UniProtKB - Q9N1E2 (G6PI_RABIT)
Glucose-6-phosphate isomerase
GPI
Functioni
In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (By similarity).
Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility. Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons. It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (By similarity).
By similarityCatalytic activityi
- EC:5.3.1.9By similarity
: glycolysis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.By similarity 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 354 | Glucose-6-phosphateCombined sources1 Publication | 1 | |
Active sitei | 358 | Proton donor2 Publications | 1 | |
Binding sitei | 358 | Glucose-6-phosphateCombined sources1 Publication | 1 | |
Active sitei | 389 | 2 Publications | 1 | |
Binding sitei | 389 | Glucose-6-phosphateCombined sources1 Publication | 1 | |
Active sitei | 519 | 2 Publications | 1 | |
Binding sitei | 519 | Glucose-6-phosphateBy similarity | 1 |
GO - Molecular functioni
- cytokine activity Source: UniProtKB-KW
- glucose-6-phosphate isomerase activity Source: UniProtKB
GO - Biological processi
- gluconeogenesis Source: UniProtKB-KW
- glucose 6-phosphate metabolic process Source: UniProtKB
- glycolytic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Cytokine, Isomerase |
Biological process | Gluconeogenesis, Glycolysis |
Enzyme and pathway databases
BRENDAi | 5.3.1.9, 1749 |
SABIO-RKi | Q9N1E2 |
UniPathwayi | UPA00109;UER00181 |
Names & Taxonomyi
Protein namesi | Recommended name: Glucose-6-phosphate isomeraseBy similarity (EC:5.3.1.9By similarity)Short name: GPIBy similarity Alternative name(s): Autocrine motility factor1 Publication Short name: AMF1 Publication Neuroleukin1 Publication Short name: NLK1 Publication Phosphoglucose isomerase1 Publication Short name: PGI1 Publication Phosphohexose isomeraseBy similarity Short name: PHIBy similarity |
Gene namesi | Name:GPIBy similarity |
Organismi | Oryctolagus cuniculus (Rabbit) |
Taxonomic identifieri | 9986 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
- extracellular space Source: UniProtKB-KW
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cytoplasm, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000180541 | 2 – 558 | Glucose-6-phosphate isomeraseAdd BLAST | 557 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Modified residuei | 12 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 34 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 107 | PhosphoserineBy similarity | 1 | |
Modified residuei | 109 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 142 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 185 | Phosphoserine; by CK2By similarity | 1 | |
Modified residuei | 250 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 454 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 454 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 454 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 455 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Hydroxylation, Phosphoprotein, Ubl conjugationInteractioni
Subunit structurei
Homodimer in the catalytically active form, monomer in the secreted form.
5 PublicationsGO - Molecular functioni
- cytokine activity Source: UniProtKB-KW
Protein-protein interaction databases
STRINGi | 9986.ENSOCUP00000001250 |
Chemistry databases
BindingDBi | Q9N1E2 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q9N1E2 |
SMRi | Q9N1E2 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9N1E2 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 159 – 160 | Glucose-6-phosphate bindingCombined sources1 Publication | 2 | |
Regioni | 210 – 215 | Glucose-6-phosphate bindingCombined sources1 Publication | 6 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2446, Eukaryota |
InParanoidi | Q9N1E2 |
OrthoDBi | 446616at2759 |
Family and domain databases
CDDi | cd05015, SIS_PGI_1, 1 hit cd05016, SIS_PGI_2, 1 hit |
Gene3Di | 1.10.1390.10, 1 hit |
HAMAPi | MF_00473, G6P_isomerase, 1 hit |
InterProi | View protein in InterPro IPR001672, G6P_Isomerase IPR023096, G6P_Isomerase_C IPR018189, Phosphoglucose_isomerase_CS IPR046348, SIS_dom_sf IPR035476, SIS_PGI_1 IPR035482, SIS_PGI_2 |
PANTHERi | PTHR11469, PTHR11469, 1 hit |
Pfami | View protein in Pfam PF00342, PGI, 1 hit |
PRINTSi | PR00662, G6PISOMERASE |
SUPFAMi | SSF53697, SSF53697, 1 hit |
PROSITEi | View protein in PROSITE PS00765, P_GLUCOSE_ISOMERASE_1, 1 hit PS00174, P_GLUCOSE_ISOMERASE_2, 1 hit PS51463, P_GLUCOSE_ISOMERASE_3, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 223 | E → K in AAF35988 (PubMed:10653639).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF199601 mRNA Translation: AAF13713.2 AF222069 mRNA Translation: AAF35988.1 |
RefSeqi | NP_001075538.1, NM_001082069.2 |
Genome annotation databases
GeneIDi | 100008744 |
KEGGi | ocu:100008744 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF199601 mRNA Translation: AAF13713.2 AF222069 mRNA Translation: AAF35988.1 |
RefSeqi | NP_001075538.1, NM_001082069.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | 2-558 | [»] | |
1N8T | X-ray | 2.50 | A/B | 2-558 | [»] | |
1XTB | X-ray | 2.00 | A/B | 1-558 | [»] | |
AlphaFoldDBi | Q9N1E2 | |||||
SMRi | Q9N1E2 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 9986.ENSOCUP00000001250 |
Chemistry databases
BindingDBi | Q9N1E2 |
ChEMBLi | CHEMBL1770045 |
Genome annotation databases
GeneIDi | 100008744 |
KEGGi | ocu:100008744 |
Organism-specific databases
CTDi | 2821 |
Phylogenomic databases
eggNOGi | KOG2446, Eukaryota |
InParanoidi | Q9N1E2 |
OrthoDBi | 446616at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00181 |
BRENDAi | 5.3.1.9, 1749 |
SABIO-RKi | Q9N1E2 |
Miscellaneous databases
EvolutionaryTracei | Q9N1E2 |
PROi | PR:Q9N1E2 |
Family and domain databases
CDDi | cd05015, SIS_PGI_1, 1 hit cd05016, SIS_PGI_2, 1 hit |
Gene3Di | 1.10.1390.10, 1 hit |
HAMAPi | MF_00473, G6P_isomerase, 1 hit |
InterProi | View protein in InterPro IPR001672, G6P_Isomerase IPR023096, G6P_Isomerase_C IPR018189, Phosphoglucose_isomerase_CS IPR046348, SIS_dom_sf IPR035476, SIS_PGI_1 IPR035482, SIS_PGI_2 |
PANTHERi | PTHR11469, PTHR11469, 1 hit |
Pfami | View protein in Pfam PF00342, PGI, 1 hit |
PRINTSi | PR00662, G6PISOMERASE |
SUPFAMi | SSF53697, SSF53697, 1 hit |
PROSITEi | View protein in PROSITE PS00765, P_GLUCOSE_ISOMERASE_1, 1 hit PS00174, P_GLUCOSE_ISOMERASE_2, 1 hit PS51463, P_GLUCOSE_ISOMERASE_3, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | G6PI_RABIT | |
Accessioni | Q9N1E2Primary (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: | May 25, 2022 | |
This is version 127 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families