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Q59088 (G6PI_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. 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:ACIAD0101
OrganismAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length557 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 – 557557Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180580

Sites

Active site3611Proton donor By similarity
Active site3921 By similarity
Active site5201 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59088 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D74AF214B139E4DC

FASTA55763,280
        10         20         30         40         50         60 
MNKNIEQFPR KTTLTPQQKL EQLMEQHKTV HLTELFDKEQ DRFAKYCVGC EDLVFDFSKQ 

        70         80         90        100        110        120 
RINQPILDAL VQLAESKQLN KWIDTLFSQN KINYTEQREA MHWALRLPAD NQVYPELAKQ 

       130        140        150        160        170        180 
VSDQLERMYQ LVNKIHEGQY RGATGEVIQD VVNIGVGGSD LGPLMVSHAL SDFKVKTAKP 

       190        200        210        220        230        240 
LNIRFVSTMD GSQLSDILHQ LRPETTLFIV SSKSFSTIDT LSNAHTARKW LEKALGRESS 

       250        260        270        280        290        300 
ILKSHFIGVS TKPDKMTEWG IHPDNQFLLW DWVGGRYSLW SCIGLPIALT IGVEGFKAFL 

       310        320        330        340        350        360 
AGAHGIDEHF RTTEFHQNIP VLMGLMGIWN TNYLNLKTHA VLPYDGRLKY FTSYLQQLEM 

       370        380        390        400        410        420 
ESNGKSTQRN GQKVENTTCP IVWGEVGPNA QHAFYQLLHQ GTQKVSCDFI APMHRYNANH 

       430        440        450        460        470        480 
FTYVENADAL IDQHLLALSN CLAQSRLLAF GNDALKVDQR EQLPAYKQYE GNQPSTTMLL 

       490        500        510        520        530        540 
KELSPRTMGK LIALYEHKVF VQSVIWDINP FDQWGVEKGK EIANDLLPIL NGESSDLSHL 

       550 
DDSTQGLIQF LLGKSNG 

« Hide

References

« Hide 'large scale' references
[1]Stark M., Kaplan N., Ron E.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33305 / BD413 / ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89900 Genomic DNA. Translation: CAA61993.1.
CR543861 Genomic DNA. Translation: CAG67079.1.
PIRS58164.
RefSeqYP_044901.1. NC_005966.1.

3D structure databases

ProteinModelPortalQ59088.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING62977.ACIAD0101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG67079; CAG67079; ACIAD0101.
GeneID2879592.
KEGGaci:ACIAD0101.
PATRIC20738182. VBIAciSp98416_0088.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261370.
KOK01810.
OMACGNELDN.
OrthoDBEOG64R61J.

Enzyme and pathway databases

BioCycASP62977:GJVV-99-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_ACIAD
AccessionPrimary (citable) accession number: Q59088
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 84 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