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P13376 (G6PIB_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 B

Short name=GPI B
EC=5.3.1.9
Alternative name(s):
Phosphoglucose isomerase B
Short name=PGI-B
Phosphohexose isomerase B
Short name=PHI-B
Gene names
Name:pgiB
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00473.

Sequence similarities

Belongs to the GPI family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glycolysis

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 – 445445Glucose-6-phosphate isomerase B HAMAP-Rule MF_00473
PRO_0000180592

Sites

Active site2851Proton donor By similarity
Active site3061 By similarity
Active site4201 By similarity

Secondary structure

.............................................................................. 445
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13376 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 078AD337669D1AE1

FASTA44550,141
        10         20         30         40         50         60 
MAISFDYSNA LPFMQENELD YLSEFVKAAH HMLHERKGPG SDFLGWVDWP IRYDKNEFSR 

        70         80         90        100        110        120 
IKQAAERIRN HSDALVVIGI GGSYLGARAA IEALSHTFHN QMNDTTQIYF AGQNISSTYI 

       130        140        150        160        170        180 
SHLLDVLEGK DLSINVISKS GTTTEPAIAF RIFRDYMEKK YGKEEARKRI YVTTDRTKGA 

       190        200        210        220        230        240 
LKKLADQEGY ETFVIPDNIG GRYSVLTAVG LLPIAVAGLN IDRMMEGAAS AYHKYNNPDL 

       250        260        270        280        290        300 
LTNESYQYAA VRNILYRKGK AIELLVNYEP SLHYVSEWWK QLFGESEGKD QKGLFPASVD 

       310        320        330        340        350        360 
FTTDLHSMGQ YVQEGRRNLI ETVLHVKKPQ IELTIQEDPE NIDGLNFLAG KTLDEVNKKA 

       370        380        390        400        410        420 
FQGTLLAHVD GGVPNLIVEL DEMNEYTFGE MVYFFEKACG ISGHLLGVNP FDQPGVEAYK 

       430        440 
KNMFALLGKP GFEDEKAALM KRLSK 

« Hide

References

[1]"Complete nucleotide sequences of two phosphoglucoisomerase isozymes from Bacillus stearothermophilus."
Tao W., Wang L., Shen R., Sheng Z.
Nucleic Acids Res. 17:10107-10108(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: T521.
[2]"The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin."
Sun Y.-J., Chou C.-C., Chen W.-S., Wu R.-T., Meng M., Hsiao C.-D.
Proc. Natl. Acad. Sci. U.S.A. 96:5412-5417(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16640 Genomic DNA. Translation: CAA34635.1.
PIRNUBSS. S06198.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0ZX-ray2.30A1-445[»]
1C7QX-ray2.30A1-445[»]
1C7RX-ray2.50A1-445[»]
2PGIX-ray2.30A1-445[»]
ProteinModelPortalP13376.
SMRP13376. Positions 2-443.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP13376.
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...

Other

EvolutionaryTraceP13376.

Entry information

Entry nameG6PIB_GEOSE
AccessionPrimary (citable) accession number: P13376
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: February 19, 2014
This is version 87 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways