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Reviewed, UniProtKB/Swiss-Prot O16027 (G3P1_GLORO)

Last modified February 9, 2010. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 1
      Short name=GAPDH-1
    EC=1.2.1.12
Gene names
Name: GPD-1
OrganismGlobodera rostochiensis (Golden nematode worm)
Taxonomic identifier31243 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Nematoda › Chromadorea › Tylenchida › Tylenchina › Tylenchoidea › Heteroderidae › Heteroderinae › Globodera

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Protein attributes

Sequence length324 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level.

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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 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›324›324Glyceraldehyde-3-phosphate dehydrogenase 1
PRO_0000145516

Regions

Nucleotide binding13 – 142NAD By similarity
Region157 – 1593Glyceraldehyde 3-phosphate binding By similarity
Region217 – 2182Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1581Nucleophile By similarity
Binding site351NAD By similarity
Binding site851NAD; via carbonyl oxygen By similarity
Binding site1881Glyceraldehyde 3-phosphate By similarity
Binding site2401Glyceraldehyde 3-phosphate By similarity
Binding site3221NAD By similarity

Experimental info

Non-terminal residue3241

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Sequences

Sequence LengthMass (Da)Tools
O16027-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 1815C606CBBE1039

FASTA32434,580
        10         20         30         40         50         60 
MVKPKVGING FGRIGRLALR AAVEKDTVQV VAINDPFIEL DYMVYMFNYD STHGRFNGKI 

        70         80         90        100        110        120 
STSAGNLVVE KEGKATHTIK VFNLKDPAEI KWAEVGAEYV IESTGVFTTI EKASAHLKGG 

       130        140        150        160        170        180 
AKKVVISAPS ADAPMYVMGV NEDKYDPAKD NVISNASCTT NCLAPLAKVI NDEFGIIEGL 

       190        200        210        220        230        240 
MTTVHAVTAT QKTVDGPNGK QWRDGRGAAQ NIIPASTGAA KAVGKVIPEL NGKLTGMAFR 

       250        260        270        280        290        300 
VPTPNVSVVD LTARLEKPAS LDAIKAAVKK AAEGNLKGIL GYTEDQVVST DFLGDSRSSI 

       310        320 
FDAGACISLN PHFVKLVSWY DNEF

« Hide

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References

[1]"Cloning of a trans-spliced glyceraldehyde-3-phosphate-dehydrogenase gene from the potato cyst nematode Globodera rostochiensis and expression of its putative promoter region in Caenorhabditis elegans."
Qin L., Smant G., Stokkermans J.P.W.G., Bakker J., Schots A., Helder J.
Mol. Biochem. Parasitol. 96:59-67(1998) [PubMed: 9851607] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Ro1 / Mierenbos.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF004522 mRNA. Translation: AAC79129.1.

3D structure databases

SMRO16027. Positions 3-324.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.12. 288734.

Family and domain databases

InterProIPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020832. GlycerAld_3-P_DH_cat_sub.
IPR020831. GlycerAld_3-P_DH_family.
IPR020828. GlycerAld_3-P_DH_NAD(P)_bd.
IPR000173. GlycerAld_3-P_DH_subfam.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
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...

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Entry information

Entry nameG3P1_GLORO
AccessionPrimary (citable) accession number: O16027
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: February 9, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents