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Arginine biosynthesis bifunctional protein ArgJ [Cleaved into: Arginine biosynthesis bifunctional protein ArgJ alpha chain; Arginine biosynthesis bifunctional protein ArgJ beta chain] [Includes: Glutamate N-acetyltransferase (EC 2.3.1.35) (Ornithine acetyltransferase) (OATase) (Ornithine transacetylase); Amino-acid acetyltransferase (EC 2.3.1.1) (N-acetylglutamate synthase) (AGSase)]

 A0A1D2QTL0_9GAMM        Unreviewed;       404 AA.
A0A1D2QTL0;
30-NOV-2016, integrated into UniProtKB/TrEMBL.
30-NOV-2016, sequence version 1.
27-SEP-2017, entry version 8.
RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000256|HAMAP-Rule:MF_01106};
Includes:
RecName: Full=Glutamate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
EC=2.3.1.35 {ECO:0000256|HAMAP-Rule:MF_01106};
AltName: Full=Ornithine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
Short=OATase {ECO:0000256|HAMAP-Rule:MF_01106};
AltName: Full=Ornithine transacetylase {ECO:0000256|HAMAP-Rule:MF_01106};
Includes:
RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_01106};
AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_01106};
Short=AGSase {ECO:0000256|HAMAP-Rule:MF_01106};
Contains:
RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000256|HAMAP-Rule:MF_01106};
Contains:
RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000256|HAMAP-Rule:MF_01106};
Name=argJ {ECO:0000256|HAMAP-Rule:MF_01106};
ORFNames=AB835_01240 {ECO:0000313|EMBL:ODS24917.1};
Candidatus Endobugula sertula (Bugula neritina bacterial symbiont).
Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
Cellvibrionaceae; Candidatus Endobugula.
NCBI_TaxID=62101 {ECO:0000313|EMBL:ODS24917.1};
[1] {ECO:0000313|EMBL:ODS24917.1}
NUCLEOTIDE SEQUENCE.
STRAIN=AB1-4 {ECO:0000313|EMBL:ODS24917.1};
PubMed=27590822;
Miller I.J., Vanee N., Fong S.S., Lim-Fong G.E., Kwan J.C.;
"Lack of overt genome reduction in the bryostatin-producing bryozoan
symbiont, 'Candidatus Endobugula sertula'.";
Appl. Environ. Microbiol. 0:0-0(2016).
-!- FUNCTION: Catalyzes two activities which are involved in the
cyclic version of arginine biosynthesis: the synthesis of N-
acetylglutamate from glutamate and acetyl-CoA as the acetyl donor,
and of ornithine by transacetylation between N(2)-acetylornithine
and glutamate. {ECO:0000256|HAMAP-Rule:MF_01106}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-
glutamate. {ECO:0000256|HAMAP-Rule:MF_01106}.
-!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L-
ornithine + N-acetyl-L-glutamate. {ECO:0000256|HAMAP-
Rule:MF_01106}.
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-
acetyl-L-ornithine (cyclic): step 1/1. {ECO:0000256|HAMAP-
Rule:MF_01106}.
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
acetyl-L-ornithine from L-glutamate: step 1/4. {ECO:0000256|HAMAP-
Rule:MF_01106}.
-!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
{ECO:0000256|HAMAP-Rule:MF_01106}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106}.
-!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e.,
capable of catalyzing only the fifth step of the arginine
biosynthetic pathway. {ECO:0000256|HAMAP-Rule:MF_01106}.
-!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|HAMAP-
Rule:MF_01106}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01106}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ODS24917.1}.
-----------------------------------------------------------------------
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EMBL; MDLC01000003; ODS24917.1; -; Genomic_DNA.
UniPathway; UPA00068; UER00106.
UniPathway; UPA00068; UER00111.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd02152; OAT; 1.
Gene3D; 3.60.70.12; -; 1.
HAMAP; MF_01106; ArgJ; 1.
InterPro; IPR002813; Arg_biosynth_ArgJ.
InterPro; IPR016117; ArgJ-like_dom.
PANTHER; PTHR23100; PTHR23100; 1.
Pfam; PF01960; ArgJ; 1.
SUPFAM; SSF56266; SSF56266; 1.
TIGRFAMs; TIGR00120; ArgJ; 1.
3: Inferred from homology;
Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106};
Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106};
Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_01106};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
Transferase {ECO:0000256|HAMAP-Rule:MF_01106}.
ACT_SITE 189 189 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_01106}.
BINDING 152 152 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01106}.
BINDING 178 178 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01106}.
BINDING 189 189 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01106}.
BINDING 275 275 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01106}.
BINDING 399 399 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01106}.
SITE 115 115 Involved in the stabilization of negative
charge on the oxyanion by the formation
of the oxyanion hole. {ECO:0000256|HAMAP-
Rule:MF_01106}.
SITE 116 116 Involved in the stabilization of negative
charge on the oxyanion by the formation
of the oxyanion hole. {ECO:0000256|HAMAP-
Rule:MF_01106}.
SITE 188 189 Cleavage; by autolysis.
{ECO:0000256|HAMAP-Rule:MF_01106}.
SEQUENCE 404 AA; 43168 MW; C317C845522CA6AD CRC64;
MAVGILNFPT MPIIDGVQLN AISAGIKNNK CHDLVLIALP DSAKTAGVFT QNAFCAAPVV
VCKSHLSYQS RYLIINSGNA NACTGEQGLR SAISCCEALA QSTNVNTTQV LPFSTGVIGD
PLPVEKITAA IPELLSGLSE DHWQLAAKGM MTTDTRPKGA TASFDYCGET FVVNGICKGA
GMIKPNMATM LGFVVSNANI SQSLLEQLSR DAVNQSFNRI TIDGDTSTND SCMLMTTCTT
SQIIDNVNEP LYTLFKDAVT SVYQTLAQAI IRDGEGATKF VTLQIEEGAN ANECLQVAYA
IAHSPLVKTA LFASDPNWGR IAAAIGYAGI QQLNVDLIRV YLNDTLIIEN GGRSASYTEA
AGQAAMDQAE ILLRVCLGRG DQQEVLWTTD LSHEYVTINA EYRN


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