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Database: UniProt
Entry: A0A1D2VRM4_9ASCO
LinkDB: A0A1D2VRM4_9ASCO
Original site: A0A1D2VRM4_9ASCO 
ID   A0A1D2VRM4_9ASCO        Unreviewed;       459 AA.
AC   A0A1D2VRM4;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   05-JUN-2019, entry version 24.
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=ASCRUDRAFT_73922 {ECO:0000313|EMBL:ODV64263.1};
OS   Ascoidea rubescens DSM 1968.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Ascoideaceae; Ascoidea.
OX   NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV64263.1, ECO:0000313|Proteomes:UP000095038};
RN   [1] {ECO:0000313|Proteomes:UP000095038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T.,
RA   Goker M., Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K.,
RA   Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K., Lapidus A., Lindquist E.,
RA   Lipzen A., Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) 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
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}.
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DR   EMBL; KV454475; ODV64263.1; -; Genomic_DNA.
DR   RefSeq; XP_020050570.1; XM_020192485.1.
DR   EnsemblFungi; ODV64263; ODV64263; ASCRUDRAFT_73922.
DR   GeneID; 30966121; -.
DR   OrthoDB; 934513at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000095038; 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   GO; GO:0006592; P:ornithine biosynthetic process; IEA:EnsemblFungi.
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:UP000095038};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095038};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03124}.
FT   ACT_SITE    235    235       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     198    198       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     224    224       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     235    235       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     325    325       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     454    454       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     459    459       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   SITE        157    157       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        158    158       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        234    235       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_03124}.
SQ   SEQUENCE   459 AA;  49234 MW;  8005ED7D460EE7D4 CRC64;
     MFLATVRSAV PKPLARLFQR ALSLEASSPV IPEDKRQYVP SSGSYPKGFR VGAISSGVKK
     HAHLDLSIIT SATPCNAAGV FTTNKFKAAP VVLDRQILND SKGKNIHSIV INSGCANAVT
     GKQGLEDATE VSSLVDALSV PSHNERPVHN STLVMSTGVI GQLLPMHKLK AGITAIFNSD
     VLKDDHQSWL NCARGIMTTD TFPKITSKSF LIDNNTYNIV GLAKGAGMIC PNMATMLGCF
     ITDAPLSTSA LNSILKYSVD RSFNCISVDG DMSTNDTILL LSNGASLSGK KTDVINEDSP
     SYSQIRDIIT SFAQSLSQLI IRDGEGATKF VTIKVNDAES YDDAKKIASS IANSSLVKTA
     LYGQDANWGR ILCAIGYSDI DINPETINLS FIPTDGSSPL KLLSNGEPEI VDEERASQIL
     KLTDLEILVE LGTGKGQNAT YWTCDLSHEY VTINGDYRS
//
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