Skip Header

Contribute Send feedback
Read comments (?) or add your own

O27090 (G3P_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 92. 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:MTH_1009
OrganismMethanobacterium thermoautotrophicum (strain Delta H)
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length337 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 – 337337Glyceraldehyde-3-phosphate dehydrogenase HAMAP MF_00559
PRO_0000145726

Regions

Nucleotide binding11 – 122NAD By similarity
Region139 – 1413Glyceraldehyde 3-phosphate binding By similarity
Region194 – 1952Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1401Nucleophile By similarity
Binding site1101NAD; via amide nitrogen By similarity
Binding site1681NAD By similarity
Binding site3011NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
O27090 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 730FEDB11CF9BAA3

FASTA33736,836
        10         20         30         40         50         60 
MISVAINGYG TIGKRVADAV AAQDDMKVAG VSKTKPDFEA RVAIEKGYDL YVSIPEREKL 

        70         80         90        100        110        120 
FGEAGIPVSG TVEDMLEEAD IVVDATPEGI GAKNLEMYRE KGIKAIFQGG EKHDAIGLSF 

       130        140        150        160        170        180 
NSFANYDESL GADYTRVVSC NTTGLCRTLK PIDDLCGIKK VRAVMVRRGA DPVQVKKGPI 

       190        200        210        220        230        240 
NAIVPNPPTV PSHHGPDLKT VMKGVNIHTV ALLVPTTLMH QHNIMVELED PVEADEIKAR 

       250        260        270        280        290        300 
LDETTRVMLV RASEGLASTA EIMEYAKELG RSRNDLFEIP VWEESINVVD GELFYMQAVH 

       310        320        330 
QESDAVPESV DAIRALLELE EDNMKSIMKT NRAMGIL 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Delta H.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB85505.1.
PIRE69001.
RefSeqNP_276144.1. NC_000916.1.

3D structure databases

ProteinModelPortalO27090.
SMRO27090. Positions 1-337.
ModBaseSearch...

Protein-protein interaction databases

STRINGO27090.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1471417.
GenomeReviewsGene locus MTH_1009 in contig AE000666_GR.
KEGGmth:MTH1009.
NMPDRfig|187420.1.peg.999.

Phylogenomic databases

eggNOGarNOG04694.
HOGENOMHBG392099.
OMAVPSHHGP.
ProtClustDBPRK04207.

Enzyme and pathway databases

BioCycMTHE187420:MTH1009-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_METTH
AccessionPrimary (citable) accession number: O27090
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: November 16, 2011
This is version 92 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