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Q21M11 (G6PI_SACD2) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. 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:Sde_1006
OrganismSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]
Taxonomic identifier203122 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus

Protein attributes

Sequence length547 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 – 547547Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000252644

Sites

Active site3511Proton donor By similarity
Active site3821 By similarity
Active site5101 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q21M11 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: E2F00A5C6917DE76

FASTA54760,371
        10         20         30         40         50         60 
MQAKTLADLY SDWDKVQAHA QAWQKRTLKD AFDADRNRAA RYSVGAAGLE LDFSKNHIDD 

        70         80         90        100        110        120 
ETLQLLMGVA DQANLKAAIK KLLRGDHVNN TEDRPALHSA LRFQGKPQTA EHQEVKATLD 

       130        140        150        160        170        180 
KMAKLIKSVH SGEWKGYKGE KITDVVNIGI GGSDLGPRMI TKALTPFHTG DVKVHFVANI 

       190        200        210        220        230        240 
DGAEIHDLTR GLNPSTTLFL VASKSFSTLE TLENSLTARK WMLDNGCAQD QLAKHFVAIS 

       250        260        270        280        290        300 
SKVEKAVEFG IAAENVYPIW DWVGGRYSLW SAIGMPIAFA IGMDNFNKLR AGAAAMDDHF 

       310        320        330        340        350        360 
AEAPLERNIP ALMGLLMFWY SSCLGTDTQA ILPYAYHLQL LPAYLQQLEM ESNGKSVTKS 

       370        380        390        400        410        420 
GERVDYQTGS IVWGTEGTNG QHSFHQLLHQ GTTMVPIDFI ATLQAHHPLD HQHKFLFANC 

       430        440        450        460        470        480 
VAQSQALMTG RDQATSEAEM RAQGMSDEQI AELAPHKVHP GNRPSNTILM DKLTPETLGA 

       490        500        510        520        530        540 
LIAAYEHKVY TLGVLWNINS FDQWGVELGK LLGTHVATAI DTTDIPSDWD SSTQTLVKKF 


TEANKNL 

« Hide

References

[1]"Complete genome sequence of the complex carbohydrate-degrading marine bacterium, Saccharophagus degradans strain 2-40 T."
Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., Richardson P.M., Borovok I., Hutcheson S.
PLoS Genet. 4:E1000087-E1000087(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2-40 / ATCC 43961 / DSM 17024.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000282 Genomic DNA. Translation: ABD80268.1.
RefSeqYP_526480.1. NC_007912.1.

3D structure databases

ProteinModelPortalQ21M11.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203122.Sde_1006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD80268; ABD80268; Sde_1006.
GeneID3965131.
KEGGsde:Sde_1006.
PATRIC23400803. VBISacDeg56404_1100.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261370.
KOK01810.
OMAMIALTHY.
OrthoDBEOG64R61J.

Enzyme and pathway databases

BioCycSDEG203122:GI2M-1017-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_SACD2
AccessionPrimary (citable) accession number: Q21M11
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: April 18, 2006
Last modified: June 11, 2014
This is version 54 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