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P17721 (G3P_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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=1.2.1.12
Gene names
Name:gap
Ordered Locus Names:TM_0688
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.

Pathway

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

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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+) (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 333332Glyceraldehyde-3-phosphate dehydrogenase
PRO_0000145711

Regions

Nucleotide binding11 – 122NAD
Region151 – 1533Glyceraldehyde 3-phosphate binding By similarity
Region210 – 2112Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1521Nucleophile
Binding site351NAD
Binding site1211NAD
Binding site1821Glyceraldehyde 3-phosphate By similarity
Binding site1831NAD
Binding site1971Glyceraldehyde 3-phosphate By similarity
Binding site2331Glyceraldehyde 3-phosphate By similarity
Binding site3151NAD
Site1791Activates thiol group during catalysis By similarity

Secondary structure

1 ........................................................................... 333
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17721 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 12B77104AB5E1CD0

FASTA33336,425
        10         20         30         40         50         60 
MARVAINGFG RIGRLVYRII YERKNPDIEV VAINDLTDTK TLAHLLKYDS VHKKFPGKVE 

        70         80         90        100        110        120 
YTENSLIVDG KEIKVFAEPD PSKLPWKDLG VDFVIESTGV FRNREKAELH LQAGAKKVII 

       130        140        150        160        170        180 
TAPAKGEDIT VVIGCNEDQL KPEHTIISCA SCTTNSIAPI VKVLHEKFGI VSGMLTTVHS 

       190        200        210        220        230        240 
YTNDQRVLDL PHKDLRRARA AAVNIIPTTT GAAKAVALVV PEVKGKLDGM AIRVPTPDGS 

       250        260        270        280        290        300 
ITDLTVLVEK ETTVEEVNAV MKEATEGRLK GIIGYNDEPI VSSDIIGTTF SGIFDATITN 

       310        320        330 
VIGGKLVKVA SWYDNEYGYS NRVVDTLELL LKM

« Hide

References

« Hide 'large scale' references
[1]"Functional expression of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima in Escherichia coli. Authenticity and kinetic properties of the recombinant enzyme."
Tomschy A., Glockhuber R., Jaenicke R.
Eur. J. Biochem. 214:43-50(1993) [PubMed: 8508805] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"Complete amino-acid sequence of glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima."
Schultes V., Deutzmann R., Jaenicke R.
Eur. J. Biochem. 192:25-31(1990) [PubMed: 2401296] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-333.
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[4]"The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5-A resolution."
Korndoerfer I., Steipe B., Huber R., Tomschy A., Jaenicke R.
J. Mol. Biol. 246:511-521(1995) [PubMed: 7877172] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X72629 Genomic DNA. Translation: CAA51205.1.
AE000512 Genomic DNA. Translation: AAD35770.1.
PIRDEHGGT. S33325.
RefSeqNP_228497.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HDGX-ray2.50O/Q2-333[»]
ProteinModelPortalP17721.
SMRP17721. Positions 2-333.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID898355.
GenomeReviewsGene locus TM_0688 in contig AE000512_GR.
KEGGtma:TM0688.
NMPDRfig|243274.1.peg.681.
PATRIC23936294. VBITheMar51294_0700.
TIGRTM_0688.

Phylogenomic databases

HOGENOMHBG571736.
OMADATFVYG.
PhylomeDBP17721.
ProtClustDBCLSK875298.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-401.
TMAR243274:TM_0688-MONOMER.

Family and domain databases

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.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00134.
PANTHERPTHR10836. GAP_DH. 1 hit.
PfamPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000149. GAP_DH. 1 hit.
PRINTSPR00078. G3PDHDRGNASE.
SMARTSM00846. Gp_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01534. GAPDH-I. 1 hit.
PROSITEPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG3P_THEMA
AccessionPrimary (citable) accession number: P17721
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 108 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents