ARGJ1_SCLS1
ID ARGJ1_SCLS1 Reviewed; 419 AA.
AC A7E5P6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ 1, mitochondrial;
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 1 alpha chain;
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ 1 beta chain;
DE Flags: Precursor;
GN ORFNames=SS1G_00621;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
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}.
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; CH476621; EDN91218.1; -; Genomic_DNA.
DR RefSeq; XP_001598532.1; XM_001598482.1.
DR AlphaFoldDB; A7E5P6; -.
DR SMR; A7E5P6; -.
DR STRING; 665079.A7E5P6; -.
DR MEROPS; T05.001; -.
DR EnsemblFungi; EDN91218; EDN91218; SS1G_00621.
DR GeneID; 5494409; -.
DR KEGG; ssl:SS1G_00621; -.
DR eggNOG; KOG2786; Eukaryota.
DR HOGENOM; CLU_027172_1_0_1; -.
DR InParanoid; A7E5P6; -.
DR OMA; DYVHENS; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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; 2.
DR Pfam; PF01960; ArgJ; 1.
DR SUPFAM; SSF56266; SSF56266; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW Autocatalytic cleavage; Mitochondrion; Multifunctional enzyme;
KW Reference proteome; Transferase.
FT CHAIN 1..187
FT /note="Arginine biosynthesis bifunctional protein ArgJ 1
FT alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000398108"
FT CHAIN 188..419
FT /note="Arginine biosynthesis bifunctional protein ArgJ 1
FT beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000398109"
FT ACT_SITE 188
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 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT SITE 165
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 166
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 187..188
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
SQ SEQUENCE 419 AA; 44219 MW; CF1A6CFD8A5B9A14 CRC64;
MVINAGAKLS IARLIRPTAS YHPAIGGIRY YSAPPESTIP AAKLKYIPTS GTYPQGFLVS
GTYVGVKPTN KSTPDLAFLA SEIPCAAAAV FTKNKFQAAP VTVSRKMLQR RENAGIRSVI
INSGCANAVT GKGGMEDAEK MVAEADRCYH APKDGKGGSS IVMSTGVIGQ RMAGMTKGAG
MIHPNMATLL GMIATDAPIA PALLPSLLKN AVDKSFNSIS IDGDTSTNDT VAVLANGVAG
GKEVTSESSK DHAAFQKVLT EFAIDLAKLV VRDGEGATKF VTIRVTEAPS EIGARKIAST
IARSPLVKTA LYGKDANWGR ILCATGYSQI SEPGEPINKV PEIVPEKTSV SFIPSDGSPE
LKLLVNGEPE SVDETRAAEI LEHEDLEILI NLGGGKEEAV YWTCDFSHEY VTINGDYRT
