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Database: UniProt
Entry: F5XZS1_RAMTT
LinkDB: F5XZS1_RAMTT
Original site: F5XZS1_RAMTT 
ID   F5XZS1_RAMTT            Unreviewed;       408 AA.
AC   F5XZS1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   05-JUN-2019, entry version 55.
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   ECO:0000313|EMBL:AEG92100.1};
GN   OrderedLocusNames=Rta_10160 {ECO:0000313|EMBL:AEG92100.1};
OS   Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543
OS   / TTB310).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG92100.1, ECO:0000313|Proteomes:UP000008385};
RN   [1] {ECO:0000313|Proteomes:UP000008385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC   {ECO:0000313|Proteomes:UP000008385};
RA   Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M.,
RA   Py B., Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S.,
RA   Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A.,
RA   Mejean V., DuBow M., Barras F., Heulin T.;
RT   "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEG92100.1, ECO:0000313|Proteomes:UP000008385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC   {ECO:0000313|Proteomes:UP000008385};
RX   PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA   De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA   Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA   Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A.,
RA   Mejean V., Dubow M.S., Barras F., Barbe V., Weissenbach J.,
RA   Mihalcescu I., Vermeglio A., Achouak W., Heulin T.;
RT   "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT   Reveals a Well-Stocked Toolbox for Adaptation to a Desert
RT   Environment.";
RL   PLoS ONE 6:E23784-E23784(2011).
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; CP000245; AEG92100.1; -; Genomic_DNA.
DR   RefSeq; WP_013900333.1; NC_015677.1.
DR   STRING; 365046.Rta_10160; -.
DR   MEROPS; T05.001; -.
DR   EnsemblBacteria; AEG92100; AEG92100; Rta_10160.
DR   KEGG; rta:Rta_10160; -.
DR   PATRIC; fig|365046.3.peg.1038; -.
DR   eggNOG; ENOG4105C5V; Bacteria.
DR   eggNOG; COG1364; LUCA.
DR   KO; K00620; -.
DR   OMA; GMIAPNM; -.
DR   OrthoDB; 1083409at2; -.
DR   BioCyc; RTAT365046:G1GYB-1051-MONOMER; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000008385; 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:UP000008385};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008385};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000313|EMBL:AEG92100.1}.
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     279    279       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     403    403       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     408    408       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   SITE        118    118       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        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        191    192       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ   SEQUENCE   408 AA;  42674 MW;  08C5BBDB118C4855 CRC64;
     MAVNLSAPRA ADLLPVPGVR IGVAEAGVRK AGRKDLTVML LEPGAAVAGV FTQNRFCAAP
     VQVCREHLKQ GDIRALVINT GNANAGTGQD GLVRARATCI ALARQLEVAP EQVLPFSTGV
     IMEPLPLERI EAGLPAALAD AQPAHWLRAA EGIMTTDTVA KAFSATAVVG GAQVTVTGIS
     KGAGMIRPNM ATMLGFLATD ARIAPGLLPA LALELAEASF NRVTVDGDTS TNDSFVVIAT
     QKAAHAPIAS LDSADGRALK AAMLQVARQL AQAIVRDGEG ATKFITVRVE GGRDAGECRQ
     VAYAIAHSPL VKTAFFASDP NLGRILAAVG YAGIADLDPG RIDLFLDDVH VAVGGGRNPS
     YREEDGQRVM KQSEITVRVV LGRGQAADTV WTCDFSYDYV KINADYRS
//
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