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Q72YI4 (G6PI_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. 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:BCE_5037
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length450 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
   PTMPhosphoprotein
   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 – 450450Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180585

Sites

Active site2911Proton donor By similarity
Active site3121 By similarity
Active site4261 By similarity

Amino acid modifications

Modified residue391Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q72YI4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A94BA63F9048F215

FASTA45050,322
        10         20         30         40         50         60 
MSTHVTFDYS KALSFIGEHE ITYLRDAVKV THHAIHEKTG AGNDFLGWVD LPLQYDKEEF 

        70         80         90        100        110        120 
ARIQKCAEKI KNDSDILLVV GIGGSYLGAR AAIEMLNHSF YNTLSKEQRK TPQVLFVGQN 

       130        140        150        160        170        180 
ISSTYMKDLM DVLEGKDFSI NVISKSGTTT EPALAFRIFR KLLEEKYGKE EARKRIYATT 

       190        200        210        220        230        240 
DKARGALKTL ADNEGYETFV IPDDVGGRFS VLTPVGLLPI AVSGLNIEEM MKGAAAGHDD 

       250        260        270        280        290        300 
FGTSELEENP AYQYAVVRNA LYNKGKTIEM LVNYEPALQY FAEWWKQLFG ESEGKDQKGI 

       310        320        330        340        350        360 
FPSSANFSTD LHSLGQYVQE GRRDLFETVL KVGKPTHELT IESEENDLDG LNYLAGETVD 

       370        380        390        400        410        420 
FVNTKAYEGT LLAHSDGGVP NLIVNIPELN EYTFGYLVYF FEKACAMSGY LLGVNPFDQP 

       430        440        450 
GVEAYKKNMF ALLGKPGFEE LKAELEERLK 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS43938.1.
RefSeqNP_981330.1. NC_003909.8.

3D structure databases

ProteinModelPortalQ72YI4.
SMRQ72YI4. Positions 5-449.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING222523.BCE_5037.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS43938; AAS43938; BCE_5037.
GeneID2747544.
KEGGbca:BCE_5037.
PATRIC18858704. VBIBacCer118379_4822.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000100403.
KOK01810.
OMAGVESYKR.
OrthoDBEOG64R61J.

Enzyme and pathway databases

UniPathwayUPA00109; UER00181.

Family and domain databases

HAMAPMF_00473. G6P_isomerase.
InterProIPR001672. G6P_Isomerase.
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_BACC1
AccessionPrimary (citable) accession number: Q72YI4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 66 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