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P49105 (G6PI_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate isomerase, cytosolic

Short name=GPI
EC=5.3.1.9
Alternative name(s):
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Gene names
Name:PHI1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

D-glucose 6-phosphate = D-fructose 6-phosphate. HAMAP-Rule MF_00473

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. HAMAP-Rule MF_00473

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00473

Subcellular location

Cytoplasm HAMAP-Rule MF_00473.

Sequence similarities

Belongs to the GPI family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
   Cellular componentCytoplasm
   Molecular functionIsomerase
Gene Ontology (GO)
   Biological_processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

glycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 567567Glucose-6-phosphate isomerase, cytosolic HAMAP-Rule MF_00473
PRO_0000180564

Sites

Active site3601Proton donor By similarity
Active site3911 By similarity
Active site5161 By similarity

Sequences

Sequence LengthMass (Da)Tools
P49105 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: EC135C89DAADACF2

FASTA56762,237
        10         20         30         40         50         60 
MASAALICGT EQWKALQAHV GAIQKTHLRD LMADADRCKA MTAEYEGIFL DYSRQQATGE 

        70         80         90        100        110        120 
TMEKLLKLAD AAKLKEKIEK MFKGEKINST ENRSVLHVAL RAPRDAVINS DGVNVVPEVW 

       130        140        150        160        170        180 
SVKDKIKQFS ETFRSGSWVG ATGKPLTNVV SVGIGGSFLG PLFVHTALQT DPEAAECAKG 

       190        200        210        220        230        240 
RQLRFLANVD PVDVARSIKD LDPETTLVVV VSKTFTTAET MLNARTLKEW IVSSLGPQAV 

       250        260        270        280        290        300 
AKHMIAVSTN LKLVKEFGID PNNAFAFWDW VGGRYSVCSA VGVLPLSLQY GFPIVQKFLE 

       310        320        330        340        350        360 
GASSIDNHFY SSSFEKNIPV LLGLLSVWNV SFLGYPARAI LPYSQALEKL APHIQQLSME 

       370        380        390        400        410        420 
SNGKGVSIDG AQLSFETGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGV VKSQQPVYLK 

       430        440        450        460        470        480 
GETVSNHDEL MSNFFAQPDA LAYGKTPEQL HSEKVPENLI PHKTFKGNRP SLSLLLPTLS 

       490        500        510        520        530        540 
AYEVGQLLSI YEHRIAVQGF IWGINSFDQW GVELGKSLAS QVRKQLHGTR MEGKPVEGFN 

       550        560 
HSTSSLLARY LAVKPSTPYD TTVLPKV 

« Hide

References

[1]"Cloning and characterization of an anaerobically induced cDNA encoding glucose-6-phosphate isomerase from maize."
Lal S.K., Sachs M.M.
Plant Physiol. 108:1295-1296(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. B73.
Tissue: Root.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17225 mRNA. Translation: AAA82734.1.
PIRT02094.
RefSeqNP_001105368.1. NM_001111898.1.
UniGeneZm.3318.

3D structure databases

ProteinModelPortalP49105.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP49105.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID542313.
KEGGzma:542313.

Organism-specific databases

GrameneP49105.
MaizeGDB13859.

Phylogenomic databases

HOGENOMHOG000125964.
KOK01810.

Enzyme and pathway databases

UniPathwayUPA00109; UER00181.

Family and domain databases

Gene3D1.10.1390.10. 1 hit.
HAMAPMF_00473. G6P_isomerase.
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...

Entry information

Entry nameG6PI_MAIZE
AccessionPrimary (citable) accession number: P49105
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways