ID   D0U4I6_9GAMM            Unreviewed;       394 AA.
AC   D0U4I6;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-JUL-2011, entry version 6.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ 1;
GN   Name=argJ1; ORFNames=SUP05_FGYC13J70035;
OS   uncultured SUP05 cluster bacterium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   unclassified Oceanospirillales; SUP05 cluster; environmental samples.
OX   NCBI_TaxID=655186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J.,
RA   Tringe S.G., Tortell P.D., Hallam S.J.;
RT   "Metagenome of a versatile chemolithoautotroph from expanding oxygen
RT   minimum zones.";
RL   Science 326:578-582(2009).
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: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-
CC       glutamate.
CC   -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L-
CC       ornithine + N-acetyl-L-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 (By similarity).
CC   -!- SIMILARITY: Belongs to the ArgJ family.
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DR   EMBL; GQ351267; ACX30518.1; -; Genomic_DNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate 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; ArgJ; 1; -.
DR   InterPro; IPR002813; Arg_biosynth_ArgJ.
DR   InterPro; IPR016117; Pept_S58_DmpA/Arg_biosyn_ArgJ.
DR   PANTHER; PTHR23100; ArgJ; 1.
DR   Pfam; PF01960; 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; Cytoplasm; Multifunctional enzyme;
KW   Transferase.
FT   SITE        182    183       Cleavage; by autolysis (By similarity).
SQ   SEQUENCE   394 AA;  42035 MW;  3311321E3D55C789 CRC64;
     MSQSLLNIEG VLSASIDAGI KNNDATDLSI IYLTESTVTA AVFTQNVFCA APVLVAKNHL
     NHHPKALLIN SGNANAGTGS QGMENTLHTC ACLAGELNIN TEQVLPFSTG VIGQQLELDK
     FNQGIPKVVV KLSTDAMGDV AKGILTTDLV EKTASKQFEV NGKTVTISGI AKGSGMIRPD
     MATMLSFIFT DVESTQAKLQ QCLTTSVNQS FNRITVDGDT STNDACTLSA TGASGVDIHD
     CVDEFQQALN EVTQSLAYQI IKDGEGATKF VEVCVKGGAS SEDCLEVAYT VAHSPLVKTA
     LFASDANWGR ILAAVGRANI SNLKIEDINI YLNEVSIIQA GEPDEHYTEE AGSNEMAKEE
     IIITIEIGKG DAQESVWTTD FSYDYVKINA EYRT
//