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Database: UniProt
Entry: G4TTK8_SERID
LinkDB: G4TTK8_SERID
Original site: G4TTK8_SERID 
ID   G4TTK8_SERID            Unreviewed;       466 AA.
AC   G4TTK8;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   05-JUN-2019, entry version 56.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03124};
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE              Short=GAT {ECO:0000256|HAMAP-Rule:MF_03124};
DE              EC=2.3.1.35 {ECO:0000256|HAMAP-Rule:MF_03124};
DE     AltName: Full=Ornithine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE              Short=OATase {ECO:0000256|HAMAP-Rule:MF_03124};
DE     AltName: Full=Ornithine transacetylase {ECO:0000256|HAMAP-Rule:MF_03124};
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE              EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_03124};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_03124};
DE              Short=AGS {ECO:0000256|HAMAP-Rule:MF_03124};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000256|HAMAP-Rule:MF_03124};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000256|HAMAP-Rule:MF_03124};
GN   ORFNames=PIIN_08602 {ECO:0000313|EMBL:CCA74651.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA74651.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA74651.1, ECO:0000313|Proteomes:UP000007148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA74651.1,
RC   ECO:0000313|Proteomes:UP000007148};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S.,
RA   Biedenkopf D., Wong P., Samans B., Grimm C., Basiewicz M., Murat C.,
RA   Martin F., Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome
RT   Analyses of the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(2011).
CC   -!- FUNCTION: Catalyzes two activities which are involved in the
CC       cyclic version of arginine biosynthesis: the synthesis of
CC       acetylglutamate from glutamate and acetyl-CoA, and of ornithine by
CC       transacetylation between acetylornithine and glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_03124, ECO:0000256|SAAS:SAAS01092298}.
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_03124};
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_03124};
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_03124}.
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_03124}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|HAMAP-Rule:MF_03124, ECO:0000256|SAAS:SAAS01092300}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-
CC       Rule:MF_03124}.
CC   -!- PTM: The alpha and beta chains are autoproteolytically processed
CC       from a single precursor protein within the mitochondrion.
CC       {ECO:0000256|HAMAP-Rule:MF_03124}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|HAMAP-
CC       Rule:MF_03124}.
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:CCA74651.1}.
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DR   EMBL; CAFZ01000339; CCA74651.1; -; Genomic_DNA.
DR   STRING; 65672.G4TTK8; -.
DR   MEROPS; T05.001; -.
DR   EnsemblFungi; CCA74651; CCA74651; PIIN_08602.
DR   InParanoid; G4TTK8; -.
DR   OMA; GMIAPNM; -.
DR   OrthoDB; 934513at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000007148; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; 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_03124};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007148};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03124,
KW   ECO:0000313|EMBL:CCA74651.1}.
FT   ACT_SITE    244    244       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     194    194       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     220    220       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     244    244       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     331    331       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     461    461       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     466    466       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   SITE        154    154       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_03124}.
FT   SITE        155    155       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_03124}.
FT   SITE        243    244       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_03124}.
SQ   SEQUENCE   466 AA;  49511 MW;  A582D2D669C74E47 CRC64;
     MQRIFGNTIR TFSSSPARWA KATPSKAHLA ITPAHENLPR GFVVTGVHAG VKKKEGVLDL
     GLILSKEPKT SAAACFTRNA FQAAPVIVCQ DVLQQTSGHA NGLIVNSGCA NAVTGKQGLK
     DAWDMVSATD NLLSKLVPAN ETPKGSHSSL VMSTGVIGQN LPISKIISAV KETSPESLDS
     TPEKWEALAR AFMTTDTFPK LRAKTFKIGD TDVRIAGIDK GAGMIHPDMG PATPAPGTGS
     LHATLLGMIA TDAAVSPQAL QDALTYAVNR SFNSISVDGD MSTNDTVVVF ANGASGMKEI
     DDVTSPEYTK FRDELTDFAA ELAQLVVRDG EGATKFVTVN VRGALTYEDA HQVASKISTS
     ALVKTALYGE DANWGRVLAA TGSTNLSAPI TPNTVSVSFI PTDGSEILPL LKNGEPEKVD
     EDRAKVILQR EDLEIRVDLG MGNEQASYWT CDFSHEYVTI NGDYRS
//
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