ID C8W632_DESAS Unreviewed; 405 AA.
AC C8W632;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 28.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ;
GN Name=argJ; OrderedLocusNames=Dtox_0567;
OS Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS B-1644).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=485916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644;
RX PubMed=21304664; DOI=10.4056/sigs.39508;;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
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: 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; CP001720; ACV61487.1; -; Genomic_DNA.
DR RefSeq; YP_003190110.1; NC_013216.1.
DR STRING; 485916.Dtox_0567; -.
DR MEROPS; T05.001; -.
DR EnsemblBacteria; ACV61487; ACV61487; Dtox_0567.
DR GeneID; 8427502; -.
DR KEGG; dae:Dtox_0567; -.
DR PATRIC; 21717841; VBIDesAce42372_0576.
DR eggNOG; COG1364; -.
DR HOGENOM; HOG000022797; -.
DR KO; K00620; -.
DR OMA; DYVHENS; -.
DR ProtClustDB; CLSK2821346; -.
DR BioCyc; DACE485916:GHUF-583-MONOMER; -.
DR UniPathway; UPA00068; UER00106.
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 Gene3D; 3.60.70.12; -; 1.
DR HAMAP; MF_01106; ArgJ; 1; -.
DR InterPro; IPR002813; Arg_biosynth_ArgJ.
DR InterPro; IPR016117; ArgJ-like_dom.
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; Transferase.
FT ACT_SITE 192 192 Nucleophile (By similarity).
FT BINDING 155 155 Substrate (By similarity).
FT BINDING 181 181 Substrate (By similarity).
FT BINDING 192 192 Substrate (By similarity).
FT BINDING 278 278 Substrate (By similarity).
FT BINDING 400 400 Substrate (By similarity).
FT BINDING 405 405 Substrate (By similarity).
FT SITE 118 118 Involved in the stabilization of negative
FT charge on the oxyanion by the formation
FT of the oxyanion hole (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 191 192 Cleavage; by autolysis (By similarity).
SQ SEQUENCE 405 AA; 42285 MW; 0B728FB35336EF3B CRC64;
MSKEFKLELV PGGVTAASGF TACGVRAGIK NDKKDLAIIY SKLPCSATGV YTTNKVQAAP
VQLTRQRLSD GHAQAVIINS GYANACNGPQ GLRDALKTSS VLAESLNIQE NQVLVASTGV
IGQNLPMDKI LNGIALAVSQ LSPEGGPDAA EAIMTTDTVS KQIAVKFELS GVPVVIGGMA
KGSGMIHPNM ATMLGFITTD AAVDVHLLNK ALKSVVEKTF NMITVDGDTS TNDMVLLLAN
GAAGNQQLDS EGSDFELFCC ALCEVCISLS KEIAGDGEGA TKLVEVKVIN AATVNDARLA
AKTVAASNLV KTAIFGADAN WGRIICAAGY SGADFDPGKV DIFLGNEQVA KDGKALDFSE
ENASEILSQK EVKILIDFKT GTETATAWGC DLTYDYIKIN GSYRS
//
