ARGJ_CITLA
ID ARGJ_CITLA Reviewed; 460 AA.
AC Q3C251;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
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 Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Citrullus.
OX NCBI_TaxID=3654;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-41 AND 239-273,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16218965; DOI=10.1111/j.1742-4658.2005.04933.x;
RA Takahara K., Akashi K., Yokota A.;
RT "Purification and characterization of glutamate N-acetyltransferase
RT involved in citrulline accumulation in wild watermelon.";
RL FEBS J. 272:5353-5364(2005).
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:16218965}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 mM for N(2)-acetyl-L-ornithine (at pH 7.0);
CC KM=17.8 mM for L-glutamate (at pH 7.0);
CC pH dependence:
CC Optimum pH is 7.0.;
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.;
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 -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
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DR EMBL; AB212224; BAE46903.1; -; mRNA.
DR AlphaFoldDB; Q3C251; -.
DR SMR; Q3C251; -.
DR MEROPS; T05.002; -.
DR SABIO-RK; Q3C251; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR GO; GO:0009507; C:chloroplast; 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; Chloroplast; Direct protein sequencing;
KW Multifunctional enzyme; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..26
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124,
FT ECO:0000269|PubMed:16218965"
FT CHAIN 27..238
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /id="PRO_0000397976"
FT CHAIN 239..460
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /id="PRO_0000397977"
FT ACT_SITE 239
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 460
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT SITE 163
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 164
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 238..239
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
SQ SEQUENCE 460 AA; 48203 MW; 50AA2399AC517835 CRC64;
MYLSVPHYPS LKFTAFQSHK RNFRVFAVAT NEAANYLPEA PILIPDGPWK QIDGGVTAAK
GFKAAGLYGG LRAKGEKPDL ALVTCDVDAI SAGAFTKNVV AAAPVLYCKK ALDISETARA
VLINAGQANA ATGDAGYQDV IECVNNLSKI LQIRPEEILV ESTGVIGHRI KKDALLNSLP
QLVRSLSSSV GGAASAAVAI TTTDLVSKSV AIESQVGGST IRIGGMAKGS GMIHPNMATM
LGVVTTDAVV ACDVWRKMVQ ISVDRSFNQI TVDGDTSTND TVIALSSGLS GFNSNIISSL
KSREAGQLQE CLDVVMQGLA KSIAWDGEGA TCLIEITVSG ASTEAEAAKV ARSVAGSSLV
KSAIYGRDPN WGRIAAAAGY AGVPFDQMKL KVSLGNILLM DGGEPQSFDR AAASNYLRRA
GETHDTVRIF ISIGDGQGEG RAWGCDLSYD YVKINAEYTT
