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P19315 (G3P_METFO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMethanobacterium formicicum
Taxonomic identifier2162 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanobacterium

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP MF_00559

Subcellular location

Cytoplasm By similarity HAMAP MF_00559.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
NADP
   Molecular functionOxidoreductase
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(P)+) (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Glyceraldehyde-3-phosphate dehydrogenase HAMAP MF_00559
PRO_0000145721

Regions

Nucleotide binding11 – 122NAD By similarity
Region140 – 1423Glyceraldehyde 3-phosphate binding By similarity
Region195 – 1962Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1411Nucleophile By similarity
Binding site1111NAD; via amide nitrogen By similarity
Binding site1691NAD By similarity
Binding site3021NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
P19315 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 8F96B2DC638A1CFE

FASTA33837,220
        10         20         30         40         50         60 
MKSVGINGYG TIGKRVADAV SAQDDMKIVG VTKRSPDFEA RMAVEKGYDL YISAPERENS 

        70         80         90        100        110        120 
FEEAGIKVTG TAEELFEKLD IVVDCTPEGI GAKNKEGTYE KMGLKATFQG GEKHDQIGLS 

       130        140        150        160        170        180 
FNSFSNYKDV IGKDYARVVS CNTTGLCRTL NPINDLCGIK KVRAVMVRRG ADPSQVKKGP 

       190        200        210        220        230        240 
INAIVPNPPT VPSHHGPDVQ TVMYDLNITT MALLVPTTLM HQHNLMVELE SSVSIDDIKD 

       250        260        270        280        290        300 
KLNETPRVLL LKAKEGLGST AEFMEYAKEL GRSRNDLFEI GVWEESLNIV DGELYYMQAI 

       310        320        330 
HQESDVVPEN VDAIRAMLEM EDNPSKSIEK TNKAMGIL 

« Hide

References

[1]"Nucleotide sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from the mesophilic methanogenic archaebacteria Methanobacterium bryantii and Methanobacterium formicicum. Comparison with the respective gene structure of the closely related extreme thermophile Methanothermus fervidus."
Fabry S., Lang J., Niermann T., Vingron M., Hensel R.
Eur. J. Biochem. 179:405-413(1989) [PubMed: 2492940] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14632 Genomic DNA. Translation: CAB37402.1.
PIRS02803.

3D structure databases

ProteinModelPortalP19315.
SMRP19315. Positions 1-338.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00559. G3P_dehdrog_arch.
[Tree]
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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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...

Entry information

Entry nameG3P_METFO
AccessionPrimary (citable) accession number: P19315
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 28, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families