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Reviewed, UniProtKB/Swiss-Prot P84998 (G3P1_KLUMA)

Last modified February 9, 2010. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 1
      Short name=GAPDH 1
    EC=1.2.1.12
Gene names
Name: GAP1
OrganismKluyveromyces marxianus (Yeast) (Candida kefyr)
Taxonomic identifier4911 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH. Ref.1

Pathway

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

Subunit structure

Homotetramer By similarity. UniProtKB P22513

Subcellular location

Cytoplasm By similarity UniProtKB P00359.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
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 functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-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 – 329329Glyceraldehyde-3-phosphate dehydrogenase 1
PRO_0000253990

Regions

Nucleotide binding11 – 122NAD By similarity UniProtKB P22513
Region148 – 1503Glyceraldehyde 3-phosphate binding By similarity UniProtKB P22513
Region208 – 2092Glyceraldehyde 3-phosphate binding By similarity UniProtKB P22513

Sites

Active site1491Nucleophile By similarity UniProtKB P22513
Binding site331NAD By similarity UniProtKB P22513
Binding site771NAD; via carbonyl oxygen By similarity UniProtKB P22513
Binding site1791Glyceraldehyde 3-phosphate By similarity UniProtKB P22513
Binding site2311Glyceraldehyde 3-phosphate By similarity UniProtKB P22513
Binding site3131NAD By similarity UniProtKB P22513
Site1761Activates thiol group during catalysis By similarity UniProtKB P22513

Amino acid modifications

Modified residue1481Phosphoserine By similarity UniProtKB P00359
Modified residue1771Phosphoserine By similarity UniProtKB P00359
Modified residue2001Phosphoserine By similarity UniProtKB P00359

Secondary structure

.................................................................. 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P84998-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 4C5C08D5C7858672

FASTA32935,253
        10         20         30         40         50         60 
MVSIAINGFG RIGRLVLRIA LERKNIDVVA INDPFISVDY AAYMFKYDST HGKYKGEVSH 

        70         80         90        100        110        120 
DGSNLIINGK KVAVFQEKDP ATLPWGKLGV DIAVDSTGVF KELDSAQKHI DAGAKKVVIT 

       130        140        150        160        170        180 
APSKTAPMFV VGVNEDKYNG EKIVSNASCT TNCLAPIAKI INDEFGIEEG LMTTVHSITA 

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

       250        260        270        280        290        300 
DLTVKLVKAA TYDEIKAAVK KVSEGKLKDV VGYTEDAVVS SDFLGDTHST IFDAAAGIQL 

       310        320 
SPKFVKLVAW YDNEYGYSTR VVDLVEHVA 

« 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], CATALYTIC ACTIVITY, PATHWAY.
Strain: ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665.
[2]"The crystal and solution structures of glyceraldehyde-3-phosphate dehydrogenase reveal different quaternary structures."
Ferreira-da-Silva F., Pereira P.J.B., Gales L., Roessle M., Svergun D.I., Moradas-Ferreira P., Damas A.M.
J. Biol. Chem. 281:33433-33440(2006) [PubMed: 16963457] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Strain: ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665.

Cross-references

Sequence databases

PIRS57279.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I5PX-ray2.30O/P1-329[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.12. 97088.

Family and domain databases

InterProIPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020832. GlycerAld_3-P_DH_cat_sub.
IPR020831. GlycerAld_3-P_DH_family.
IPR020828. GlycerAld_3-P_DH_NAD(P)_bd.
IPR000173. GlycerAld_3-P_DH_subfam.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[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.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P1_KLUMA
AccessionPrimary (citable) accession number: P84998
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: February 9, 2010
This is version 27 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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