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Q9N1E2 (G6PI_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate isomerase
Short name=GPI
EC=5.3.1.9
Alternative name(s):
Autocrine motility factor
Short name=AMF
Neuroleukin
Short name=NLK
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Gene names
Name:GPI
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Post-translational modification

ISGylated By similarity.

Sequence similarities

Belongs to the GPI family.

Ontologies

Keywords
   Biological processAngiogenesis
Gluconeogenesis
Glycolysis
   Cellular componentCytoplasm
Secreted
   Molecular functionCytokine
Isomerase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

gluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

glycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglucose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 558557Glucose-6-phosphate isomerase
PRO_0000180541

Sites

Active site3581Proton donor Ref.3 Ref.4
Active site3891 Ref.3 Ref.4
Active site5191 Ref.3 Ref.4

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue121N6-acetyllysine By similarity
Modified residue1091Phosphothreonine By similarity
Modified residue1421N6-acetyllysine By similarity
Modified residue1851Phosphoserine; by CK2 By similarity
Modified residue4541N6-malonyllysine By similarity

Experimental info

Sequence conflict2231E → K in AAF35988. Ref.2

Secondary structure

1 ..................................................................................................... 558
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9N1E2 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BB4E3AB31BBD55E4

FASTA55862,747
        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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH D-SORBITOL-6-PHOSPHATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF199601 mRNA. Translation: AAF13713.2.
AF222069 mRNA. Translation: AAF35988.1.
RefSeqNP_001075538.1. NM_001082069.2.
UniGeneOcu.278.

3D structure databases

PDBe
RCSB PDB
PDBj
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/B2-557[»]
1N8TX-ray2.50A/B2-557[»]
1XTBX-ray2.00A/B1-558[»]
ProteinModelPortalQ9N1E2.
SMRQ9N1E2. Positions 2-558.
ModBaseSearch...

Proteomic databases

PRIDEQ9N1E2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100008744.

Organism-specific databases

CTD2821.

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261370.
HOVERGENHBG002877.
OrthoDBEOG44MXRS.

Enzyme and pathway databases

SABIO-RKQ9N1E2.
UniPathwayUPA00109; UER00181.

Family and domain databases

Gene3D1.10.1390.10. 1 hit.
InterProIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERPTHR11469. PTHR11469. 1 hit.
PfamPF00342. PGI. 1 hit.
[Graphical view]
PRINTSPR00662. G6PISOMERASE.
PROSITEPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ9N1E2.
ChEMBLCHEMBL1770045.
EvolutionaryTraceQ9N1E2.

Entry information

Entry nameG6PI_RABIT
AccessionPrimary (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: April 3, 2013
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

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

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