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Database: UniProt
Entry: ARGJ_TALSN
LinkDB: ARGJ_TALSN
Original site: ARGJ_TALSN 
ID   ARGJ_TALSN              Reviewed;         470 AA.
AC   B8M9V7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   18-SEP-2019, entry version 53.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03124};
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE              Short=GAT {ECO:0000255|HAMAP-Rule:MF_03124};
DE              EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_03124};
DE     AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE              Short=OATase {ECO:0000255|HAMAP-Rule:MF_03124};
DE     AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_03124};
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE              EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_03124};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_03124};
DE              Short=AGS {ECO:0000255|HAMAP-Rule:MF_03124};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_03124};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_03124};
DE   Flags: Precursor;
GN   ORFNames=TSTA_118750;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 /
OS   NRRL 1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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:0000255|HAMAP-Rule:MF_03124}.
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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-
CC       Rule:MF_03124}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000255|HAMAP-Rule:MF_03124}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|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:0000255|HAMAP-Rule:MF_03124}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-
CC       terminal transit peptide but none has been predicted.
CC       {ECO:0000255|HAMAP-Rule:MF_03124}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_03124}.
DR   EMBL; EQ962655; EED18109.1; -; Genomic_DNA.
DR   RefSeq; XP_002482101.1; XM_002482056.1.
DR   SMR; B8M9V7; -.
DR   STRING; 28564.XP_002482101.1; -.
DR   MEROPS; T05.001; -.
DR   PRIDE; B8M9V7; -.
DR   EnsemblFungi; EED18109; EED18109; TSTA_118750.
DR   GeneID; 8099888; -.
DR   EuPathDB; FungiDB:TSTA_118750; -.
DR   eggNOG; KOG2786; Eukaryota.
DR   eggNOG; COG1364; LUCA.
DR   InParanoid; B8M9V7; -.
DR   OMA; GMIAPNM; -.
DR   OrthoDB; 934513at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00111.
DR   Proteomes; UP000001745; 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; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Autocatalytic cleavage; Complete proteome; Mitochondrion;
KW   Multifunctional enzyme; Reference proteome; Transferase.
FT   CHAIN         1    238       Arginine biosynthesis bifunctional
FT                                protein ArgJ alpha chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_03124}.
FT                                /FTId=PRO_0000398114.
FT   CHAIN       239    470       Arginine biosynthesis bifunctional
FT                                protein ArgJ beta chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_03124}.
FT                                /FTId=PRO_0000398115.
FT   ACT_SITE    239    239       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     199    199       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     228    228       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     239    239       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     325    325       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     465    465       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     470    470       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   SITE        160    160       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   SITE        161    161       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   SITE        238    239       Cleavage; by autolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_03124}.
SQ   SEQUENCE   470 AA;  49749 MW;  136D79646ACB6DC4 CRC64;
     MMILTKTGPL GPVTNSFIIA TTRRGQIRLY NILQDTTIPE PKRKHIPSSG TYPKGFRVSG
     THVGVKAANT KYPDLALISS DEPCTAAAVF TTNKFQAAPV QISKLTLDQR KGKGIQSVVI
     NSGCANAVTG KGGLEDAQSM ASKVDECNGI SEPSTLVMST GVIGQRLPIS KILDKIPTAY
     SNLANTHNAW LATARAICTT DTFPKLISQT FTLPSSPGIT YSLAGMTKGA GMIHPNMATL
     LGVLCTDAPV DASAMKPLLL QAVSRSFNSI SIDGDTSTND TIAFLANGAA GGQPVTSSSA
     DYTALQKVLT SFAQSLSQLV VRDGEGATKF VTVRIQNSPC YESARRIAST IARSPLVKTA
     LYGRDANWGR ILCAVGYADG VTEGTVIPER TSVSFKPVDG SPVLRLLVNG EPEVVDEERA
     SAILQDEDLE IIVDLGGGSK GEKGLGGEEA VYWFCDFSHE YVTINGDYRT
//
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