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A5ULT9 (G3P_METS3) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 35. 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:Msm_0962
OrganismMethanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861) [Complete proteome] [HAMAP]
Taxonomic identifier420247 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanobrevibacter

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
   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 – 338338Glyceraldehyde-3-phosphate dehydrogenase HAMAP MF_00559
PRO_0000300971

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
A5ULT9 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: C534794D04B1BA6E

FASTA33837,130
        10         20         30         40         50         60 
MKSVAINGYG TIGKRVADAV AAQDDMKVIG VSKTRPNYES RTAVEEKGYD LYIGIPERAD 

        70         80         90        100        110        120 
QFKEAGIEIA GTVEDMIQEA DVVVDCTPGT IGPQNLEMYK KAGVKAIYQG GEDHELTGLS 

       130        140        150        160        170        180 
FNAISNYDDS YGKDYTRVVS CNTTGLTRTL STIDPIADIK KVRAVMVRRG SDPSEVKKGP 

       190        200        210        220        230        240 
INSIVPNPPK VPSHHGPDVK TVMEGIDVTT MALLVPTTLM HQHNIMVEIN NEVETQEIID 

       250        260        270        280        290        300 
ALEKRSRVLV VDASEGLGST AELMEYAKEL GRNRNDLYEI PVWRESINVV GNELYYMQAV 

       310        320        330 
HQESDVVPEN IDAIRALLEM ESDNEKSIAK TNKAMGIL 

« Hide

References

[1]"Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut."
Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007) [PubMed: 17563350] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PS / ATCC 35061 / DSM 861.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000678 Genomic DNA. Translation: ABQ87167.1.
RefSeqYP_001273535.1. NC_009515.1.

3D structure databases

ProteinModelPortalA5ULT9.
SMRA5ULT9. Positions 1-338.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5ULT9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5217242.
GenomeReviewsGene locus Msm_0962 in contig CP000678_GR.
KEGGmsi:Msm_0962.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04694.
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_METS3
AccessionPrimary (citable) accession number: A5ULT9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 10, 2007
Last modified: November 16, 2011
This is version 35 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