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A2BLC6 (G3P_HYPBU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 41. 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
Ordered Locus Names:Hbut_0939
OrganismHyperthermus butylicus (strain DSM 5456 / JCM 9403)
Taxonomic identifier415426 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus

Protein attributes

Sequence length343 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
Reference 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 – 343343Glyceraldehyde-3-phosphate dehydrogenase HAMAP MF_00559
PRO_0000300970

Regions

Nucleotide binding13 – 142NAD 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
A2BLC6 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: DFAFF32D589DCBFF

FASTA34337,560
        10         20         30         40         50         60 
MARVRVGVNG FGTIGKRVAE AIMLQPDMEL VGVTKTKPDY TAKYAVSRGI PVYVPKESLE 

        70         80         90        100        110        120 
EFQAKGIEPA GTIEELLEKV DVIVDATPGG TGRKYKPLYE KAGVKMIFQG GEKADIAELS 

       130        140        150        160        170        180 
FSTLCNYEQA LGKTSLRVVS CNTTGLLRAI CSISRLAPVR RVRATIVRRA ADPKEIKRGP 

       190        200        210        220        230        240 
VNAIKPDPVK TPSHHALDVK TVLPDLDIVT MAVVVPTTLM HVHIVYAELE KPVTREDVVA 

       250        260        270        280        290        300 
TFESTPRILL ADASYGLAST AELVEYARDL GRKRYDIPEL IVWLDSIAVN GVEVMWMQAV 

       310        320        330        340 
HQEAIVVPEN IDAIRAVAEL AKTAEETIRI TDERLGLLKG RIP 

« Hide

References

[1]"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
Archaea 2:127-135(2007) [PubMed: 17350933] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5456 / JCM 9403.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000493 Genomic DNA. Translation: ABM80787.1.
RefSeqYP_001013132.1. NC_008818.1.

3D structure databases

ProteinModelPortalA2BLC6.
SMRA2BLC6. Positions 3-339.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2BLC6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4782951.
GenomeReviewsGene locus Hbut_0939 in contig CP000493_GR.
KEGGhbu:Hbut_0939.

Phylogenomic databases

eggNOGarNOG04694.
HOGENOMHBG392099.
OMAVPSHHGP.
ProtClustDBPRK04207.

Enzyme and pathway databases

BioCycHBUT415426:HBUT_0939-MONOMER.

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_HYPBU
AccessionPrimary (citable) accession number: A2BLC6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 20, 2007
Last modified: November 16, 2011
This is version 41 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