GenomeNet

Database: UniProt
Entry: N6XCX0_9ACTO
LinkDB: N6XCX0_9ACTO
Original site: N6XCX0_9ACTO 
ID   N6XCX0_9ACTO            Unreviewed;       377 AA.
AC   N6XCX0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   05-JUN-2019, entry version 41.
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   ECO:0000313|EMBL:ENO19088.1};
GN   ORFNames=HMPREF9004_0007 {ECO:0000313|EMBL:ENO19088.1};
OS   Schaalia cardiffensis F0333.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; Schaalia.
OX   NCBI_TaxID=888050 {ECO:0000313|EMBL:ENO19088.1, ECO:0000313|Proteomes:UP000013015};
RN   [1] {ECO:0000313|EMBL:ENO19088.1, ECO:0000313|Proteomes:UP000013015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0333 {ECO:0000313|EMBL:ENO19088.1,
RC   ECO:0000313|Proteomes:UP000013015};
RA   Aqrawi P., Ayvaz T., Bess C., Blankenburg K., Coyle M., Deng J.,
RA   Forbes L., Fowler G., Francisco L., Fu Q., Gibbs R., Gross S.,
RA   Gubbala S., Hale W., Hemphill L., Highlander S., Hirani K.,
RA   Jackson L., Jakkamsetti A., Javaid M., Jayaseelan J.C., Jiang H.,
RA   Joshi V., Korchina V., Kovar C., Lara F., Lee S., Liu Y., Mata R.,
RA   Mathew T., Munidasa M., Muzny D., Nazareth L., Ngo R., Nguyen L.,
RA   Nguyen N., Okwuonu G., Ongeri F., Palculict T., Patil S.,
RA   Petrosino J., Pham C., Pham P., Pu L.-L., Qin X., Qu J., Reid J.,
RA   Ross M., Ruth R., Saada N., San Lucas F., Santibanez J., Shang Y.,
RA   Simmons D., Song X.-Z., Tang L.-Y., Thornton R., Warren J.,
RA   Weissenberger G., Wilczek-Boney K., Worley K., Youmans B., Zhang J.,
RA   Zhang L., Zhao Z., Zhou C., Zhu D., Zhu Y.;
RT   "Reference genome for the Human Microbiome Project.";
RL   Submitted (MAR-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ENO19088.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AQHZ01000001; ENO19088.1; -; Genomic_DNA.
DR   STRING; 888050.HMPREF9004_0007; -.
DR   EnsemblBacteria; ENO19088; ENO19088; HMPREF9004_0007.
DR   PATRIC; fig|888050.3.peg.7; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000013015; Unassembled WGS sequence.
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:ENO19088.1};
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:UP000013015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013015};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW   ECO:0000313|EMBL:ENO19088.1}.
FT   ACT_SITE    170    170       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     159    159       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     170    170       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     250    250       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     372    372       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   BINDING     377    377       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01106}.
FT   SITE         97     97       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         98     98       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        169    170       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ   SEQUENCE   377 AA;  38953 MW;  43F8362D4ECA1F74 CRC64;
     MAAGIKHTEG ALDLALVVNE GPVFASAGVF TSNRVVAAPV TLTRSHLASA SLKAIILNSG
     GANACTGQAG FHDAQASARH LAPLLGCEVK EVGVCSTGMI GQRLPMDKIL HGTDAAVAAL
     ASTPEAGAQA ADAIRTTDTV PKTYEFSSQE GWQIGAMAKG AGMLAPALAT MLCVITSDAI
     LDDDMAAAAL SEAVRTTFNR TDSDGCMSTN DSVILLASGA SGVAPSEEDF TEALRSTCAN
     LARQLLADAE GASHDIEITV AHASDEAAGE AVARAVSRSN LFKTAVFGND PNWGRILSEV
     GTVPESVAPF DPEQIDVSIN GVMVCRNGGV GEDRSLVDMT PREVQVLIDL KAGEENVVLW
     TNDLTHDYVH ENSAYSS
//
DBGET integrated database retrieval system