ARGJ_MYCTO
ID ARGJ_MYCTO Reviewed; 404 AA.
AC P9WPZ2; L0TA91; P63571; P94988;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
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=MT1691;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC version of arginine biosynthesis: the synthesis of N-acetylglutamate
CC from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by
CC transacetylation between N(2)-acetylornithine and glutamate.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-
CC acetyl-L-glutamate; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=2.3.1.35;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine
CC (cyclic): step 1/1.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e.
CC capable of catalyzing only the fifth step of the arginine biosynthetic
CC pathway.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000305}.
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DR EMBL; AE000516; AAK45960.1; -; Genomic_DNA.
DR PIR; H70620; H70620.
DR RefSeq; WP_003408160.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPZ2; -.
DR SMR; P9WPZ2; -.
DR EnsemblBacteria; AAK45960; AAK45960; MT1691.
DR KEGG; mtc:MT1691; -.
DR PATRIC; fig|83331.31.peg.1818; -.
DR HOGENOM; CLU_027172_2_0_11; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02152; OAT; 1.
DR Gene3D; 3.10.20.340; -; 1.
DR HAMAP; MF_01106; ArgJ; 1.
DR InterPro; IPR002813; Arg_biosynth_ArgJ.
DR InterPro; IPR016117; ArgJ-like_dom_sf.
DR InterPro; IPR042195; ArgJ_beta_C.
DR PANTHER; PTHR23100; PTHR23100; 1.
DR Pfam; PF01960; ArgJ; 1.
DR SUPFAM; SSF56266; SSF56266; 1.
DR TIGRFAMs; TIGR00120; ArgJ; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW Autocatalytic cleavage; Cytoplasm; Multifunctional enzyme; Transferase.
FT CHAIN 1..199
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000426866"
FT CHAIN 200..404
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000426867"
FT ACT_SITE 200
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000250"
FT SITE 128
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000250"
FT SITE 199..200
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 404 AA; 41147 MW; 7BD0CCD5FB8DE634 CRC64;
MTDLAGTTRL LRAQGVTAPA GFRAAGVAAG IKASGALDLA LVFNEGPDYA AAGVFTRNQV
KAAPVLWTQQ VLTTGRLRAV ILNSGGANAC TGPAGFADTH ATAEAVAAAL SDWGTETGAI
EVAVCSTGLI GDRLPMDKLL AGVAHVVHEM HGGLVGGDEA AHAIMTTDNV PKQVALHHHD
NWTVGGMAKG AGMLAPSLAT MLCVLTTDAA AEPAALERAL RRAAAATFDR LDIDGSCSTN
DTVLLLSSGA SEIPPAQADL DEAVLRVCDD LCAQLQADAE GVTKRVTVTV TGAATEDDAL
VAARQIARDS LVKTALFGSD PNWGRVLAAV GMAPITLDPD RISVSFNGAA VCVHGVGAPG
AREVDLSDAD IDITVDLGVG DGQARIRTTD LSHAYVEENS AYSS
