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Database: UniProt
Entry: A0A1C5I4U9_9ACTN
LinkDB: A0A1C5I4U9_9ACTN
Original site: A0A1C5I4U9_9ACTN 
ID   A0A1C5I4U9_9ACTN        Unreviewed;       390 AA.
AC   A0A1C5I4U9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   05-JUN-2019, entry version 20.
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=GA0074704_2891 {ECO:0000313|EMBL:SCG53159.1};
OS   Micromonospora siamensis.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=299152 {ECO:0000313|EMBL:SCG53159.1, ECO:0000313|Proteomes:UP000198210};
RN   [1] {ECO:0000313|EMBL:SCG53159.1, ECO:0000313|Proteomes:UP000198210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45097 {ECO:0000313|EMBL:SCG53159.1,
RC   ECO:0000313|Proteomes:UP000198210};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-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; LT607751; SCG53159.1; -; Genomic_DNA.
DR   BioCyc; GCF_900090305:GA0074704_RS14380-MONOMER; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000198210; Chromosome i.
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:UP000198210};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198210};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000313|EMBL:SCG53159.1}.
FT   ACT_SITE    186    186       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     153    153       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     175    175       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     186    186       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     266    266       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     385    385       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     390    390       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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:0000256|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:0000256|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        185    186       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ   SEQUENCE   390 AA;  39467 MW;  8C6E6AF927404E06 CRC64;
     MTVTTPRGFR AAGVAAGLKA SGAADVALVV NDGPDATVAG VFTANRVKAA PVLWTQQVVR
     GGVVRAVVLN SGGANACTGP AGFQDTHATA EHTAAALTGS SPRRRLGAGE VAVCSTGLIG
     ERLPMPKLLP GVRTAIRGLS RDGGAAAAEA IMTTDTRPKT TVARGAGFTV GGMAKGAGML
     APAMATMLCV LTTDAVAGPE ALDAALRAAT RVTFDRIDSD GCMSTNDTVL LLASGASGVE
     PTEDELATAV TAACHDLAQQ LIADAEGATK QIAIEVVGAA SEDDAVEVGR SVARNNLVKT
     ALFGNDPNWG RILAAVGTTT AAFEPDALDV AVNGIWVCRG GAAAEDRAKV DLTGRDVTIR
     IDLHVGDETA TVWTNDLSHA YVHENSAYST
//
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