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Database: UniProt
Entry: ARGJ_NEIG1
LinkDB: ARGJ_NEIG1
Original site: ARGJ_NEIG1 
ID   ARGJ_NEIG1              Reviewed;         406 AA.
AC   Q5F7I3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   26-FEB-2020, entry version 93.
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}; OrderedLocusNames=NGO1194;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC       version of arginine biosynthesis: the synthesis of N-acetylglutamate
CC       from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by
CC       transacetylation between N(2)-acetylornithine and glutamate.
CC       {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; EC=2.3.1.35;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01106};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC         Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01106};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC       and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine
CC       (cyclic): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01106}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       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 biosynthetic
CC       pathway.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01106}.
DR   EMBL; AE004969; AAW89854.1; -; Genomic_DNA.
DR   RefSeq; WP_003691802.1; NC_002946.2.
DR   RefSeq; YP_208266.1; NC_002946.2.
DR   SMR; Q5F7I3; -.
DR   PRIDE; Q5F7I3; -.
DR   EnsemblBacteria; AAW89854; AAW89854; NGO_1194.
DR   GeneID; 3282038; -.
DR   KEGG; ngo:NGO1194; -.
DR   PATRIC; fig|242231.10.peg.1401; -.
DR   HOGENOM; CLU_027172_1_0_4; -.
DR   KO; K00620; -.
DR   OMA; GMIAPNM; -.
DR   BioCyc; NGON242231:G1FZ9-1067-MONOMER; -.
DR   UniPathway; UPA00068; UER00111.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000535; 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; Cytoplasm; Multifunctional enzyme;
KW   Reference proteome; Transferase.
FT   CHAIN           1..189
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT                   /id="PRO_0000227234"
FT   CHAIN           190..406
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT                   /id="PRO_0000227235"
FT   ACT_SITE        190
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         152
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         179
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         190
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         277
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         401
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   BINDING         406
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   SITE            119
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   SITE            120
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT   SITE            189..190
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
SQ   SEQUENCE   406 AA;  42851 MW;  A3F3635905E2C856 CRC64;
     MAVNLTEKTA EQLPDIDGIA LYTAQAGVKK PGHTDLTLIA VAAGSTVGAV FTTNRFCAAP
     VHIAKSHLFD EDGVRALVIN TGNANAGTGA QGRIDALAVC AAAARQIGCK PNQVMPFSTG
     VILEPLPADK IIAALPKMQP AFWNEAARAI MTTDTVPKAA SREGKVGDQH TVRATGIAKG
     SGMIHPNMAT MLGFIATDAK VSQPVLQLMT QEIADETFNT ITVDGDTSTN DSFVIIATGK
     NSQSEIDNIA DPRYAQLKEL LCSLALELAQ AIVRDGEGAT KFITVRVENA KTCDEARQAA
     YAAARSPLVK TAFFASDPNL GRLLAAIGYA DVADLDTDLV EMYLDDILVA EHGGRAASYT
     EAQGQAVMSK DEITVRIKLH RGQAAATVYT CDLSHGYVSI NADYRS
//
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