Reviewed (UniProtKB/Swiss-Prot)

  • THAT AND
  • THAT AND

Reviewed (UniProtKB/Swiss-Prot)





Protein Names | ProteinIDs  | Organism | Gene Names  | GeneID | Genome Annotation(Ensembl) |  Protein Sequence | 
General annotation |  References | Order
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
 B8M9V7
NCBI RefSeq

XP_002482101.1, XM_002482056.1.
Organism
Latin Name/
(Common Name)
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / OS NRRL 1006) (Penicillium stipitatum).
Taxonomic Identifier (NCBI)
 441959
Gene Names
 TALSN [GenPool]
GeneID

8099888
Genome
Annotation (Ensembl)
Protein Sequence
 
SEQUENCE   470 AA;  49749 MW;  136D79646ACB6DC4 CRC64;
MMILTKTGPL GPVTNSFIIA TTRRGQIRLY NILQDTTIPE PKRKHIPSSG TYPKGFRVSG
THVGVKAANT KYPDLALISS DEPCTAAAVF TTNKFQAAPV QISKLTLDQR KGKGIQSVVI
NSGCANAVTG KGGLEDAQSM ASKVDECNGI SEPSTLVMST GVIGQRLPIS KILDKIPTAY
SNLANTHNAW LATARAICTT DTFPKLISQT FTLPSSPGIT YSLAGMTKGA GMIHPNMATL
LGVLCTDAPV DASAMKPLLL QAVSRSFNSI SIDGDTSTND TIAFLANGAA GGQPVTSSSA
DYTALQKVLT SFAQSLSQLV VRDGEGATKF VTVRIQNSPC YESARRIAST IARSPLVKTA
LYGRDANWGR ILCAVGYADG VTEGTVIPER TSVSFKPVDG SPVLRLLVNG EPEVVDEERA
SAILQDEDLE IIVDLGGGSK GEKGLGGEEA VYWFCDFSHE YVTINGDYRT
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

  • "Genome sequence of Talaromyces stipitatus strain ATCC 10500.", Fedorova N.D., Joardar V.S., Maiti R., Schobel S., Amedeo P., Galens K., Inman J.M., Galinsky K.J., White O.R., Whitty B.R., Wortman J.R., Nierman W.C., Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.,

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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
Site238 - 2392Cleavage; by autolysis (By similarity).
Polypeptide chain? - 238239Arginine biosynthesis bifunctional protein ArgJ alpha chain (By similarity).
Polypeptide chain239 - 470232Arginine biosynthesis bifunctional protein ArgJ beta chain (By similarity).
Transit peptide1 - ?0Mitochondrion (Potential).
Protein-protein
Interaction
Databases
DIP
IntAct
MINT
STRING
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)
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