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Reviewed, UniProtKB/Swiss-Prot P83077 (G3P2_BACCE)

Last modified June 16, 2009. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 2
      Short name=GAPDH 2
    EC=1.2.1.12
Gene names
Name: gap2
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length14 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Miscellaneous

Under acid-stress, this protein is expressed at a higher level in wild-type B.cereus than in the acid-sensitive mutant strain NB1. Ref.1

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›14›14Glyceraldehyde-3-phosphate dehydrogenase 2
PRO_0000271248

Regions

Nucleotide binding10 – 112NAD By similarity UniProtKB P00361

Experimental info

Non-terminal residue141

Sequences

Sequence LengthMass (Da)Tools
P83077-1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 209872BB19F5E0C8

FASTA141,604
        10 
MKQGINGFAR RGRL 

« Hide

References

[1]"Acid stress in the food pathogen Bacillus cereus."
Browne N., Dowds B.C.A.
J. Appl. Microbiol. 92:404-414(2002) [PubMed: 11872115] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: NCIMB 11796 / DSM 626.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.12. 604.

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DH.
[Graphical view]
PROSITEPS00071. GAPDH. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P2_BACCE
AccessionPrimary (citable) accession number: P83077
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: October 1, 2001
Last modified: June 16, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents