ARGJ_THENN
ID ARGJ_THENN Reviewed; 397 AA.
AC Q9Z4S1; B9K8S4;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 113.
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=CTN_1181;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10732680; DOI=10.1007/pl00008670;
RA Dimova D., Weigel P., Takahashi M., Marc F., Van Duyne G.D., Sakanyan V.;
RT "Thermostability, oligomerization and DNA-binding properties of the
RT regulatory protein ArgR from the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Mol. Gen. Genet. 263:119-130(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 180-187, FUNCTION AS AN OATASE AND AGSASE,
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP REACTION MECHANISM, AND SUBUNIT.
RC STRAIN=NCIMB 8224 / CCM 2186 / 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).
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=2.4 mM for acetyl-CoA (AGSase activity)
CC {ECO:0000269|PubMed:10931207};
CC KM=8.1 mM for N-acetyl-L-ornithine (OATase activity)
CC {ECO:0000269|PubMed:10931207};
CC KM=27.9 mM for L-glutamate (OATase activity)
CC {ECO:0000269|PubMed:10931207};
CC Vmax=7.7 mmol/min/mg enzyme (AGSase activity)
CC {ECO:0000269|PubMed:10931207};
CC Vmax=290 mmol/min/mg enzyme (OATase activity)
CC {ECO:0000269|PubMed:10931207};
CC pH dependence:
CC Optimum pH is 8 for OATase activity and 7.5-8 for AGSase activity.
CC {ECO:0000269|PubMed:10931207};
CC Temperature dependence:
CC Optimum temperature is 90 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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; AJ009897; CAB38110.1; -; Genomic_DNA.
DR EMBL; CP000916; ACM23357.1; -; Genomic_DNA.
DR RefSeq; WP_015919672.1; NC_011978.1.
DR AlphaFoldDB; Q9Z4S1; -.
DR SMR; Q9Z4S1; -.
DR STRING; 309803.CTN_1181; -.
DR MEROPS; T05.002; -.
DR EnsemblBacteria; ACM23357; ACM23357; CTN_1181.
DR KEGG; tna:CTN_1181; -.
DR eggNOG; COG1364; Bacteria.
DR HOGENOM; CLU_027172_1_0_0; -.
DR OMA; DYVHENS; -.
DR SABIO-RK; Q9Z4S1; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR Proteomes; UP000000445; 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 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..179
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002259"
FT CHAIN 180..397
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002260"
FT ACT_SITE 180
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 107
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 108
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 179..180
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT CONFLICT 105
FT /note="S -> F (in Ref. 1; CAB38110)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="T -> P (in Ref. 1; CAB38110)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="K -> R (in Ref. 1; CAB38110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 43043 MW; E8AC135A1EECC308 CRC64;
MFVPRGFSYA GVHCRIKRKR KDLGIIFSEV PCTAAGVFTT NVVKAAPVIY DMEILGKNPS
GIRAITVNSG VANACTGEQG MINARRMAEK TAKELNIPVE SVLVSSTGVI GVQLPMEKVE
SGIEEAVKNL SKDPVPFAEA IMTTDTKIKI HSKKVTIEGK EITVLGIAKG SGMIHPNMAT
MLSFITTDAN VSEDALKKLL KISVDDSYNM IDVDGDTSTN DMVIILANGL AGNAPIQEET
DGFWKLYEAV HEVNQVLAEK IVEDGEGATK VIEVEVRNAP DRNSARLIAR AIVSSNLVKT
AIYGEDANWG RVIAAAGYSG AQFDPDRLDL FFESAAGRIK VAENGQGVDF DEDTAKKILS
EKKVKIILDM KQGKELARAW GCDLTEKYVE INGRYRT
