Function and Biology

Crystal structure of human dimethylarginine dymethylaminohydrolase-1 (DDAH-1)

Source organism: Homo sapiens
Biochemical function: metal ion binding
Biological process: negative regulation of cellular response to hypoxia
Cellular component: extracellular exosome

EC 3.5.3.18: Dimethylargininase

Reaction catalysed:
N(omega),N(omega)-dimethyl-L-arginine + H(2)O = dimethylamine + L-citrulline
Systematic name:
N(omega),N(omega')-dimethyl-L-arginine dimethylamidohydrolase
Alternative Name(s):
  • Dimethylarginine dimethylaminohydrolase
  • N(G),N(G)-dimethyl-L-arginine dimethylamidohydrolase
  • N(G),N(G)-dimethylarginine dimethylaminohydrolase
  • N(omega),N(omega')-methyl-L-arginine dimethylamidohydrolase
  • Omega,omega'-di-N-methyl-L-arginine dimethylamidohydrolase

Sequence family

Pfam Protein family (Pfam)
PF19420
Domain description: N,N dimethylarginine dimethylhydrolase, eukaryotic
Occurring in:
  1. N(G),N(G)-dimethylarginine dimethylaminohydrolase 1

InterPro InterPro annotation
IPR033199
Domain description: Dimethylarginine dimethylaminohydrolase-like
Occurring in:
  1. N(G),N(G)-dimethylarginine dimethylaminohydrolase 1

Structure domain

CATH CATH domain
3.75.10.10
Class: Alpha Beta
Architecture: 5-stranded Propeller
Topology: L-arginine/glycine Amidinotransferase; Chain A
Homology: L-arginine/glycine Amidinotransferase; Chain A
Occurring in:
  1. N(G),N(G)-dimethylarginine dimethylaminohydrolase 1
The deposited structure of PDB entry 3i2e contains 2 copies of CATH domain 3.75.10.10 (L-arginine/glycine Amidinotransferase; Chain A) in N(G),N(G)-dimethylarginine dimethylaminohydrolase 1. Showing 1 copy in chain A.