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B1YD06 (G3P_THENV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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

Short name=GAPDH
EC=1.2.1.59
Alternative name(s):
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Gene names
Name:gap
Ordered Locus Names:Tneu_0730
OrganismThermoproteus neutrophilus (strain DSM 2338 / JCM 9278 / V24Sta) [Complete proteome] [HAMAP]
Taxonomic identifier444157 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeThermoproteus

Protein attributes

Sequence length344 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
   Technical termComplete proteome
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 – 344344Glyceraldehyde-3-phosphate dehydrogenase HAMAP MF_00559
PRO_1000129247

Regions

Nucleotide binding11 – 122NAD By similarity
Region139 – 1413Glyceraldehyde 3-phosphate binding By similarity
Region195 – 1962Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1401Nucleophile By similarity
Binding site1101NAD; via amide nitrogen By similarity
Binding site1691NAD By similarity
Binding site3021NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B1YD06 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 2378B8F775D14492

FASTA34437,902
        10         20         30         40         50         60 
MIRVGIVGYG TIGKRIADAV VAQDDMKIAG VLKVSPDYEA KVAVSRGFPV YTLPDRVEKF 

        70         80         90        100        110        120 
KKAGIEPAGT IEDLIKASDV VVDASPEDVG RENKEKYYQR YDKPVIFQGG EEADVAEVSF 

       130        140        150        160        170        180 
NALANYEEAR GKRYVRVVSC NTTGITRVLT SLTLNGVGIK KARIFIARRG ADPKEHKKGP 

       190        200        210        220        230        240 
INDVVPNPAT VPSHHGPDVQ TILRNVDIVT MAVAVPVTIM HMHMAYIELD SAYPKDQVIE 

       250        260        270        280        290        300 
AFAKTPRIFL ADVGAGFQSL AQVIEYARDL GRPRGDFPEV AVFRDSVTTH GNELYLMYGV 

       310        320        330        340 
HQESIVVPEN IDAIRSIFGT LPKWRSIEKT DKSLKLTTEG KRYG 

« Hide

References

[1]"Complete sequence of Thermoproteus neutrophilus V24Sta."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2338 / JCM 9278 / V24Sta.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001014 Genomic DNA. Translation: ACB39669.1.
RefSeqYP_001794115.1. NC_010525.1.

3D structure databases

ProteinModelPortalB1YD06.
SMRB1YD06. Positions 1-337.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1YD06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6165513.
GenomeReviewsGene locus Tneu_0730 in contig CP001014_GR.
KEGGtne:Tneu_0730.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG392099.
OMAVPSHHGP.
ProtClustDBPRK04207.

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.
KOK00150.
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_THENV
AccessionPrimary (citable) accession number: B1YD06
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 30 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