ID A8LE41_FRASN Unreviewed; 390 AA.
AC A8LE41;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 13-NOV-2019, entry version 91.
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=Franean1_1738 {ECO:0000313|EMBL:ABW11176.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia;
OC unclassified Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW11176.1, ECO:0000313|Proteomes:UP000001313};
RN [1] {ECO:0000313|Proteomes:UP000001313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CP000820; ABW11176.1; -; Genomic_DNA.
DR RefSeq; WP_020459348.1; NC_009921.1.
DR STRING; 298653.Franean1_1738; -.
DR EnsemblBacteria; ABW11176; ABW11176; Franean1_1738.
DR KEGG; fre:Franean1_1738; -.
DR eggNOG; ENOG4105C5V; Bacteria.
DR eggNOG; COG1364; LUCA.
DR HOGENOM; HOG000022797; -.
DR KO; K00620; -.
DR OMA; GMIAPNM; -.
DR OrthoDB; 1083409at2; -.
DR BioCyc; FSP298653:G1G9X-1736-MONOMER; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000001313; 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:ABW11176.1};
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:UP000001313};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW Reference proteome {ECO:0000313|Proteomes:UP000001313};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW ECO:0000313|EMBL:ABW11176.1}.
FT ACT_SITE 186 186 Nucleophile. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 146 146 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 175 175 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 186 186 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 266 266 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 385 385 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 390 390 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 185 186 Cleavage; by autolysis.
FT {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ SEQUENCE 390 AA; 39275 MW; 9D7721BD5DF52D07 CRC64;
MSVTAARGFR AAGAAAGLKP SGRPDVALVV NDGPADAAAG VFTRNRVQAA PVLWTRQVLT
TGRLRAVVLN SGGANACTGP EGFADTHATA EHVGAALGIG AGEVAVCSTG LIGVRLPMDL
LLPGVTQAVV ALSPAGGDAA AEAIRTTDTV AKQAVRTSTS GAAGDGVVTV GGMGKGAAML
APSLATMLVV VTTDAVADSA TLDRVVREAC RTTFERVDSD GCLSTNDTVL LLASGASGRS
LPEAELTELV TAVCDDLAGQ MLGDAEGSTK TISITVTGAA SEADALEVGR SVARNNLLKC
ALYGKDPNWG RVLAAIGTTS AAFEPDRLDV TMNGIQVCRG GAPGEPRELV DLGGREISIV
ADLHAGDVEL TVRTNDLTDG YVYENSAYST
//
