ARGJ3_STRCL
ID ARGJ3_STRCL Reviewed; 393 AA.
AC P0DJQ6; Q53940;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ 3 {ECO:0000255|HAMAP-Rule:MF_01106};
DE Includes:
DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_01106};
DE AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Short=OATase {ECO:0000255|HAMAP-Rule:MF_01106};
DE AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Includes:
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01106};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Short=AGSase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_01106};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_01106};
GN Name=argJ3 {ECO:0000255|HAMAP-Rule:MF_01106}; Synonyms=oat2;
OS Streptomyces clavuligerus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1901;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC 3585 / VKM Ac-602;
RX PubMed=10681345; DOI=10.1128/aac.44.3.720-726.2000;
RA Jensen S.E., Elder K.J., Aidoo K.A., Paradkar A.S.;
RT "Enzymes catalyzing the early steps of clavulanic acid biosynthesis are
RT encoded by two sets of paralogous genes in Streptomyces clavuligerus.";
RL Antimicrob. Agents Chemother. 44:720-726(2000).
RN [2]
RP PRESENCE OF PARALOGS.
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC 3585 / VKM Ac-602;
RX PubMed=14982786; DOI=10.1128/aac.48.3.930-939.2004;
RA Tahlan K., Park H.-U., Wong A., Beatty P.H., Jensen S.E.;
RT "Two sets of paralogous genes encode the enzymes involved in the early
RT stages of clavulanic acid and clavam metabolite biosynthesis in
RT Streptomyces clavuligerus.";
RL Antimicrob. Agents Chemother. 48:930-939(2004).
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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_01106}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000255|HAMAP-Rule:MF_01106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC Rule:MF_01106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U87786; AAF86622.1; -; Genomic_DNA.
DR RefSeq; WP_003952513.1; NZ_CP027858.1.
DR AlphaFoldDB; P0DJQ6; -.
DR SMR; P0DJQ6; -.
DR STRING; 443255.SCLAV_4193; -.
DR eggNOG; COG1364; Bacteria.
DR OrthoDB; 1083409at2; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
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; Amino-acid biosynthesis; Arginine biosynthesis;
KW Autocatalytic cleavage; Cytoplasm; Multifunctional enzyme; Transferase.
FT CHAIN 1..180
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT /id="PRO_0000419086"
FT CHAIN 181..393
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT /id="PRO_0000419087"
FT ACT_SITE 181
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT SITE 111
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT SITE 112
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT SITE 180..181
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
SQ SEQUENCE 393 AA; 41608 MW; 951ECEE6B9664E48 CRC64;
MSDSTPKTPR GFVVHTAPVG LADDGRDDFT VLASTAPATV SAVFTRSRFA GPSVVLCREA
VADGQARGVV VLARNANVAT GLEGEENARE VREAVARALG LPEGEMLIAS TGVIGRQYPM
ESIREHLKTL EWPAGEGGFD RAARAIMTTD TRPKEVRVSV GGATLVGIAK GVGMLEPDMA
TLLTFFATDA RLDPAEQDRL FRRVMDRTFN AVSIDTDTST SDTAVLFANG LAGEVDAGEF
EEALHTAALA LVKDIASDGE GAAKLIEVQV TGARDDAQAK RVGKTVVNSP LVKTAVHGCD
PNWGRVAMAI GKCSDDTDID QERVTIRFGE VEVYPPKARG DQADDALRAA VAEHLRGDEV
VIGIDLAIAD GAFTVYGCDL TEGYVRLNSE YTT
