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Database: UniProt
Entry: A0A0I9TDT5_9MYCO
LinkDB: A0A0I9TDT5_9MYCO
Original site: A0A0I9TDT5_9MYCO 
ID   A0A0I9TDT5_9MYCO        Unreviewed;       400 AA.
AC   A0A0I9TDT5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   05-JUN-2019, entry version 29.
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=ABW16_20225 {ECO:0000313|EMBL:KLO26275.1};
OS   Mycolicibacter heraklionensis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacter.
OX   NCBI_TaxID=512402 {ECO:0000313|EMBL:KLO26275.1, ECO:0000313|Proteomes:UP000036464};
RN   [1] {ECO:0000313|EMBL:KLO26275.1, ECO:0000313|Proteomes:UP000036464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Davo {ECO:0000313|EMBL:KLO26275.1,
RC   ECO:0000313|Proteomes:UP000036464};
RA   Greninger A.L., Cunningham G., Miller S.;
RT   "Genome sequence of Mycobacterium heraklionense Davo strain.";
RL   Submitted (MAY-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KLO26275.1}.
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DR   EMBL; LDPO01000023; KLO26275.1; -; Genomic_DNA.
DR   RefSeq; WP_047320987.1; NZ_LDPO01000023.1.
DR   EnsemblBacteria; KLO26275; KLO26275; ABW16_20225.
DR   PATRIC; fig|512402.5.peg.2590; -.
DR   OrthoDB; 1083409at2; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000036464; 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:UP000036464};
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}.
FT   ACT_SITE    196    196       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     185    185       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     196    196       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     276    276       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     395    395       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     400    400       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   SITE        123    123       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        124    124       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        195    196       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ   SEQUENCE   400 AA;  40920 MW;  ED599706893C72FB CRC64;
     MTDQKLLREQ GVTAPGGFRA AGIAAGIKVS GNPDLALVFN EGPDYAAAGV FTSNQVKAAP
     VLWSRQVLKA GRLRAVILNS GGANACTGPG GFQDTHSTAE AVAAALSDWG TETGAAEVAV
     CSTGLIGDRL PMDKLLAGVT EVVQAMAGGL VGGDEAARAI MTTDTVPKQV ALHHKGDWTV
     GGMAKGAGML APSLATMLVV LTTDAKVDAQ ALDTALRRAT AVTFDRLDID GSCSTNDTVL
     LLSSGASEIT PSQDDLDAAV LAVCDDLCAQ LQADAEGVTK RVSITVSGAG SDDDALIAAR
     IVARDSLVKT ALFGSDPNWG RVLAAVGMVP FTIDPDRITV SFNGSPVFHD GMPMPGAREV
     DLSGADIHVT VELNLGSGQA MVRTTDLSHA YVEENSAYSS
//
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