Glyceraldehyde 3-phosphate dehydrogenase

Glyceraldehyde 3-phosphate dehydrogenase (abbreviated GAPDH) (EC 1.2.1.12) is an enzyme of about 37kDa that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. In addition to this long established metabolic function, GAPDH has recently been implicated in several non-metabolic processes, including transcription activation, initiation of apoptosis, ER to Golgi vesicle shuttling, and fast axonal, or axoplasmic transport. In sperm, a testis-specific isoenzyme GAPDHS is expressed.

GAPDH
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGAPDH, GAPD, G3PD, HEL-S-162eP, glyceraldehyde-3-phosphate dehydrogenase
External IDsOMIM: 138400 MGI: 5434255 HomoloGene: 107053 GeneCards: GAPDH
Orthologs
SpeciesHumanMouse
Entrez

2597

100042025

Ensembl

ENSG00000111640

n/a

UniProt

P04406

P16858

RefSeq (mRNA)

XM_001476707

RefSeq (protein)

NP_001243728
NP_001276674
NP_001276675
NP_002037
NP_001344872

NP_001276655
NP_032110

Location (UCSC)Chr 12: 6.53 – 6.54 Mbn/a
PubMed search
Wikidata
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Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
determinants of enzyme thermostability observed in the molecular structure of thermus aquaticus d-glyceraldehyde-3-phosphate dehydrogenase at 2.5 angstroms resolution
Identifiers
SymbolGp_dh_N
PfamPF00044
Pfam clanCL0063
InterProIPR020828
PROSITEPDOC00069
SCOP21gd1 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain
crystal structure of glyceraldehyde-3-phosphate dehydrogenase from pyrococcus horikoshii ot3
Identifiers
SymbolGp_dh_C
PfamPF02800
Pfam clanCL0139
InterProIPR020829
PROSITEPDOC00069
SCOP21gd1 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
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