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Database: UniProt
Entry: ARGJ_ACIAD
LinkDB: ARGJ_ACIAD
Original site: ARGJ_ACIAD 
ID   ARGJ_ACIAD              Reviewed;         406 AA.
AC   Q6FED8;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   13-NOV-2019, entry version 107.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              Short=OATase {ECO:0000255|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01106};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              Short=AGSase {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_01106};
GN   Name=argJ {ECO:0000255|HAMAP-Rule:MF_01106};
GN   OrderedLocusNames=ACIAD0650;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- FUNCTION: Catalyzes two activities which are involved in the
CC       cyclic version of arginine biosynthesis: the synthesis of N-
CC       acetylglutamate from glutamate and acetyl-CoA as the acetyl donor,
CC       and of ornithine by transacetylation between N(2)-acetylornithine
CC       and glutamate. {ECO:0000255|HAMAP-Rule:MF_01106}.
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;
CC         EC=2.3.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01106};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-
CC         glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01106};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-
CC       acetyl-L-ornithine (cyclic): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01106}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 1/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01106}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e.
CC       capable of catalyzing only the fifth step of the arginine
CC       biosynthetic pathway.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01106}.
DR   EMBL; CR543861; CAG67570.1; -; Genomic_DNA.
DR   RefSeq; WP_004919769.1; NC_005966.1.
DR   SMR; Q6FED8; -.
DR   STRING; 62977.ACIAD0650; -.
DR   MEROPS; T05.001; -.
DR   EnsemblBacteria; CAG67570; CAG67570; ACIAD0650.
DR   KEGG; aci:ACIAD0650; -.
DR   eggNOG; ENOG4105C5V; Bacteria.
DR   eggNOG; COG1364; LUCA.
DR   HOGENOM; HOG000022798; -.
DR   KO; K00620; -.
DR   OMA; GMIAPNM; -.
DR   OrthoDB; 1083409at2; -.
DR   BioCyc; ASP62977:ACIAD_RS02970-MONOMER; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00111.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Autocatalytic cleavage; Complete proteome; Cytoplasm;
KW   Multifunctional enzyme; Reference proteome; Transferase.
FT   CHAIN         1    189       Arginine biosynthesis bifunctional
FT                                protein ArgJ alpha chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_01106}.
FT                                /FTId=PRO_0000002093.
FT   CHAIN       190    406       Arginine biosynthesis bifunctional
FT                                protein ArgJ beta chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_01106}.
FT                                /FTId=PRO_0000002094.
FT   ACT_SITE    190    190       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     153    153       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     179    179       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     190    190       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     277    277       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     401    401       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     406    406       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        116    116       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        117    117       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        189    190       Cleavage; by autolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01106}.
SQ   SEQUENCE   406 AA;  43579 MW;  55FEE68AD5206727 CRC64;
     MAVGDVTMPH MHVVNGVKIG STEAYVRYPN RRDLVVFKFV EGSHVAGVFT QSAFAAAPVL
     VSKKHLAESA IRYLIINTGN ANAATGQTGV INAQKTCTKL AELAGVESSQ VLPFSTGVIG
     EQLPIERLLD GIQPALQDLK DDAWTEAAFG IMTTDTTPKG ASEQFELDGV VYTMTGISKG
     AGMIRPNMAT MLSFVATDAP ISQSLVQTLL KTTVEQSFNR ITIDGDTSTN DSCIFVATGQ
     AGGVEISSEQ DPRYSKILEI LQRIMNRLAQ LIVRDGEGAT KFITVAVEGG ENTQECCDVA
     YSIAHSPLIK TAVFASDPNW GRIVMAIGKA GVPQLDVSKV QVWLDDVQIC RDGGAAADYT
     EEQGARVMAQ AEMTIRVDLG RGTAKDTVYT CDLSYDYVKI NADYRS
//
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