Reviewed (UniProtKB/Swiss-Prot)

  • THAT AND
  • THAT AND

Reviewed (UniProtKB/Swiss-Prot)





Protein Names
Recommended name:
Arginine biosynthesis bifunctional protein ArgJ, mitochondrial;Glutamate N-acetyltransferase;Ornithine acetyltransferase;Ornithine transacetylase;Amino-acid acetyltransferase;N-acetylglutamate synthase;Arginine biosynthesis bifunctional protein ArgJ alpha chain;Arginine biosynthesis bifunctional protein ArgJ beta chain;
Alternative name(s):
Protein IDs
(Accession numbers)
UniProtKB
A7TPS8
NCBI RefSeq

XP_001643587.1, XM_001643537.1.

Organism
Latin Name/
(Common Name)
Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) OS (Kluyveromyces polysporus).
Taxonomic Identifier (NCBI)
436907
Gene Names
VANPO [GenPool]
GeneID

5543849

Genome
Annotation (Ensembl)
Protein Sequence
SEQUENCE   441 AA;  47559 MW;  DEBEFAC1DC624E64 CRC64;
MKLNTKLLQQ ASKSVDKYAL YVPKNGVFPR GFQVGSTASG VKKNGNLDLG IIRNTNTSRP
AAAAAVFTTN KFKAAPVVVS KQILEDKNGT GINAIVINSG CANSVTGEVG IEDAKKLISH
VDSKLGTSMS TLPMSTGVIG QRLHVNKISK GIDEIFDNNK FGSDFQSWLD MAKSICTTDT
FPKLVTSRFS LPNGEKYTLT GIAKGAGMIC PNMATLLGFI VTDLPIKSSA LKSILTHATN
RSFNCISVDG DMSTNDTICM IANGAVETKE IDETSQEYVQ VQNQVTEFAQ QLAQLVVRDG
EGSTKFVTVK VQNSLTFEDA KIIAESISNS LLVKTALYGQ DANWGRILCA IGYAKLDNLK
SLNVDKINVS FIATDGSEPK ELKLVVNGVP QLEIDEARAS EILNLNDLEI SVDLGTGTEE
AQFWTCDISH EYVTINGDYR T
General annotation
Function
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate (By similarity).
Cofactor
Subunit structure
Heterodimer of an alpha and a beta chain (By similarity).
Subcellular location

Mitochondrion matrix (By similarity).

Tissue specificity
Induction
Domain
Post-translational modification

The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion (By similarity).

Involvement in disease

References
  • "Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication.", Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H., Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007)., PubMed:17494770 DOI:10.1073/pnas.0608218104

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Gene & Protein
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Protein Domain Databases
InterPro

IPR002813, Arg_biosynth_ArgJ.

IPR016117, Pept_S58_DmpA/Arg_biosyn_ArgJ.

Gene3D
PANTHER

PTHR23100, ArgJ; 1.

Pfam

PF01960, ArgJ; 1.

PRINTS
SUPFAM

SSF56266, Pept_S58_DmpA/Arg_biosyn_ArgJ; 1.

PROSITE
3D Structure
Database (PDB)
Entry
Method
Resolution (A)
Chain
Positions
PDBsum
Sequence
Annotation
Feature key
Position(s)
Length
Description
Site214 - 2152Cleavage; by autolysis (By similarity).
Polypeptide chain? - 214215Arginine biosynthesis bifunctional protein ArgJ alpha chain (By similarity).
Polypeptide chain215 - 441227Arginine biosynthesis bifunctional protein ArgJ beta chain (By similarity).
Transit peptide1 - ?0Mitochondrion (Potential).
Protein-protein
Interaction
Databases
DIP
IntAct
MINT
STRING

A7TPS8

Binary Interactions
With
Entry
#Exp.
IntAct
Enzyme and Pathway Databases
Pathway
Interaction DB
Reactome
Phylogenomic Database
HOVERGEN
InParanoid
OMA
OrthoDB

EOG42VCR0

Proteomics
Database (PRIDE)
Comparative
Toxicogenomics
Database (CTD)
Order Your Custom Protein
Secured Online Quotation
Email: gene@genscript.com
Phone: 1-877-436-7274 (Toll-Free) 1-732-885-9188
Fax: 1-732-210-0262 1-732-885-5878