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P84999 (G3P3_KLUMA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glyceraldehyde-3-phosphate dehydrogenase 3
Short name=GAPDH 3
EC=1.2.1.12
Gene names
Name:GAP3
OrganismKluyveromyces marxianus (Yeast) (Candida kefyr)
Taxonomic identifier4911 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length331 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
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

NADP binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Glyceraldehyde-3-phosphate dehydrogenase 3
PRO_0000253991

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

Sequences

Sequence LengthMass (Da)Tools
P84999 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 5E09084264795F01

FASTA33135,524
        10         20         30         40         50         60 
MVRIAINGFG RIGRLVLRIA LSRKNIEVVA INDPFITVDY AAYMFKYDST HGRFDGEVSH 

        70         80         90        100        110        120 
DGKALIIDGK 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], CATALYTIC ACTIVITY, PATHWAY.
Strain: ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665.

Cross-references

Sequence databases

PIRS57281.

3D structure databases

ProteinModelPortalP84999.
SMRP84999. Positions 1-329.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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 nameG3P3_KLUMA
AccessionPrimary (citable) accession number: P84999
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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