ARGJ_METJA
ID ARGJ_METJA Reviewed; 402 AA.
AC Q57645;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 Contains:
DE RecName: Full=Glutamate N-acetyltransferase alpha chain;
DE Contains:
DE RecName: Full=Glutamate N-acetyltransferase beta chain;
GN Name=argJ; OrderedLocusNames=MJ0186;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PROTEIN SEQUENCE OF 185-192, FUNCTION AS AN OATASE, BIOPHYSICOCHEMICAL
RP PROPERTIES, CATALYTIC ACTIVITY, ACTIVITY REGULATION, REACTION MECHANISM,
RP 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 only the synthesis of N-acetylglutamate from
CC glutamate and acetyl-CoA as the acetyl donor.
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 -!- ACTIVITY REGULATION: Competitively inhibited by L-ornithine.
CC {ECO:0000269|PubMed:10931207}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.6 mM for N-acetyl-L-ornithine {ECO:0000269|PubMed:10931207};
CC KM=11.3 mM for L-glutamate {ECO:0000269|PubMed:10931207};
CC Vmax=175 mmol/min/mg enzyme {ECO:0000269|PubMed:10931207};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:10931207};
CC Temperature dependence:
CC Optimum temperature is above 95 degrees Celsius.
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 -!- 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; L77117; AAB98166.1; -; Genomic_DNA.
DR PIR; C64323; C64323.
DR RefSeq; WP_010869681.1; NC_000909.1.
DR AlphaFoldDB; Q57645; -.
DR SMR; Q57645; -.
DR STRING; 243232.MJ_0186; -.
DR MEROPS; T05.002; -.
DR DNASU; 1451033; -.
DR EnsemblBacteria; AAB98166; AAB98166; MJ_0186.
DR GeneID; 1451033; -.
DR KEGG; mja:MJ_0186; -.
DR eggNOG; arCOG04413; Archaea.
DR HOGENOM; CLU_027172_1_0_2; -.
DR InParanoid; Q57645; -.
DR OMA; DYVHENS; -.
DR OrthoDB; 29910at2157; -.
DR PhylomeDB; Q57645; -.
DR SABIO-RK; Q57645; -.
DR UniPathway; UPA00068; UER00111.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006592; P:ornithine biosynthetic process; IBA:GO_Central.
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 Reference proteome; Transferase.
FT CHAIN 1..184
FT /note="Glutamate N-acetyltransferase alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002273"
FT CHAIN 185..402
FT /note="Glutamate N-acetyltransferase beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002274"
FT ACT_SITE 185
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="substrate"
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 109
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 184..185
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 402 AA; 43757 MW; 2D915AB01CC7A8D6 CRC64;
MRVIDGGVTA PKGFKANGYK EGKFGVAIII SEKDAVGAGT FTTNKVVAHP VVLSRELIKN
RDKFRAIVAN SGNANCFTKD GMEDAKEMQR LVAELFNINE DEVLVASTGV IGRKMDMNII
KDRINKVYNL IKEGNSSINA AKAIMTTDTK PKEIAVEFEV NGKTVRVGGI AKGAGMIAPN
MLHATMLCFI TTDIEIDKES LTNILQKVVD KTFNNISVDG DTSTNDTVFV LANGLSGVNY
EECGEEFENA LLYVCRELAK MIVKDGEGAT KFMEVVVKGA KTEEDAVKAS KAIVNSLLVK
TAVFGGDPNW GRIVAAVGYS GADFNPEVVD VILSNYKDEV YLVKDGIPLA DEGTEELKKA
EEIMKSDEIK IVVDLKMGEF ENVCYGCDLS YEYVRINAEY TT
