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Database: UniProt
Entry: D9SJP2_GALCS
LinkDB: D9SJP2_GALCS
Original site: D9SJP2_GALCS 
ID   D9SJP2_GALCS            Unreviewed;       409 AA.
AC   D9SJP2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   05-JUN-2019, entry version 65.
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=Galf_0347 {ECO:0000313|EMBL:ADL54391.1};
OS   Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea
OS   capsiferriformans (strain ES-2)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Gallionella.
OX   NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL54391.1, ECO:0000313|Proteomes:UP000001235};
RN   [1] {ECO:0000313|EMBL:ADL54391.1, ECO:0000313|Proteomes:UP000001235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES-2 {ECO:0000313|EMBL:ADL54391.1,
RC   ECO:0000313|Proteomes:UP000001235};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N.,
RA   Ivanova N., Mikhailova N., Shelobolina E.S., Picardal F., Roden E.,
RA   Emerson D., Woyke T.;
RT   "Complete sequence of Gallionella capsiferriformans ES-2.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002159; ADL54391.1; -; Genomic_DNA.
DR   RefSeq; WP_013292334.1; NC_014394.1.
DR   STRING; 395494.Galf_0347; -.
DR   EnsemblBacteria; ADL54391; ADL54391; Galf_0347.
DR   KEGG; gca:Galf_0347; -.
DR   eggNOG; ENOG4105C5V; Bacteria.
DR   eggNOG; COG1364; LUCA.
DR   HOGENOM; HOG000022798; -.
DR   KO; K00620; -.
DR   OMA; GMIAPNM; -.
DR   OrthoDB; 1083409at2; -.
DR   BioCyc; GCAP395494:G1GMJ-355-MONOMER; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001235; 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:ADL54391.1};
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:UP000001235};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001235};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000313|EMBL:ADL54391.1}.
FT   ACT_SITE    193    193       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     156    156       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     182    182       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     193    193       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     280    280       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     404    404       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     409    409       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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        120    120       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        192    193       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ   SEQUENCE   409 AA;  43015 MW;  AECE03C5D56C5A39 CRC64;
     MPVNLNPPVA KQLLPVAGVT LGIAEANIKR ENRKDLLVMQ LCEGAKVAGV FTQNRFCAAP
     VIVAREHLAA DEGIRALVVN TGNANAGTGE QGLLDARMTC AALAGLLGCK SNQILPFSTG
     VIMEPLPVAK IAAGLPAAVA NMTGDNWFDA AHAIMTTDIV AKAISKQVVV EGVTVTITGI
     AKGSGMIHPN MATMLGYIAT DVTISQALLQ QLVTTAANRS FNCITVDGDT STNDALMLIA
     TGQAAHNEVT SQDSAVYGVL LDAISEVAIY LAQAIVRDGE GATKFITVKI EGGRDEEECK
     KIGYAIAHSP LVKTAFFASD PNLGRILAAI GYAGVEDLDV SALQLYLDDV LVAENGGRAA
     SYQEADGQRV MAQSDITIRV VLNRSDVNAT LWTCDFSYDY VKINASYRS
//
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