ID   ARGJ_BACST              Reviewed;         410 AA.
AC   Q07908;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Arginine biosynthesis bifunctional protein argJ;
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase;
DE              EC=2.3.1.35;
DE     AltName: Full=Ornithine acetyltransferase;
DE              Short=OATase;
DE     AltName: Full=Ornithine transacetylase;
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase;
DE              EC=2.3.1.1;
DE     AltName: Full=N-acetylglutamate synthase;
DE              Short=AGS;
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein argJ alpha chain;
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein argJ beta chain;
GN   Name=argJ;
OS   Bacillus stearothermophilus (Geobacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIB 8224 / CCM 2186;
RX   MEDLINE=93232760; PubMed=8473852;
RA   Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I.,
RA   Pierard P., Glansdorff N.;
RT   "Primary structure, partial purification and regulation of key enzymes
RT   of the acetyl cycle of arginine biosynthesis in Bacillus
RT   stearothermophilus: dual function of ornithine acetyltransferase.";
RL   J. Gen. Microbiol. 139:393-402(1993).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=NCIB 8224 / CCM 2186;
RX   MEDLINE=20389546; PubMed=10931207;
RX   DOI=10.1046/j.1432-1327.2000.01593.x;
RA   Marc F., Weigel P., Legrain C., Almeras Y., Santrot M., Glansdorff N.,
RA   Sakanyan V.;
RT   "Characterization and kinetic mechanism of mono- and bifunctional
RT   ornithine acetyltransferases from thermophilic microorganisms.";
RL   Eur. J. Biochem. 267:5217-5226(2000).
RN   [3]
RP   CHARACTERIZATION, AND MUTAGENESIS OF THR-197.
RC   STRAIN=NCIB 8224 / CCM 2186;
RX   MEDLINE=21326091; PubMed=11320085; DOI=10.1074/jbc.M100392200;
RA   Marc F., Weigel P., Legrain C., Glansdorff N., Sakanyan V.;
RT   "An invariant threonine is involved in self-catalyzed cleavage of the
RT   precursor protein for ornithine acetyltransferase.";
RL   J. Biol. Chem. 276:25404-25410(2001).
CC   -!- FUNCTION: Catalyzes two activities which are involved in the
CC       cyclic version of arginine biosynthesis: the synthesis of
CC       acetylglutamate from glutamate and acetyl-CoA, and of ornithine by
CC       transacetylation between acetylornithine and glutamate.
CC   -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L-
CC       ornithine + N-acetyl-L-glutamate.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-
CC       glutamate.
CC   -!- ENZYME REGULATION: Feedback inhibition by L-arginine.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-
CC       acetyl-L-ornithine (cyclic): step 1/1.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 1/4.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- MISCELLANEOUS: Independently synthesized alpha and beta subunits
CC       do not reconstitute a functional protein. Self-catalyzed precursor
CC       cleavage is a necessary step to form an active enzyme, probably by
CC       directing appropriate folding and/or topological organization of
CC       the active site.
CC   -!- MISCELLANEOUS: Some bacteria possess a monofunctional argJ, i.e.,
CC       capable of catalyzing only the fifth step of the arginine
CC       biosynthetic pathway.
CC   -!- SIMILARITY: Belongs to the argJ family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L06036; AAA22197.1; -; Genomic_DNA.
DR   PIR; I39766; I39766.
DR   SMR; Q07908; 197-408.
DR   MEROPS; T05.001; -.
DR   BRENDA; 2.3.1.1; 266715.
DR   BRENDA; 2.3.1.35; 266715.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:amino-acid N-acetyltransferase activity; IEA:HAMAP.
DR   GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01106; -; 1.
DR   InterPro; IPR002813; Arg_biosynth_ArgJ.
DR   PANTHER; PTHR23100; ArgJ; 1.
DR   Pfam; PF01960; ArgJ; 1.
DR   ProDom; PD004193; ArgJ; 2.
DR   TIGRFAMs; TIGR00120; ArgJ; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Cytoplasm; Multifunctional enzyme; Transferase.
FT   CHAIN         1    196       Arginine biosynthesis bifunctional
FT                                protein argJ alpha chain.
FT                                /FTId=PRO_0000002119.
FT   CHAIN       197    410       Arginine biosynthesis bifunctional
FT                                protein argJ beta chain.
FT                                /FTId=PRO_0000002120.
FT   SITE        196    197       Cleavage; by autolysis.
FT   MUTAGEN     197    197       T->G: No autoproteolysis; loss of
FT                                activity.
FT   MUTAGEN     197    197       T->S,C: Low rate of intramolecular
FT                                cleavage; loss of activity.
SQ   SEQUENCE   410 AA;  43377 MW;  00E948D64E8A8913 CRC64;
     MTITKQTGQV TAVADGTVVT PEGFQAAGVN AGLRYSKNDL GVILCDVPAS AAAVYTQSHF
     QAAPLKVTQA SLAVEQKLQA VIVNRPCANA CTGAQGLKDA YEMRELCAKQ FGLALHHVAV
     ASTGVIGEYL PMEKIRAGIK QLVPGVTMAD AEAFQTAILT TDTVMKRACY QTTIDGKTVT
     VGGAAKGSGM IHPNMATMLA FITTDANVSS PVLHAALRSI TDVSFNQITV DGDTSTNDMV
     VVMASGLAGN DELTPDHPDW ENFYEALRKT CEDLAKQIAK DGEGATKLIE VRVRGAKTDE
     EAKKIAKQIV GSNLVKTAVY GADANWGRII GAIGYSDAEV NPDNVDVAIG PMVMLKGSEP
     QPFSEEEAAA YLQQETVVIE VDLHIGDGVG VAWGCDLTYD YVKINASYRT
//