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Database: UniProt
Entry: ARGJ_STRT2
LinkDB: ARGJ_STRT2
Original site: ARGJ_STRT2 
ID   ARGJ_STRT2              Reviewed;         397 AA.
AC   Q5M5L0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   05-JUN-2019, entry version 100.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              Short=OATase {ECO:0000255|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01106};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01106};
DE              Short=AGSase {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_01106};
GN   Name=argJ {ECO:0000255|HAMAP-Rule:MF_01106};
GN   OrderedLocusNames=stu0465;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D.,
RA   Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D.,
RA   Ngui K., Masuy D., Hancy F., Burteau S., Boutry M., Delcour J.,
RA   Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy
RT   bacterium Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-
CC       Rule:MF_01106}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01106}.
DR   EMBL; CP000023; AAV60175.1; -; Genomic_DNA.
DR   RefSeq; WP_011225582.1; NC_006448.1.
DR   SMR; Q5M5L0; -.
DR   STRING; 264199.stu0465; -.
DR   MEROPS; T05.002; -.
DR   EnsemblBacteria; AAV60175; AAV60175; stu0465.
DR   KEGG; stl:stu0465; -.
DR   PATRIC; fig|264199.4.peg.468; -.
DR   eggNOG; ENOG4105C5V; Bacteria.
DR   eggNOG; COG1364; LUCA.
DR   HOGENOM; HOG000022797; -.
DR   KO; K00620; -.
DR   OMA; GMIAPNM; -.
DR   BioCyc; STHE264199:G1G41-490-MONOMER; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00111.
DR   Proteomes; UP000001170; 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; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Autocatalytic cleavage; Complete proteome; Cytoplasm;
KW   Multifunctional enzyme; Reference proteome; Transferase.
FT   CHAIN         1    183       Arginine biosynthesis bifunctional
FT                                protein ArgJ alpha chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_01106}.
FT                                /FTId=PRO_0000227260.
FT   CHAIN       184    397       Arginine biosynthesis bifunctional
FT                                protein ArgJ beta chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_01106}.
FT                                /FTId=PRO_0000227261.
FT   ACT_SITE    184    184       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     147    147       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     173    173       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     184    184       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     270    270       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     392    392       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   BINDING     397    397       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        113    113       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        114    114       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000255|HAMAP-
FT                                Rule:MF_01106}.
FT   SITE        183    184       Cleavage; by autolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01106}.
SQ   SEQUENCE   397 AA;  42117 MW;  50FC2245BF664455 CRC64;
     MKVIDGTIAS PLGFSADGLH AGFKKRKMDF GWIVSEKPAS VAGVYTTNKV IAAPLIVTKT
     SVKKAGKMRA IVVNSGVANS CTGTQGLEDA YTMQEWTAEK LGVEPDMIGV ASTGIIGELL
     PMDTLKNGLS KLVVNGNAND FAKAILTTDT ATKTIAVTET FGRDVVTMAG VAKGSGMIHP
     NMATMLGFIT CDANISSDTL QLALSQNVEK TFNQITVDGD TSTNDMVLVM SNGCALNDEI
     LPDTPEFDKF SKMLNFVMQE LAKKIAKDGE GANKLIQVDV VNAPNALDAR MMAKSVVGSS
     LVKTAIFGED PNWGRILAAV GYAGVDVPVD NVDIMIGGLP VMLASSPVTF DDEEMKDIMH
     GDEVTITVDL HSGQEKGTAW GCDLSYDYVK INALYHT
//
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