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ARGJ_ASPFN
ID   ARGJ_ASPFN              Reviewed;         466 AA.
AC   B8NEJ3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=AFLA_061910;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC       version of arginine biosynthesis: the synthesis of acetylglutamate from
CC       glutamate and acetyl-CoA, and of ornithine by transacetylation between
CC       acetylornithine and glutamate. {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; EC=2.3.1.35;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03124};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC         Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03124};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC       and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine
CC       (cyclic): step 1/1. {ECO:0000255|HAMAP-Rule:MF_03124}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       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. {ECO:0000255|HAMAP-
CC       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 from a
CC       single precursor protein within the mitochondrion. {ECO:0000255|HAMAP-
CC       Rule:MF_03124}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       Rule:MF_03124}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_03124}.
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DR   EMBL; EQ963477; EED51928.1; -; Genomic_DNA.
DR   RefSeq; XP_002378935.1; XM_002378894.1.
DR   AlphaFoldDB; B8NEJ3; -.
DR   SMR; B8NEJ3; -.
DR   STRING; 5059.CADAFLAP00006800; -.
DR   MEROPS; T05.001; -.
DR   EnsemblFungi; EED51928; EED51928; AFLA_061910.
DR   VEuPathDB; FungiDB:AFLA_061910; -.
DR   eggNOG; KOG2786; Eukaryota.
DR   HOGENOM; CLU_027172_1_0_1; -.
DR   OMA; DYVHENS; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00111.
DR   Proteomes; UP000001875; 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; Mitochondrion; Multifunctional enzyme; Transferase.
FT   CHAIN           1..233
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT                   /id="PRO_0000398014"
FT   CHAIN           234..466
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT                   /id="PRO_0000398015"
FT   ACT_SITE        234
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         461
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         466
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   SITE            155
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   SITE            156
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   SITE            233..234
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
SQ   SEQUENCE   466 AA;  48922 MW;  920031716F63B08E CRC64;
     MASPAQPAAT MAAFARMVKG QVRSYSAPVD MAIPASKRKF IPSSGSYPKG FVVSGTHVGV
     KASNTKFPDL ALISSETPCS AAAVFTTNKF QAAPVQVSRD IIKTRQGQGI RSVVINSGCA
     NAVTGKGGLE DAVSMGKKVD ECDGLNEPST LVMSTGVIGQ RLPISKILKK VPVAHANLSS
     THDAWLTTAR AICTTDTFPK LLSRTFTLPS SPGRTYSLAG MTKGAGMIHP NMATLLGVLC
     TDAPIEPSAL QSLLKHSVNR SFNSISVDGD TSTNDTIAIL ANGAAGGAPI SSSSSDDYAA
     MQDILTSFAQ SLSQLVVRDG EGATKFVTVR VQNSPDYESG RLIASTIARS PLVKTALYGK
     DANWGRILCA IGYTQGVAPG TVVPEHTSVS FKPVDGSPVL NLLVNGEPEQ VDEERASVIL
     QEEDLEIVVD LGGGEKGEQG LGGEEAVYWF CDFSHEYVTI NGDYRT
 
 
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