ID A0A1G6SDM7_9ACTN Unreviewed; 384 AA.
AC A0A1G6SDM7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN05216270_10243 {ECO:0000313|EMBL:SDD15020.1};
OS Glycomyces harbinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Glycomyces.
OX NCBI_TaxID=58114 {ECO:0000313|EMBL:SDD15020.1, ECO:0000313|Proteomes:UP000198949};
RN [1] {ECO:0000313|EMBL:SDD15020.1, ECO:0000313|Proteomes:UP000198949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3516 {ECO:0000313|EMBL:SDD15020.1,
RC ECO:0000313|Proteomes:UP000198949};
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 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|ARBA:ARBA00000498, ECO:0000256|HAMAP-
CC 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|ARBA:ARBA00011475, 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|ARBA:ARBA00006774,
CC ECO:0000256|HAMAP-Rule:MF_01106}.
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DR EMBL; FNAD01000002; SDD15020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6SDM7; -.
DR STRING; 58114.SAMN05216270_10243; -.
DR OrthoDB; 9804242at2; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000198949; 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; ArgJ beta chain, C-terminal domain; 1.
DR Gene3D; 3.60.70.12; L-amino peptidase D-ALA esterase/amidase; 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 NCBIfam; TIGR00120; ArgJ; 1.
DR PANTHER; PTHR23100; ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ; 1.
DR PANTHER; PTHR23100:SF0; ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ, MITOCHONDRIAL; 1.
DR Pfam; PF01960; ArgJ; 1.
DR SUPFAM; SSF56266; DmpA/ArgJ-like; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01106}; Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW Rule:MF_01106}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01106}.
FT CHAIN 1..179
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT /id="PRO_5023235407"
FT CHAIN 180..384
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT /id="PRO_5023235406"
FT ACT_SITE 180
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 384
FT /ligand="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 179..180
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
SQ SEQUENCE 384 AA; 38523 MW; 0DB85774EDD23449 CRC64;
MTITTPKGFK ASGVTAGLKA SGNPDMALVV NDGPLQVAAG RFTGNRVKAA PVKWSQQVLT
TGALKAVILN SGGANACTGA EGFQNTHATA EKTAELLGCG AVEVAVCSTG LIGEQLPMDK
LLPGVEAAAA ALSADGGEAA ATAIMTTDSV AKNAVVTSPA GWTIGGIAKG AGMLAPGLAT
MLVVLTTDAV IDQPLADAAI GTACRYSFDR LDSDGSMSTN DTVLLLASGA SGVEAAADEF
ITALTDLCKD LGKQLLGDAE GSTKDIAITV SGAATEDDAV EVGRCVARDS LVKTAMFGCD
PNWGRILAAV GVSKAPFDAD QVDVAVNGVQ ICKAGAAGDS RDLVDLKGRA VAIDIDLHNG
AAAATVWTND LSHDYVHENS AYST
//
