ID   ARGJ_GEOSL              Reviewed;         393 AA.
AC   P62061;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   16-JUN-2009, entry version 43.
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; OrderedLocusNames=GSU2049;
OS   Geobacter sulfurreducens.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=35554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R.,
RA   Van Aken S.E., Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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 (By
CC       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 (Probable).
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; AE017180; AAR35425.1; -; Genomic_DNA.
DR   RefSeq; NP_953098.1; -.
DR   MEROPS; T05.001; -.
DR   GeneID; 2686046; -.
DR   GenomeReviews; AE017180_GR; GSU2049.
DR   KEGG; gsu:GSU2049; -.
DR   NMPDR; fig|243231.1.peg.2036; -.
DR   TIGR; GSU2049; -.
DR   HOGENOM; P62061; -.
DR   OMA; P62061; VHENSAY.
DR   BioCyc; GSUL243231:GSU_2049-MON; -.
DR   BRENDA; 2.3.1.1; 276898.
DR   BRENDA; 2.3.1.35; 276898.
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   Complete proteome; Cytoplasm; Multifunctional enzyme; Transferase.
FT   CHAIN         1    178       Arginine biosynthesis bifunctional
FT                                protein argJ alpha chain (By similarity).
FT                                /FTId=PRO_0000002169.
FT   CHAIN       179    393       Arginine biosynthesis bifunctional
FT                                protein argJ beta chain (By similarity).
FT                                /FTId=PRO_0000002170.
FT   SITE        178    179       Cleavage; by autolysis (By similarity).
SQ   SEQUENCE   393 AA;  40986 MW;  8808BFB962CB9C57 CRC64;
     MNVKGFRFSA VEAAIKKPGR LDLALICSDA PAAVAAVYTT NKVKAAPVLL DMERTTSGTC
     RAVVVNSGNA NACTGDRGME DARETTSLVA ERIGASEHEV LVCSTGVIGV PLPMERIRGG
     IPSLVAGLGS ATLDQIAAAI MTTDTFPKLE ARTGTAGGVG YTIAGIAKGA GMIMPNMATM
     LAFVVTDAAV DPQWLDRVFR RANDTSFNAI TVDGDMSTND TAIIMANGAA GNPVLSEGSE
     GAAEFAVLLE EVLLSLAKLI VKDGEGATKF VEVTVKGARS DADAKRAAMA VANSCLVKTA
     FFGQDANWGR IFAAVGYSGA DVEPDRAELF FDDVRMVQGG VFAGGDAEAR GTGVLRKKEF
     TVTVDLHLGD GRATVYTSDL SYDYVKINAD YRT
//