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Q89A35 (G6PI_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 68. 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

Short name=GPI
EC=5.3.1.9
Alternative name(s):
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Gene names
Name:pgi
Ordered Locus Names:bbp_518
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00473.

Sequence similarities

Belongs to the GPI family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180612

Sites

Active site3551Proton donor By similarity
Active site3861 By similarity
Active site5141 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89A35 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: AAA1319D1434F007

FASTA55263,907
        10         20         30         40         50         60 
MKKINPNNTE SWKMLQNHFY EIKSFHIKEL FKKDKNRFKK FSLKFDNRIL VDYSKNRITS 

        70         80         90        100        110        120 
FTIKLLLKLA NEMDLNNSIK SMFSGKIINE TENRAVLHTA LRNRSNSSII HNGCNIMFDI 

       130        140        150        160        170        180 
NKVLEKMKHF SNLVINRKWL GYTGKYITDI VNIGIGGSDL GPKMVIKALN SYRNHLNIHF 

       190        200        210        220        230        240 
VSNVDGANIF NVLKKLNPES TLFIIVSKTF TTQETIVNAN TAKKWMLNAV NKNEFLDQHF 

       250        260        270        280        290        300 
IAVTTNAQEA MNFGIRYKNI FLFWDWVGGR FSLWSSVGLS IVLAVGFKNF EQLLDGAYMM 

       310        320        330        340        350        360 
DQHYLHTKFD NNIPVLLALI GVWYNNFFKS ETEAIFFYDW NMNYFSSFLQ QMNMESNGKN 

       370        380        390        400        410        420 
ICRSGEFVNW QTGPIIWGEP GTNGQHAFYQ LLHQGTKLIP SDFIISIIPK HPFKDHHKYL 

       430        440        450        460        470        480 
LSHFFAQTQA LAFGKFNQKC NVHINDKKTF DERLSSISFH KVCKGNQPSN SIVLDQLNPY 

       490        500        510        520        530        540 
NLGILIALYE HKVFTQGVIF NIFSFDQWGV ELGKLLAKEI FLNMNTTGSK NYEYDSSTNG 

       550 
LINFYKIHSN NT 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO27221.1.
RefSeqNP_778116.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89A35.
SMRQ89A35. Positions 7-550.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp518.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO27221; AAO27221; bbp_518.
GeneID1058454.
KEGGbab:bbp518.
PATRIC21245855. VBIBucAph80364_0513.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0166.
KOK01810.
OMANCHFVAN.
OrthoDBEOG64R61J.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-518-MONOMER.
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_BUCBP
AccessionPrimary (citable) accession number: Q89A35
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: June 11, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways