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Reviewed, UniProtKB/Swiss-Prot Q01077 (G3P2_KLUMA)

Last modified November 25, 2008. Version 54. 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
OrganismKluyveromyces marxianus (Yeast) (Candida kefyr)
Taxonomic identifier4911 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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 By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords

   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase

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-KW

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Glyceraldehyde-3-phosphate dehydrogenase 2
PRO_0000145558

Regions

Nucleotide binding11 – 122NAD By similarity
Region148 – 1503Glyceraldehyde 3-phosphate binding By similarity
Region208 – 2092Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1491Nucleophile By similarity
Binding site331NAD By similarity
Binding site781NAD; via carbonyl oxygen By similarity
Binding site1791Glyceraldehyde 3-phosphate By similarity
Binding site2311Glyceraldehyde 3-phosphate By similarity
Binding site3131NAD By similarity
Site1761Activates thiol group during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01077-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: FEDB08479F4B5F09

FASTA33135,540
        10         20         30         40         50         60 
MVRIAINGFG RIGRLVLRIA LSRKNIEVVA INDPFITVDY AAYMFKYDST HGRFDGEVSH 

        70         80         90        100        110        120 
DGKSLIIDGK KVLVFQERDP ATLPWGAEKI DIAIDSTGIF KELDSAQKHI DAGAKKVVIT 

       130        140        150        160        170        180 
APSSTAPMFV VGVNEDKYAG QTIVSNASCT TNCLAPLAKI INNAFGIEEG LMTTVHSITA 

       190        200        210        220        230        240 
TQKTVDGPSH KDWRGGRTAS GNIIPSSTGA AKAVGKVLPE LQGKLTGMAF RVPTVDVSVV 

       250        260        270        280        290        300 
DLTVKLAKPA TYEEIKAVVK KASENELKGV MGYTEDAVVS SDFLGDTHSS IFDAAAGIQL 

       310        320        330 
SPQFVKLVSW YDNEFGYSTR VVDLVELVAK N 

« Hide

References

[1]"Characterization of the glyceraldehyde-3-phosphate dehydrogenase gene family from Kluyveromyces marxianus -- polymerase chain reaction-single-strand conformation polymorphism as a tool for the study of multigenic families."
Fernandes P.A., Sena-Esteves M., Moradas-Ferreira P.
Yeast 11:725-733(1995) [PubMed: 7668042] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665.

Cross-references

Sequence databases

S80241 Genomic DNA. Translation: AAB35209.1.
PIRS57280.

3D structure databases

SMRQ01077. Positions 1-329.
ModBaseSearch...

Family and domain databases

InterProIPR000173. GlycerAld_3-P_DHase.
IPR006424. Glyceraldehyde-3-P_DHase_1.
[Graphical view]
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P2_KLUMA
AccessionPrimary (citable) accession number: Q01077
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 25, 2008
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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