ARGJ_YEAST
ID ARGJ_YEAST Reviewed; 441 AA.
AC Q04728; D6VZN6; Q04682; Q09168;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03124};
DE AltName: Full=Extracellular mutant protein 40;
DE Includes:
DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE Short=GAT {ECO:0000255|HAMAP-Rule:MF_03124};
DE EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_03124};
DE AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE Short=OATase {ECO:0000255|HAMAP-Rule:MF_03124};
DE AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_03124};
DE Includes:
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_03124};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_03124};
DE Short=AGS {ECO:0000255|HAMAP-Rule:MF_03124};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_03124};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_03124};
DE Flags: Precursor;
GN Name=ARG7 {ECO:0000255|HAMAP-Rule:MF_03124}; Synonyms=ECM40;
GN OrderedLocusNames=YMR062C; ORFNames=YM9916.01C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RA Li W., Fitzgerald M.C., Neigeborn L., Mitchell A.P.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 9-28 AND 215-234, AND CHARACTERIZATION.
RX PubMed=7705341; DOI=10.1111/j.1432-1033.1995.tb20262.x;
RA Liu Y., van Heeswijck R., Hoej P., Hoogenraad N.;
RT "Purification and characterization of ornithine acetyltransferase from
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 228:291-296(1995).
RN [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=9428669; DOI=10.1111/j.1432-1033.1997.0232a.x;
RA Crabeel M., Abadjieva A., Hilven P., Desimpelaere J., Soetens O.;
RT "Characterization of the Saccharomyces cerevisiae ARG7 gene encoding
RT ornithine acetyltransferase, an enzyme also endowed with acetylglutamate
RT synthase activity.";
RL Eur. J. Biochem. 250:232-241(1997).
RN [6]
RP PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF THR-215.
RX PubMed=10753950; DOI=10.1074/jbc.275.15.11361;
RA Abadjieva A., Hilven P., Pauwels K., Crabeel M.;
RT "The yeast ARG7 gene product is autoproteolyzed to two subunit peptides,
RT yielding active ornithine acetyltransferase.";
RL J. Biol. Chem. 275:11361-11367(2000).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17651682; DOI=10.1016/j.ab.2007.06.032;
RA Takahara K., Akashi K., Yokota A.;
RT "Continuous spectrophotometric assays for three regulatory enzymes of the
RT arginine biosynthetic pathway.";
RL Anal. Biochem. 368:138-147(2007).
CC -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC version of arginine biosynthesis: the synthesis of acetylglutamate from
CC glutamate and acetyl-CoA, and of ornithine by transacetylation between
CC acetylornithine and glutamate. {ECO:0000255|HAMAP-Rule:MF_03124,
CC ECO:0000269|PubMed:9428669}.
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:0000255|HAMAP-Rule:MF_03124};
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:0000255|HAMAP-Rule:MF_03124};
CC -!- ACTIVITY REGULATION: Inhibited by ornithine.
CC {ECO:0000269|PubMed:9428669}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.4 mM for glutamate {ECO:0000269|PubMed:17651682};
CC KM=2.8 mM for N-acetylornithine {ECO:0000269|PubMed:17651682};
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. {ECO:0000255|HAMAP-Rule:MF_03124}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03124, ECO:0000269|PubMed:14576278}.
CC -!- PTM: The alpha and beta chains are autoproteolytically processed from a
CC single precursor protein within the mitochondrion. {ECO:0000255|HAMAP-
CC Rule:MF_03124, ECO:0000269|PubMed:10753950}.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
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DR EMBL; U90438; AAB49897.1; -; Genomic_DNA.
DR EMBL; Z48952; CAA88787.1; -; Genomic_DNA.
DR EMBL; Z49703; CAA89772.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09960.1; -; Genomic_DNA.
DR PIR; S52822; S52822.
DR RefSeq; NP_013778.1; NM_001182560.1.
DR AlphaFoldDB; Q04728; -.
DR SMR; Q04728; -.
DR BioGRID; 35237; 58.
DR IntAct; Q04728; 1.
DR STRING; 4932.YMR062C; -.
DR MEROPS; T05.001; -.
DR iPTMnet; Q04728; -.
DR MaxQB; Q04728; -.
DR PaxDb; Q04728; -.
DR PRIDE; Q04728; -.
DR EnsemblFungi; YMR062C_mRNA; YMR062C; YMR062C.
DR GeneID; 855084; -.
DR KEGG; sce:YMR062C; -.
DR SGD; S000004666; ARG7.
DR VEuPathDB; FungiDB:YMR062C; -.
DR eggNOG; KOG2786; Eukaryota.
DR HOGENOM; CLU_027172_1_0_1; -.
DR InParanoid; Q04728; -.
DR OMA; DYVHENS; -.
DR BioCyc; MetaCyc:YMR062C-MON; -.
DR BioCyc; YEAST:YMR062C-MON; -.
DR SABIO-RK; Q04728; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR PRO; PR:Q04728; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04728; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IDA:SGD.
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 GO; GO:0006592; P:ornithine biosynthetic process; IDA:SGD.
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; Direct protein sequencing; Mitochondrion;
KW Multifunctional enzyme; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..8
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124,
FT ECO:0000269|PubMed:7705341"
FT CHAIN 9..214
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT /id="PRO_0000002283"
FT CHAIN 215..441
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT /id="PRO_0000002284"
FT ACT_SITE 215
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 436
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT SITE 136
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT SITE 137
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT SITE 214..215
FT /note="Cleavage; by autolysis"
FT MUTAGEN 215
FT /note="T->A: Blocks autocatalytic processing of the
FT precursor protein."
FT /evidence="ECO:0000269|PubMed:10753950"
SQ SEQUENCE 441 AA; 47849 MW; 7AC03B7A72E3CE46 CRC64;
MRISSTLLQR SKQLIDKYAL YVPKTGSFPK GFEVGYTASG VKKNGSLDLG VILNTNKSRP
STAAAVFTTN KFKAAPVLTS KKVLETARGK NINAIVVNSG CANSVTGDLG MKDAQVMIDL
VNDKIGQKNS TLVMSTGVIG QRLQMDKIST GINKIFGEEK FGSDFNSWLN VAKSICTTDT
FPKLVTSRFK LPSGTEYTLT GMAKGAGMIC PNMATLLGFI VTDLPIESKA LQKMLTFATT
RSFNCISVDG DMSTNDTICM LANGAIDTKE INEDSKDFEQ VKLQVTEFAQ RLAQLVVRDG
EGSTKFVTVN VKNALHFEDA KIIAESISNS MLVKTALYGQ DANWGRILCA IGYAKLNDLK
SLDVNKINVS FIATDNSEPR ELKLVANGVP QLEIDETRAS EILALNDLEV SVDLGTGDQA
AQFWTCDLSH EYVTINGDYR S
