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Database: UniProt
Entry: A4SV86_POLAQ
LinkDB: A4SV86_POLAQ
Original site: A4SV86_POLAQ 
ID   A4SV86_POLAQ            Unreviewed;       411 AA.
AC   A4SV86;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   05-JUN-2019, entry version 97.
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=Pnuc_0179 {ECO:0000313|EMBL:ABP33400.1};
OS   Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS   QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153 {ECO:0000313|EMBL:ABP33400.1, ECO:0000313|Proteomes:UP000000231};
RN   [1] {ECO:0000313|EMBL:ABP33400.1, ECO:0000313|Proteomes:UP000000231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1
RC   {ECO:0000313|Proteomes:UP000000231};
RX   PubMed=22675600; DOI=10.4056/sigs.2395367;
RA   Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P.,
RA   Bruce D., Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J.,
RA   Brettin T., Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA   Goker M., Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT   "Complete genome sequence of Polynucleobacter necessarius subsp.
RT   asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL   Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP33400.1; -; Genomic_DNA.
DR   RefSeq; WP_011902025.1; NC_009379.1.
DR   STRING; 312153.Pnuc_0179; -.
DR   MEROPS; T05.001; -.
DR   EnsemblBacteria; ABP33400; ABP33400; Pnuc_0179.
DR   GeneID; 31480528; -.
DR   KEGG; pnu:Pnuc_0179; -.
DR   eggNOG; ENOG4105C5V; Bacteria.
DR   eggNOG; COG1364; LUCA.
DR   HOGENOM; HOG000022798; -.
DR   KO; K00620; -.
DR   OMA; GMIAPNM; -.
DR   BioCyc; PNEC312153:G1G8K-192-MONOMER; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000000231; 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:ABP33400.1};
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:UP000000231};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000231};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000313|EMBL:ABP33400.1}.
FT   ACT_SITE    196    196       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     159    159       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     185    185       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     196    196       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     282    282       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     406    406       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     411    411       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   SITE        122    122       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        123    123       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        195    196       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ   SEQUENCE   411 AA;  43364 MW;  16576A6D595375B7 CRC64;
     MTVNLPLPQK SELKPVKGFE MGIAKAGIKK ADRKDLLVMR LAPGSQVAGV FTLNRFCAAP
     VQVCREHLAQ EGRHGEIRAL VVNTGNANAG TGEQGMKHAL ETCAALAKDL GINPAQILPF
     STGVILEPLP IEKIIAALPA AVANLGDDQW LDAAEAIMTT DTQPKASSVT IQTPAGSVVL
     TGICKGAGMI HPNMATMLGF IATDAGFAPG LLGDLTRDVA DLSFNAITID GDTSTNDSFI
     IMATGQSSVQ IQSISDPAYA IVRDALVGLA RKLAQMIVRD GEGATKFMTI EVVGGKTAEE
     CRLVAKAVAH SPLVKTAFFA SDPNLGRILA AIGYAGITDL DVNHVQMWLG DVWVAKDGGR
     NPSYQEADGQ RVMQAPEITV KIDLGRGTAS QTMWTCDLSH DYVSINADYR S
//
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