ARGJ_GEOSE
ID ARGJ_GEOSE Reviewed; 410 AA.
AC Q07908;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 116.
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;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX PubMed=8473852; DOI=10.1099/00221287-139-3-393;
RA Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I.,
RA Pierard P., Glansdorff N.;
RT "Primary structure, partial purification and regulation of key enzymes of
RT the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus:
RT dual function of ornithine acetyltransferase.";
RL J. Gen. Microbiol. 139:393-402(1993).
RN [2]
RP PROTEIN SEQUENCE OF 197-204, FUNCTION AS AN OATASE AND AGSASE,
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP REACTION MECHANISM, AND SUBUNIT.
RC STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX PubMed=10931207; DOI=10.1046/j.1432-1327.2000.01593.x;
RA Marc F., Weigel P., Legrain C., Almeras Y., Santrot M., Glansdorff N.,
RA Sakanyan V.;
RT "Characterization and kinetic mechanism of mono- and bifunctional ornithine
RT acetyltransferases from thermophilic microorganisms.";
RL Eur. J. Biochem. 267:5217-5226(2000).
RN [3]
RP MUTAGENESIS OF THR-197, AUTOCATALYTIC CLEAVAGE, REACTION MECHANISM, AND
RP SUBUNIT.
RC STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX PubMed=11320085; DOI=10.1074/jbc.m100392200;
RA Marc F., Weigel P., Legrain C., Glansdorff N., Sakanyan V.;
RT "An invariant threonine is involved in self-catalyzed cleavage of the
RT precursor protein for ornithine acetyltransferase.";
RL J. Biol. Chem. 276:25404-25410(2001).
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:0000269|PubMed:10931207}.
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 Evidence={ECO:0000269|PubMed:10931207};
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 Evidence={ECO:0000269|PubMed:10931207};
CC -!- ACTIVITY REGULATION: Competitively inhibited by L-ornithine.
CC {ECO:0000269|PubMed:10931207}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.9 mM for acetyl-CoA (AGSase activity)
CC {ECO:0000269|PubMed:10931207};
CC KM=2.7 mM for N-acetyl-L-ornithine (OATase activity)
CC {ECO:0000269|PubMed:10931207};
CC KM=19.2 mM for L-glutamate (OATase activity)
CC {ECO:0000269|PubMed:10931207};
CC Vmax=2.5 mmol/min/mg enzyme (AGSase activity)
CC {ECO:0000269|PubMed:10931207};
CC Vmax=27 mmol/min/mg enzyme (OATase activity)
CC {ECO:0000269|PubMed:10931207};
CC pH dependence:
CC Optimum pH is 8 for OATase activity and 8-8.5 for AGSase activity.
CC {ECO:0000269|PubMed:10931207};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius (OATase activity).
CC {ECO:0000269|PubMed:10931207};
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:0000269|PubMed:10931207, ECO:0000269|PubMed:11320085}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Independently synthesized alpha and beta subunits do not
CC reconstitute a functional protein. Self-catalyzed precursor cleavage is
CC a necessary step to form an active enzyme, probably by directing
CC appropriate folding and/or topological organization of the active site
CC (PubMed:11320085). {ECO:0000305|PubMed:11320085}.
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; L06036; AAA22197.1; -; Genomic_DNA.
DR PIR; I39766; I39766.
DR AlphaFoldDB; Q07908; -.
DR SMR; Q07908; -.
DR MEROPS; T05.002; -.
DR KEGG; ag:AAA22197; -.
DR SABIO-RK; Q07908; -.
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: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 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW Autocatalytic cleavage; Cytoplasm; Direct protein sequencing;
KW Multifunctional enzyme; Transferase.
FT CHAIN 1..196
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /id="PRO_0000002119"
FT CHAIN 197..410
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /id="PRO_0000002120"
FT ACT_SITE 197
FT /note="Nucleophile"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 123
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 124
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 196..197
FT /note="Cleavage; by autolysis"
FT MUTAGEN 197
FT /note="T->G: No autoproteolysis; loss of activity."
FT /evidence="ECO:0000269|PubMed:11320085"
FT MUTAGEN 197
FT /note="T->S,C: Low rate of intramolecular cleavage; loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:11320085"
SQ SEQUENCE 410 AA; 43377 MW; 00E948D64E8A8913 CRC64;
MTITKQTGQV TAVADGTVVT PEGFQAAGVN AGLRYSKNDL GVILCDVPAS AAAVYTQSHF
QAAPLKVTQA SLAVEQKLQA VIVNRPCANA CTGAQGLKDA YEMRELCAKQ FGLALHHVAV
ASTGVIGEYL PMEKIRAGIK QLVPGVTMAD AEAFQTAILT TDTVMKRACY QTTIDGKTVT
VGGAAKGSGM IHPNMATMLA FITTDANVSS PVLHAALRSI TDVSFNQITV DGDTSTNDMV
VVMASGLAGN DELTPDHPDW ENFYEALRKT CEDLAKQIAK DGEGATKLIE VRVRGAKTDE
EAKKIAKQIV GSNLVKTAVY GADANWGRII GAIGYSDAEV NPDNVDVAIG PMVMLKGSEP
QPFSEEEAAA YLQQETVVIE VDLHIGDGVG VAWGCDLTYD YVKINASYRT
