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Q47IJ3 (G6PI_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 57. 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:Daro_0581
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length526 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 – 526526Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180636

Sites

Active site3431Proton donor By similarity
Active site3741 By similarity
Active site4941 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47IJ3 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 9C0F962811D2D069

FASTA52657,499
        10         20         30         40         50         60 
MNPIDSPAWR ALAAHAEAIR PLHLRDLFAT DPQRFELFSL HHDGLLLDYS KQRVSVETMA 

        70         80         90        100        110        120 
LLRAYAETAD VTGWRRRMLD GESINHTEGR AVRHMSLRAG DQAPAEVRAA LARQQAFCES 

       130        140        150        160        170        180 
IHNGVWRGFS GERITDVVNI GIGGSDLGPR MAALALSARQ QPDIAVHFIA NVDSADIAPL 

       190        200        210        220        230        240 
LASLNPRTTL FIVASKTFTT LETLTNARTA RDWLLATAGQ ESAIARHFVA ISTNLELTKQ 

       250        260        270        280        290        300 
FGIADDNVFE FWDWVGGRFS IWSAIGLSLA LAIGWKNFEQ LQAGARAMDR HFIDTPADEN 

       310        320        330        340        350        360 
LPLTLALLSL WNTNFLGAST EAMLPYSQSL HLFPAYLQQL EMESNGKQID RDGKPLNIAT 

       370        380        390        400        410        420 
SPVIWGESGT NGQHSFYQLF HQGGHLIPAD FVALREADFP LPGHHASLLA NCLAQSAALA 

       430        440        450        460        470        480 
FGQTAEEVRA AGIPEALIPY KVFPGNQPSN TLLLPSLDPY TLGQLLALFE HKVFCLGVLW 

       490        500        510        520 
NLNAFDQWGV ELGKQLAGQL TPLIEGNGDL SAFDSSTRGL ITALKG 

« Hide

References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ45338.1.
RefSeqYP_283808.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ47IJ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_0581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ45338; AAZ45338; Daro_0581.
GeneID3568807.
KEGGdar:Daro_0581.
PATRIC21599776. VBIDecAro89105_0588.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261370.
KOK01810.
OMANCHFVAN.
OrthoDBEOG64R61J.

Enzyme and pathway databases

BioCycDARO159087:GI5B-598-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_DECAR
AccessionPrimary (citable) accession number: Q47IJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: September 13, 2005
Last modified: June 11, 2014
This is version 57 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