ARGJ_ORYSJ
ID ARGJ_ORYSJ Reviewed; 463 AA.
AC Q10N79; A0A0N7KH15; Q10N78;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
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;
GN OrderedLocusNames=Os03g0279400, LOC_Os03g17120;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q10N79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q10N79-2; Sequence=VSP_039734, VSP_039735;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK101851; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DP000009; ABF95293.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF95294.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11646.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83553.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83554.1; -; Genomic_DNA.
DR EMBL; AK101851; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK106253; BAG97658.1; -; mRNA.
DR RefSeq; XP_015630479.1; XM_015774993.1. [Q10N79-1]
DR AlphaFoldDB; Q10N79; -.
DR SMR; Q10N79; -.
DR STRING; 4530.OS03T0279400-02; -.
DR MEROPS; T05.002; -.
DR PaxDb; Q10N79; -.
DR PRIDE; Q10N79; -.
DR EnsemblPlants; Os03t0279400-01; Os03t0279400-01; Os03g0279400. [Q10N79-2]
DR EnsemblPlants; Os03t0279400-02; Os03t0279400-02; Os03g0279400. [Q10N79-1]
DR GeneID; 4332434; -.
DR Gramene; Os03t0279400-01; Os03t0279400-01; Os03g0279400. [Q10N79-2]
DR Gramene; Os03t0279400-02; Os03t0279400-02; Os03g0279400. [Q10N79-1]
DR KEGG; osa:4332434; -.
DR eggNOG; KOG2786; Eukaryota.
DR HOGENOM; CLU_027172_1_1_1; -.
DR InParanoid; Q10N79; -.
DR OMA; DYVHENS; -.
DR OrthoDB; 934513at2759; -.
DR PlantReactome; R-OSA-1119263; Arginine biosynthesis.
DR PlantReactome; R-OSA-1119622; Arginine biosynthesis II (acetyl cycle).
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10N79; OS.
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; Alternative splicing; Amino-acid biosynthesis;
KW Arginine biosynthesis; Autocatalytic cleavage; Chloroplast;
KW Multifunctional enzyme; Plastid; Reference proteome; Transferase.
FT CHAIN 1..243
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT /id="PRO_0000397980"
FT CHAIN 244..463
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT /id="PRO_0000397981"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT SITE 168
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 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 243..244
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT VAR_SEQ 365
FT /note="A -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_039734"
FT VAR_SEQ 366..463
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_039735"
SQ SEQUENCE 463 AA; 47853 MW; EAFF8EC808387D51 CRC64;
MPPPSLLLLH PRTPLPHHHR SSFRTSSPRP SRMVCAAAEG FISAAPILLP DGPWKQVEGG
VTAAKGFKAA GIYGGLRAKG EKPDLALVAC DVDATVAGAF TTNVVAAAPV LYCKRVLNSS
KTARAVLINA GQANAATGDA GYQDTVDSAD AVAKLLNVST NDILIQSTGV IGQRIKKEAL
VNSLHRLVGS LSSSIEGANS AAVAITTTDL VSKSIAVQTE IGGVPIKIGG MAKGSGMIHP
NMATMLGVLT TDAQVSSDVW REMVRTSVSR SFNQITVDGD TSTNDCVIAL ASGLSGLSSI
LTHDSTEAQQ FQACLDAVMQ GLAKSIAWDG EGATCLIEVT VAGANNEAEA AKIARSVASS
SLVKAAVFGR DPNWGRIACS VGYSGIQFDA DQLDISLGAI PLMKNGQPLP FDRSAASKYL
KDAGDIHGTV NIDVSVGRGG GSGKAWGCDL SYKYVEINAE YTT
