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P10618 (G3P_METFE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 106. 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:
Glyceraldehyde-3-phosphate dehydrogenase

Short name=GAPDH
EC=1.2.1.59
Alternative name(s):
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Gene names
Name:gap
OrganismMethanothermus fervidus
Taxonomic identifier2180 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanothermaceaeMethanothermus

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exhibits a dual-cofactor specificity, with a marked preference for NADP+ over NAD+. HAMAP-Rule MF_00559

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H. HAMAP-Rule MF_00559

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. HAMAP-Rule MF_00559

Subunit structure

Homotetramer. Ref.2

Subcellular location

Cytoplasm HAMAP-Rule MF_00559.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Glyceraldehyde-3-phosphate dehydrogenase HAMAP-Rule MF_00559
PRO_0000145722

Regions

Nucleotide binding11 – 122NADP HAMAP-Rule MF_00559
Nucleotide binding34 – 352NADP HAMAP-Rule MF_00559
Region139 – 1413Glyceraldehyde 3-phosphate binding By similarity
Region194 – 1952Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1401Nucleophile By similarity
Binding site1101NADP; via amide nitrogen
Binding site1711NADP
Binding site3001NADP; via carbonyl oxygen By similarity

Secondary structure

.............................................................. 337
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10618 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: D83CBA88AAE5B0B8

FASTA33737,408
        10         20         30         40         50         60 
MKAVAINGYG TVGKRVADAI AQQDDMKVIG VSKTRPDFEA RMALKKGYDL YVAIPERVKL 

        70         80         90        100        110        120 
FEKAGIEVAG TVDDMLDEAD IVIDCTPEGI GAKNLKMYKE KGIKAIFQGG EKHEDIGLSF 

       130        140        150        160        170        180 
NSLSNYEESY GKDYTRVVSC NTTGLCRTLK PLHDSFGIKK VRAVIVRRGA DPAQVSKGPI 

       190        200        210        220        230        240 
NAIIPNPPKL PSHHGPDVKT VLDINIDTMA VIVPTTLMHQ HNVMVEVEET PTVDDIIDVF 

       250        260        270        280        290        300 
EDTPRVILIS AEDGLTSTAE IMEYAKELGR SRNDLFEIPV WRESITVVDN EIYYMQAVHQ 

       310        320        330 
ESDIVPENVD AVRAILEMEE DKYKSINKTN KAMNILQ 

« Hide

References

[1]"Primary structure of glyceraldehyde-3-phosphate dehydrogenase deduced from the nucleotide sequence of the thermophilic archaebacterium Methanothermus fervidus."
Fabry S., Hensel R.
Gene 64:189-197(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The crystal structure of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus in the presence of NADP(+) at 2.1 A resolution."
Charron C., Talfournier F., Isupov M.N., Littlechild J.A., Branlant G., Vitoux B., Aubry A.
J. Mol. Biol. 297:481-500(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19980 Genomic DNA. Translation: AAA88227.1.
PIRJT0286.
RefSeqYP_004003841.1. NC_014658.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CF2X-ray2.10O/P/Q/R1-337[»]
ProteinModelPortalP10618.
SMRP10618. Positions 1-336.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9961991.
KEGGmfv:Mfer_0276.

Phylogenomic databases

KOK00150.

Enzyme and pathway databases

SABIO-RKP10618.
UniPathwayUPA00109; UER00184.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00559. G3P_dehdrog_arch.
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.
IPR006436. Glyceraldehyde-3-P_DH_2_arc.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01546. GAPDH-II_archae. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10618.

Entry information

Entry nameG3P_METFE
AccessionPrimary (citable) accession number: P10618
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: February 19, 2014
This is version 106 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