Arginase

Details

Name
Arginase
Synonyms
  • 3.5.3.1
Gene Name
rocF
Organism
Bacillus caldovelox
Amino acid sequence
>lcl|BSEQ0019358|Arginase
MKPISIIGVPMDLGQTRRGVDMGPSAMRYAGVIERLERLHYDIEDLGDIPIGKAERLHEQ
GDSRLRNLKAVAEANEKLAAAVDQVVQRGRFPLVLGGDHSIAIGTLAGVAKHYERLGVIW
YDAHGDVNTAETSPSGNIHGMPLAASLGFGHPALTQIGGYSPKIKPEHVVLIGVRSLDEG
EKKFIREKGIKIYTMHEVDRLGMTRVMEETIAYLKERTDGVHLSLDLDGLDPSDAPGVGT
PVIGGLTYRESHLAMEMLAEAQIITSAEFVEVNPILDERNKTASVAVALMGSLFGEKLM
Number of residues
299
Molecular Weight
32432.98
Theoretical pI
5.77
GO Classification
Functions
arginase activity / metal ion binding
Processes
arginine metabolic process / urea cycle
General Function
Metal ion binding
Specific Function
Controls arginine catabolism.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0005849|900 bp
ATGAAGCCAATTTCAATTATCGGGGTTCCGATGGATTTAGGGCAGACACGCCGCGGCGTT
GATATGGGGCCGAGCGCAATGCGTTATGCAGGCGTCATCGAACGTCTGGAACGTCTTCAT
TACGATATTGAAGATTTGGGAGATATTCCGATTGGAAAAGCAGAGCGGTTGCACGAGCAA
GGAGATTCACGGTTGCGCAATTTGAAAGCGGTTGCGGAAGCGAACGAGAAACTTGCGGCG
GCGGTTGACCAAGTCGTTCAGCGGGGGCGATTTCCGCTTGTGTTGGGCGGCGACCATAGC
ATCGCCATTGGCACGCTCGCCGGGGTGGCGAAACATTATGAGCGGCTTGGAGTGATCTGG
TATGACGCGCATGGCGACGTCAACACCGCGGAAACGTCGCCGTCTGGAAACATTCATGGC
ATGCCGCTGGCGGCGAGCCTCGGGTTTGGCCATCCGGCGCTGACGCAAATCGGCGGATAC
AGCCCCAAAATCAAGCCGGAACATGTCGTGTTGATCGGCGTCCGTTCCCTTGATGAAGGG
GAGAAGAAGTTTATTCGCGAAAAAGGAATCAAAATTTACACGATGCATGAGGTTGATCGG
CTCGGAATGACAAGGGTGATGGAAGAAACGATCGCCTATTTAAAAGAACGAACGGATGGC
GTTCATTTGTCGCTTGACTTGGATGGCCTTGACCCAAGCGACGCACCGGGAGTCGGAACG
CCTGTCATTGGAGGATTGACATACCGCGAAAGCCATTTGGCGATGGAGATGCTGGCCGAG
GCACAAATCATCACTTCAGCGGAATTTGTCGAAGTGAACCCGATCTTGGATGAGCGGAAC
AAAACAGCATCAGTGGCTGTAGCGCTGATGGGGTCGTTGTTTGGTGAAAAACTCATGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP53608
UniProtKB Entry NameARGI_BACCD
GenBank Gene IDU48226
General References
  1. Bewley MC, Lott JS, Baker EN, Patchett ML: The cloning, expression and crystallisation of a thermostable arginase. FEBS Lett. 1996 May 20;386(2-3):215-8. [Article]
  2. Bewley MC, Jeffrey PD, Patchett ML, Kanyo ZF, Baker EN: Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily. Structure. 1999 Apr 15;7(4):435-48. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00536GuanidineapprovedunknownDetails