ARGJ_MAIZE
ID ARGJ_MAIZE Reviewed; 464 AA.
AC C0PF72;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03124};
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;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73;
RA Yu Y., Currie J., Lomeli R., Angelova A., Collura K., Wissotski M.,
RA Campos D., Kudrna D., Golser W., Ashely E., Haller K., Descour A.,
RA Fernandes J., Soderlund C., Walbot V.;
RT "Maize full-length cDNA project.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- 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. {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
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DR EMBL; BT066941; ACN33838.1; -; mRNA.
DR RefSeq; NP_001169464.1; NM_001175993.1.
DR AlphaFoldDB; C0PF72; -.
DR SMR; C0PF72; -.
DR STRING; 4577.GRMZM2G044237_P03; -.
DR MEROPS; T05.002; -.
DR PaxDb; C0PF72; -.
DR PRIDE; C0PF72; -.
DR EnsemblPlants; Zm00001eb012670_T001; Zm00001eb012670_P001; Zm00001eb012670.
DR GeneID; 100383335; -.
DR Gramene; Zm00001eb012670_T001; Zm00001eb012670_P001; Zm00001eb012670.
DR KEGG; zma:100383335; -.
DR eggNOG; KOG2786; Eukaryota.
DR HOGENOM; CLU_027172_1_1_1; -.
DR OMA; DYVHENS; -.
DR OrthoDB; 934513at2759; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; C0PF72; baseline and differential.
DR Genevisible; C0PF72; ZM.
DR GO; GO:0009507; C:chloroplast; 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: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; 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 2: Evidence at transcript level;
KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW Autocatalytic cleavage; Chloroplast; Multifunctional enzyme; Plastid;
KW Reference proteome; Transferase.
FT CHAIN 1..244
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT /id="PRO_0000397994"
FT CHAIN 245..464
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT /id="PRO_0000397995"
FT ACT_SITE 245
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 459
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 464
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT SITE 169
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 170
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 244..245
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
SQ SEQUENCE 464 AA; 47952 MW; 4313164F81BA3EA5 CRC64;
MSPPSVLLLH SRIPLQPRPF RMNSRAAPSR VVVCSVASTE GFISAAPILL PDGPWKQVEG
GVTAAKGFKA AGIYSGLRAK GEKPDLALVA CDVDATVAGA FTTNVVAAAP VLYCKHVLST
SKTGRAVLIN AGQANAATGD LGYQDAVDSA DAVAKLLNVS TDNILIQSTG VIGQRIKKEA
LLNSLPRLVG SLSSSVQGAN SAAVAITTTD LVSKSIAVQT EIGGVAIRIG GMAKGSGMIH
PNMATMLGVL TTDAQVSSDV WREMIRMSVS RSFNQITVDG DTSTNDCVIA MASGLSGLSG
IQSLDSIEAQ QFQACLDAVM QSLAKSIAWD GEGATCLIEV TVSGANNEAE AAKIARSVAS
SSLVKAAIFG RDPNWGRIAC SVGYSGIQFD ANRLDISLGV IPLMKNGQPL PFDRLTASKY
LKDAGDAHGT VNIDISVGSG GGNGKAWGCD LSYKYVEINA EYTT
