ID A0A0M4G3D9_9BACI Unreviewed; 405 AA.
AC A0A0M4G3D9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 05-JUN-2019, entry version 25.
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=AM500_21945 {ECO:0000313|EMBL:ALC92941.1};
OS Bacillus sp. FJAT-18017.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC92941.1, ECO:0000313|Proteomes:UP000060713};
RN [1] {ECO:0000313|EMBL:ALC92941.1, ECO:0000313|Proteomes:UP000060713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC92941.1,
RC ECO:0000313|Proteomes:UP000060713};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J.,
RA Ge C., Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) 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}.
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DR EMBL; CP012602; ALC92941.1; -; Genomic_DNA.
DR RefSeq; WP_053601834.1; NZ_CP012602.1.
DR EnsemblBacteria; ALC92941; ALC92941; AM500_21945.
DR PATRIC; fig|1705566.3.peg.4852; -.
DR OrthoDB; 1083409at2; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000060713; Chromosome.
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:UP000060713};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW Reference proteome {ECO:0000313|Proteomes:UP000060713};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01106}.
FT ACT_SITE 192 192 Nucleophile. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 155 155 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 181 181 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 192 192 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 278 278 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 400 400 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 405 405 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT SITE 119 119 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 120 120 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 191 192 Cleavage; by autolysis.
FT {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ SEQUENCE 405 AA; 43124 MW; F127B1EA2A5E9F94 CRC64;
MSGEKINQEE RGIYILPKGF KAGGMHCGLK RKKEDLGYIA SDIPATAAGV YTVNSFQAAP
LVVTQKSLEV EGKIQALIVN SGNANACTGK QGIEDAYEMQ SQFAKKLGIN DHLVAVTSTG
VIGELLPMEC LRNGIDKLLN PENQSPVNFQ KAILTTDTCI KSAFAQVEVD GSIVTISGAA
KGSGMIHPNM ATMLAFITTD ANIEQPALLS ALKESTNQTF NMITVDGDSS TNDMVLALAN
GLAGNEVLNE SHQDWQEFSS AFKTVCEALA KQIARDGEGA TKLIEVRVSG AQSLEAARAV
GKAVISSNLV KTAIYGEDAN WGRIVAAIGY SGIPVNPEDV EVTIGHFSVF ANGLPLPFSE
EEAKVYLSGE EVVIFIDLKQ GDAQASAWGC DLTYDYIKIN ASYRT
//
