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Database: UniProt
Entry: ARGJ_STRMU
LinkDB: ARGJ_STRMU
Original site: ARGJ_STRMU 
ID   ARGJ_STRMU              Reviewed;         397 AA.
AC   Q8DV45;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   05-JUN-2019, entry version 111.
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=SMU_664;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J.,
RA   Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P.,
RA   Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A.,
RA   Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58398.1; -; Genomic_DNA.
DR   RefSeq; NP_721092.1; NC_004350.2.
DR   RefSeq; WP_002261877.1; NC_004350.2.
DR   SMR; Q8DV45; -.
DR   STRING; 210007.SMU_664; -.
DR   MEROPS; T05.002; -.
DR   DNASU; 1028088; -.
DR   EnsemblBacteria; AAN58398; AAN58398; SMU_664.
DR   GeneID; 1028088; -.
DR   KEGG; smu:SMU_664; -.
DR   PATRIC; fig|210007.7.peg.589; -.
DR   eggNOG; ENOG4105C5V; Bacteria.
DR   eggNOG; COG1364; LUCA.
DR   KO; K00620; -.
DR   OMA; GMIAPNM; -.
DR   PhylomeDB; Q8DV45; -.
DR   BioCyc; SMUT210007:G1FZX-648-MONOMER; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00111.
DR   Proteomes; UP000002512; 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_0000002249.
FT   CHAIN       184    397       Arginine biosynthesis bifunctional
FT                                protein ArgJ beta chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_01106}.
FT                                /FTId=PRO_0000002250.
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;  42419 MW;  3116A8DCBCB7EFD6 CRC64;
     MKIIDGNIAS PLGFSADGLH AGFKKRKKDF GWIVSEVPAS VAGVYTTNKV IAAPLIVTRE
     SVKKAQKMQA LVVNSGVANS CTGLQGMEDA YTMQKWTATK LKIAPELVGV ASTGVIGDLM
     PMDTLQKGLS KLVVNGNSDD FAQAILTTDT KVKTVAVTEQ FGRDEVTMAG VAKGSGMIHP
     NMATMLAFIT CDAVISSETL QLALSQNVET TFNQITVDGD TSTNDMVLVL SNGCTLNKEI
     LPDTPEFDKF SAMLHFVMQE LAKKIAKDGE GATKLIEVEV INAPNSLDAC MMAKSVVGSS
     LVKTAIFGED PNWGRILAAV GYAGVDVPVD NIDIYLADIP VMLASSPVDF DEEDMQDVMR
     ADTIKIIVDL HAGDSVGKAW GCDLSYDYVK INALYRT
//
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