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Database: UniProt
Entry: A0A1I3N2B9_9BRAD
LinkDB: A0A1I3N2B9_9BRAD
Original site: A0A1I3N2B9_9BRAD 
ID   A0A1I3N2B9_9BRAD        Unreviewed;       413 AA.
AC   A0A1I3N2B9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-NOV-2019, entry version 12.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.35 {ECO:0000256|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              Short=OATase {ECO:0000256|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine transacetylase {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_01106};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              Short=AGSase {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000256|HAMAP-Rule:MF_01106};
GN   Name=argJ {ECO:0000256|HAMAP-Rule:MF_01106};
GN   ORFNames=SAMN05216525_117115 {ECO:0000313|EMBL:SFJ03341.1};
OS   Bradyrhizobium sp. Gha.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=1855318 {ECO:0000313|EMBL:SFJ03341.1, ECO:0000313|Proteomes:UP000199284};
RN   [1] {ECO:0000313|EMBL:SFJ03341.1, ECO:0000313|Proteomes:UP000199284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gha {ECO:0000313|EMBL:SFJ03341.1,
RC   ECO:0000313|Proteomes:UP000199284};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-
CC       Rule:MF_01106}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000256|HAMAP-Rule:MF_01106}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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. {ECO:0000256|HAMAP-Rule:MF_01106}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|HAMAP-
CC       Rule:MF_01106}.
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DR   EMBL; FOQM01000017; SFJ03341.1; -; Genomic_DNA.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000199284; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199284};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000313|EMBL:SFJ03341.1}.
FT   ACT_SITE    195    195       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     158    158       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     184    184       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     195    195       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     285    285       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     408    408       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     413    413       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   SITE        121    121       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000256|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        122    122       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000256|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        194    195       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ   SEQUENCE   413 AA;  42624 MW;  99712FCF0F9F689B CRC64;
     MSSSVSPLAP TNVPDMPVIA GVRLATAEAG IRYKNRTDVL LAIMDKGTAV AGVFTKSKCP
     SAPVEWCRAK LKGGKARALV VNSGNANAFT GKTGRASTAL TAKIAAKAVG CSESEIFLAS
     TGVIGEPLDA TKFDGVLGRL AVTAEAGDYL AAAKAIMTTD TFPKVATATV KLGKAKVTIN
     GMAKGAGMIA PDMATMLSFI FTDAPIAPAA LQALLKAGVE DTFNAVTIDG DTSTSDTLLA
     FATGAAAEHG APKISRASDP RLKAFTKAFN RILADLSEQV ARDGEGARKL VEITVEGAKT
     KASARKIAMS IANSPLVKTA IAGEDANWGR VVMAVGKAGE PADRDKLSIS FNGIRVAKSG
     ARDPDYDEAQ VSEAMKAPEI AIKVSLGLGK GRDRVLTCDL TKEYVAINGD YRS
//
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