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P26517 (G3PC1_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glyceraldehyde-3-phosphate dehydrogenase 1, cytosolic
EC=1.2.1.12
Gene names
Name:GAPC
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism By similarity.

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.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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

Chain1 – 337337Glyceraldehyde-3-phosphate dehydrogenase 1, cytosolic
PRO_0000145602

Regions

Nucleotide binding13 – 142NAD By similarity
Region153 – 1553Glyceraldehyde 3-phosphate binding By similarity
Region213 – 2142Glyceraldehyde 3-phosphate binding By similarity

Sites

Active site1541Nucleophile By similarity
Binding site351NAD By similarity
Binding site821NAD; via carbonyl oxygen By similarity
Binding site1841Glyceraldehyde 3-phosphate By similarity
Binding site2361Glyceraldehyde 3-phosphate By similarity
Binding site3181NAD By similarity
Site1811Activates thiol group during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P26517 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 8150135A6FDA6726

FASTA33736,514
        10         20         30         40         50         60 
MGKIKIGING FGRIGRLVAR VALQSDDVEL VAVNDPFITT EYMTYMFKYD TVHGHWKHSD 

        70         80         90        100        110        120 
IKLKDDKTLL FGEKPVTVFG VRNPEEIPWG EAGADYVVES TGVFTDKDKA AAHLKGGAKK 

       130        140        150        160        170        180 
VVISAPSKDA PMFVVGVNED KYTSDVNIVS NASCTTNCLA PLAKVINDNF GIIEGLMTTV 

       190        200        210        220        230        240 
HAITATQKTV DGPSSKDWRG GRAASFNIIP SSTGAAKAVG KVLPELNGKL TGMSFRVPTV 

       250        260        270        280        290        300 
DVSVVDLTVR TEKAASYDDI KKAIKAASEG KLKGIMGYVE EDLVSTDFVG DSRSSIFDAK 

       310        320        330 
AGIALNDHFV KLVSWYDNEW GYSNRVVDLI RHMAKTQ

« Hide

References

[1]"Molecular evidence for pre-Cretaceous angiosperm origins."
Martin W., Gierl A., Saedler H.
Nature 339:46-48(1989)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X60343 mRNA. Translation: CAA42901.1.
PIRDEBHG. S18482.
UniGeneHv.22848.

3D structure databases

ProteinModelPortalP26517.
SMRP26517. Positions 3-337.
ModBaseSearch...

Proteomic databases

PRIDEP26517.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP26517.

Enzyme and pathway databases

UniPathwayUPA00109; UER00184.

Gene expression databases

GenevestigatorP26517.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
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]
PANTHERPTHR10836. PTHR10836. 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 nameG3PC1_HORVU
AccessionPrimary (citable) accession number: P26517
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: March 6, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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