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Database: UniProt
Entry: A0A0Q6DX60_9MICO
LinkDB: A0A0Q6DX60_9MICO
Original site: A0A0Q6DX60_9MICO 
ID   A0A0Q6DX60_9MICO        Unreviewed;       385 AA.
AC   A0A0Q6DX60;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   11-DEC-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=ASG45_08015 {ECO:0000313|EMBL:KQT74509.1};
OS   Microbacterium sp. Leaf436.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Microbacterium.
OX   NCBI_TaxID=1736377 {ECO:0000313|EMBL:KQT74509.1, ECO:0000313|Proteomes:UP000051552};
RN   [1] {ECO:0000313|EMBL:KQT74509.1, ECO:0000313|Proteomes:UP000051552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf436 {ECO:0000313|EMBL:KQT74509.1,
RC   ECO:0000313|Proteomes:UP000051552};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT74509.1, ECO:0000313|Proteomes:UP000051552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf436 {ECO:0000313|EMBL:KQT74509.1,
RC   ECO:0000313|Proteomes:UP000051552};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC       version of arginine biosynthesis: the synthesis of N-acetylglutamate
CC       from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by
CC       transacetylation between N(2)-acetylornithine and glutamate.
CC       {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; EC=2.3.1.35;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01106};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC         Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01106};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC       and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine
CC       (cyclic): step 1/1. {ECO:0000256|HAMAP-Rule:MF_01106}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       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 biosynthetic
CC       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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQT74509.1}.
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DR   EMBL; LMRB01000002; KQT74509.1; -; Genomic_DNA.
DR   RefSeq; WP_055835261.1; NZ_LMRB01000002.1.
DR   EnsemblBacteria; KQT74509; KQT74509; ASG45_08015.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000051552; 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   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   CHAIN           1..180
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT                   /id="PRO_5023240840"
FT   CHAIN           181..385
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT                   /id="PRO_5023240841"
FT   ACT_SITE        181
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         148
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         170
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         181
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         261
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         380
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         385
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   SITE            109
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   SITE            110
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   SITE            180..181
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
SQ   SEQUENCE   385 AA;  39558 MW;  FC3F336974D6FF50 CRC64;
     MSVTVPAGFE AAGVAVGLKP TGARDVAVVV NRGPLKVGAA VFTSNRAKAN PILWSEQVVK
     DGVIEAVVLN SGGANCFTGA FGFQTTHQTA ERAAELLGVG AGDVVVCSTG LIGTGDEVFR
     AKVLAGVDTG IATLSTDGGE DASLAIMTTD SRPKRAVHVG DGWSIGAMAK GAGMLAPGLA
     TMLVVVTTDV VLDADEADAA LRAATRVSFD RLDSDGCMST NDQVTLLASG ASGIRVPADQ
     FATALAAVCD DLAAQLQGDA EGASHDITIR VTQAASEDEA VEVGRSIARN NLFKAAVFGN
     DPNWGRVLAA IGTTSARFDP YDVDVWMNGV RVCTAGGPDR PREDVDLTPR ALDLVVDLRA
     GSAEATIRTN DLTHDYVHEN SAYSS
//
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