ID A0LUC4_ACIC1 Unreviewed; 384 AA.
AC A0LUC4;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 05-JUN-2019, entry version 101.
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 OrderedLocusNames=Acel_1262 {ECO:0000313|EMBL:ABK53034.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / 11B).
OC Bacteria; Actinobacteria; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53034.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / 11B {ECO:0000313|Proteomes:UP000008221};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Berry A.M., Adney W.S., Normand P.,
RA Leu D., Pujic P., Richardson P.;
RT "Complete sequence of Acidothermus cellulolyticus 11B.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABK53034.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / 11B {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S.,
RA Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
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; CP000481; ABK53034.1; -; Genomic_DNA.
DR RefSeq; WP_011720097.1; NC_008578.1.
DR STRING; 351607.Acel_1262; -.
DR EnsemblBacteria; ABK53034; ABK53034; Acel_1262.
DR KEGG; ace:Acel_1262; -.
DR eggNOG; ENOG4105C5V; Bacteria.
DR eggNOG; COG1364; LUCA.
DR HOGENOM; HOG000022797; -.
DR KO; K00620; -.
DR OMA; GMIAPNM; -.
DR OrthoDB; 1083409at2; -.
DR BioCyc; ACEL351607:G1G7K-1292-MONOMER; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000008221; 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 ECO:0000313|EMBL:ABK53034.1};
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:UP000008221};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW ECO:0000313|EMBL:ABK53034.1}.
FT ACT_SITE 180 180 Nucleophile. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 146 146 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 169 169 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 180 180 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 260 260 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 379 379 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 384 384 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT SITE 109 109 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 110 110 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 179 180 Cleavage; by autolysis.
FT {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ SEQUENCE 384 AA; 38874 MW; 3BA825EC50F3D627 CRC64;
MSVTTPAGFR AAGVASGIKE SGRPDVALVV NDGPRSAAAA RVTRNRIKAA PVLWTEQVAR
GGRIGAVVLN SGNANACTGP DGFADVHHTA ELVGDLLGIG AADVAVCSTG IIGVRLPTDR
LFAGIRAAHA ALDPDGGPAA AEAIMTTDTV PKQVARTASS GWRLGGMAKG AGMLAPELAT
MLVVLTTDAD LEPHVLDAAL GAATAVTFER LDTDGCLSTN DTVVLLASGA SGVRPEPEEF
TAVLVDACAD LAHQLAADAE GAGKLITVEV RGAASEPDAV QVARAVARSN LVKCAIGGGD
PNWGRILAAI GTTTARFEPD GIDVAINGVQ VCRRSAIGED RAKVDLSGRD VTITIELHAG
AATARLLTTD LTAAYVHENS AYST
//
