ID ARGJ_NEIG1 Reviewed; 406 AA.
AC Q5F7I3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 31-OCT-2012, entry version 54.
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=AGSase;
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; OrderedLocusNames=NGO1194;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes two activities which are involved in the
CC cyclic version of arginine biosynthesis: the synthesis of N-
CC acetylglutamate from glutamate and acetyl-CoA as the acetyl donor,
CC and of ornithine by transacetylation between N(2)-acetylornithine
CC and glutamate (By similarity).
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 (By similarity).
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; AE004969; AAW89854.1; -; Genomic_DNA.
DR RefSeq; YP_208266.1; NC_002946.2.
DR ProteinModelPortal; Q5F7I3; -.
DR STRING; Q5F7I3; -.
DR EnsemblBacteria; EBNEIT00000002699; EBNEIP00000002540; EBNEIG00000002699.
DR GeneID; 3282038; -.
DR GenomeReviews; AE004969_GR; NGO1194.
DR KEGG; ngo:NGO1194; -.
DR PATRIC; 20335685; VBINeiGon24812_1401.
DR eggNOG; COG1364; -.
DR HOGENOM; HOG000022798; -.
DR KO; K00620; -.
DR OMA; PNMGTML; -.
DR ProtClustDB; PRK05388; -.
DR BioCyc; NGON242231:NGO1194-MONOMER; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:EC.
DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR HAMAP; MF_01106; ArgJ; 1; -.
DR InterPro; IPR002813; Arg_biosynth_ArgJ.
DR InterPro; IPR016117; Pept_S58_DmpA/Arg_biosyn_ArgJ.
DR PANTHER; PTHR23100; PTHR23100; 1.
DR Pfam; PF01960; ArgJ; 1.
DR ProDom; PD004193; Arg_biosynth_ArgJ; 1.
DR SUPFAM; SSF56266; Pept_S58_DmpA/Arg_biosyn_ArgJ; 1.
DR TIGRFAMs; TIGR00120; ArgJ; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW Autocatalytic cleavage; Complete proteome; Cytoplasm;
KW Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1 189 Arginine biosynthesis bifunctional
FT protein ArgJ alpha chain (By similarity).
FT /FTId=PRO_0000227234.
FT CHAIN 190 406 Arginine biosynthesis bifunctional
FT protein ArgJ beta chain (By similarity).
FT /FTId=PRO_0000227235.
FT ACT_SITE 190 190 Nucleophile (By similarity).
FT BINDING 152 152 Substrate (By similarity).
FT BINDING 179 179 Substrate (By similarity).
FT BINDING 190 190 Substrate (By similarity).
FT BINDING 277 277 Substrate (By similarity).
FT BINDING 401 401 Substrate (By similarity).
FT BINDING 406 406 Substrate (By similarity).
FT SITE 119 119 Involved in the stabilization of negative
FT charge on the oxyanion by the formation
FT of the oxyanion hole (By similarity).
FT SITE 120 120 Involved in the stabilization of negative
FT charge on the oxyanion by the formation
FT of the oxyanion hole (By similarity).
FT SITE 189 190 Cleavage; by autolysis (By similarity).
SQ SEQUENCE 406 AA; 42851 MW; A3F3635905E2C856 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 GRLLAAIGYA DVADLDTDLV EMYLDDILVA EHGGRAASYT
EAQGQAVMSK DEITVRIKLH RGQAAATVYT CDLSHGYVSI NADYRS
//