ID A0A0C2AP31_9ACTN Unreviewed; 389 AA.
AC A0A0C2AP31;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 05-JUN-2019, entry version 31.
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=HY68_22255 {ECO:0000313|EMBL:KIF70700.1};
OS Streptomyces sp. AcH 505.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=352211 {ECO:0000313|EMBL:KIF70700.1, ECO:0000313|Proteomes:UP000031567};
RN [1] {ECO:0000313|EMBL:KIF70700.1, ECO:0000313|Proteomes:UP000031567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AcH 505 {ECO:0000313|EMBL:KIF70700.1,
RC ECO:0000313|Proteomes:UP000031567};
RA Tarkka M.T., Feldhahn L., Buscot F., Wubet T.;
RT "Genome sequence of the mycorrhiza helper bacterium Streptomyces.";
RL Submitted (NOV-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an
CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC preliminary data. {ECO:0000313|EMBL:KIF70700.1}.
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DR EMBL; JTIY01000001; KIF70700.1; -; Genomic_DNA.
DR RefSeq; WP_041991512.1; NZ_JTIY01000001.1.
DR EnsemblBacteria; KIF70700; KIF70700; HY68_22255.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000031567; 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 Complete proteome {ECO:0000313|Proteomes:UP000031567};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW Reference proteome {ECO:0000313|Proteomes:UP000031567};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01106}.
FT ACT_SITE 185 185 Nucleophile. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 152 152 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 174 174 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 185 185 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 265 265 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 384 384 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 389 389 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT SITE 115 115 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 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 184 185 Cleavage; by autolysis.
FT {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ SEQUENCE 389 AA; 39238 MW; D2DFF1B96BCD5432 CRC64;
MSVTAAQGFT AAGIAAGIKD SGGPDLALVV NTGPRTAAAG VFTSNRVKAA PVLWSEQVVK
GGAITAVVLN SGGANACTGP QGFQDTHATA EKAAEVLSAA GPAEHSAGEI AVASTGLIGV
PLPMDKLLPG VEKAAAALSE HGGEKAAIAI KTTDTVHKTA VAGGAGWTVG GMAKGAGMLA
PGLATMLVVL TTDADVETSA LDTALRAATR TTFDRVDSDG CMSTNDTVLL LASGAAGVTP
GYDEFAEAVR TVCADLARQL IGDAEGASKD IRIEVINAAT EDDAVEVGRS IARNNLLKCA
IHGEDPNWGR VLSAIGTTGA AFEPDQLNVA INGVWVCKNG AVGEDRDLVD MRYREVKITA
DLAAGGDSAV IWANDLTADY VHENSAYSS
//
