFNHF SLTLNTNHGH
60 70 80 90 100
ILLDYSKNLV TEEVMHMLLD LAKSRGVEAA RESMFNGEKI NSTEDRAVLH
110 120 130 140 150
VALRNRSNTP IVVDGKDVMP EVNKVLDKMK AFCQRVRSGD WKGYTGKTIT
160 170 180 190 200
DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWFVSNIDGT HIAKTLACLN
210 220 230 240 250
PESSLFIIAS KTFTTQETIT NAETAKDWFL LSAKDPSTVA KHFVALSTNT
260 270 280 290 300
AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA
310 320 330 340 350
HWMDQHFRTT PLEKNAPVLL AMLGIWYINC FGCETQAVLP YDQYLHRFAA
360 370 380 390 400
YFQQGDMESN GKYITKSGAR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK
410 420 430 440 450
MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMKGK STEEARKELQ
460 470 480 490 500
AAGKSPEDLM KLLPHKVFEG NRPTNSIVFT KLTPFILGAL IAMYEHKIFV
510 520 530 540 550
QGVVWDINSF DQWGVELGKQ LAKKIEPELD GSSPVTSHDS STNGLINFIK

QQREAKIQ
Length:558
Mass (Da):62,747
Last modified:January 23, 2007 - v3
Checksum:iBB4E3AB31BBD55E4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti223E → K in AAF35988 (PubMed:10653639).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF199601 mRNA. Translation: AAF13713.2.
AF222069 mRNA. Translation: AAF35988.1.
RefSeqiNP_001075538.1. NM_001082069.2.
UniGeneiOcu.278.

Genome annotation databases

GeneIDi100008744.
KEGGiocu:100008744.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF199601 mRNA. Translation: AAF13713.2.
AF222069 mRNA. Translation: AAF35988.1.
RefSeqiNP_001075538.1. NM_001082069.2.
UniGeneiOcu.278.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DQRX-ray2.50A/B2-558[»]
1G98X-ray1.90A/B1-558[»]
1HM5X-ray1.80A/B1-558[»]
1HOXX-ray2.10A/B1-558[»]
1KOJX-ray1.90A/B2-558[»]
1N8TX-ray2.50A/B2-558[»]
1XTBX-ray2.00A/B1-558[»]
ProteinModelPortaliQ9N1E2.
SMRiQ9N1E2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000001250.

Chemistry databases

BindingDBiQ9N1E2.
ChEMBLiCHEMBL1770045.

Proteomic databases

PRIDEiQ9N1E2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008744.
KEGGiocu:100008744.

Organism-specific databases

CTDi2821.

Phylogenomic databases

eggNOGiKOG2446. Eukaryota.
COG0166. LUCA.
HOGENOMiHOG000261370.
HOVERGENiHBG002877.
InParanoidiQ9N1E2.
KOiK01810.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00181.
BRENDAi5.3.1.9. 1749.
SABIO-RKQ9N1E2.

Miscellaneous databases

EvolutionaryTraceiQ9N1E2.
PROiQ9N1E2.

Family and domain databases

Gene3Di1.10.1390.10. 1 hit.
HAMAPiMF_00473. G6P_isomerase. 1 hit.
InterProiIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERiPTHR11469. PTHR11469. 1 hit.
PfamiPF00342. PGI. 1 hit.
[Graphical view]
PRINTSiPR00662. G6PISOMERASE.
PROSITEiPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiG6PI_RABIT
AccessioniPrimary (citable) accession number: Q9N1E2
Secondary accession number(s): Q9N184
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.