ID   ARGJ_NEIGO              Reviewed;         406 AA.
AC   P38434; Q53567;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 61.
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   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CDC 50;
RX   MEDLINE=92210515; PubMed=1339419;
RA   Martin P.R., Mulks M.H.;
RT   "Sequence analysis and complementation studies of the argJ gene
RT   encoding ornithine acetyltransferase from Neisseria gonorrhoeae.";
RL   J. Bacteriol. 174:2694-2701(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRL 30465;
RX   MEDLINE=92176016; PubMed=1339413;
RA   Martin P.R., Mulks M.H.;
RT   "Molecular characterization of the argJ mutation in Neisseria
RT   gonorrhoeae strains with requirements for arginine, hypoxanthine, and
RT   uracil.";
RL   Infect. Immun. 60:970-975(1992).
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   -!- 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 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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.
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DR   EMBL; M65216; AAA25447.1; -; Genomic_DNA.
DR   EMBL; S85363; AAB21605.2; -; Genomic_DNA.
DR   PIR; A43850; A43850.
DR   BRENDA; 2.3.1.1; 588.
DR   BRENDA; 2.3.1.35; 588.
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   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Cytoplasm; Multifunctional enzyme; Transferase.
FT   CHAIN         1    189       Arginine biosynthesis bifunctional
FT                                protein argJ alpha chain (By similarity).
FT                                /FTId=PRO_0000002197.
FT   CHAIN       190    406       Arginine biosynthesis bifunctional
FT                                protein argJ beta chain (By similarity).
FT                                /FTId=PRO_0000002198.
FT   SITE        189    190       Cleavage; by autolysis (By similarity).
FT   CONFLICT    120    120       G -> A (in Ref. 2; AAB21605).
SQ   SEQUENCE   406 AA;  42866 MW;  5515EA4EB7503814 CRC64;
     MAVNLTEKTA EQLPDIDGIA LYTAQAGVKK PGHTDLTLIA VAAGSTVGAV FTTNRFCAAP
     VHIAKSHLFD EDGVRALVIN TGNANAGTGA QGRIDALAVC AAAARQIGCK PNQVMPFSTG
     VILEPLPADK IIAALPKMQP AFWNEAARAI MTTDTVPKAA SREGKVGDQH TVRATGIAKG
     SGMIHPNMAT MLGFIATDAK VSQPVLQLMT QEIADETFNT ITVDGDTSTN DSFVIIATGK
     NSQSEIDNIA DPRYAQLKEL LCSLALELAQ AIVRDGEGAT KFITVRVENA KTCDEARQAA
     YAAARSPLVK TAFFASDPNL GKRLAAIGYA DVADLDTDLV EMYLDDILVA EHGGRAASYT
     EAQGQAVMSK DEITVRIKLH RGQAAATVYT CDLSHGYVSI NADYRS
//