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Database: UniProt
Entry: A0A024THX8_9STRA
LinkDB: A0A024THX8_9STRA
Original site: A0A024THX8_9STRA 
ID   A0A024THX8_9STRA        Unreviewed;       410 AA.
AC   A0A024THX8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   05-JUN-2019, entry version 34.
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=H310_12800 {ECO:0000313|EMBL:ETV93201.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Stramenopiles; Oomycetes; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV93201.1, ECO:0000313|Proteomes:UP000024375};
RN   [1] {ECO:0000313|EMBL:ETV93201.1, ECO:0000313|Proteomes:UP000024375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV93201.1,
RC   ECO:0000313|Proteomes:UP000024375};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-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
CC       acetylglutamate from glutamate and acetyl-CoA, and of ornithine by
CC       transacetylation between acetylornithine and glutamate.
CC       {ECO:0000256|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: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}.
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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03124}.
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DR   EMBL; KI913994; ETV93201.1; -; Genomic_DNA.
DR   RefSeq; XP_008878222.1; XM_008880000.1.
DR   EnsemblProtists; ETV93201; ETV93201; H310_12800.
DR   GeneID; 20089850; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000024375; 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   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.
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:UP000024375};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024375};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03124,
KW   ECO:0000313|EMBL:ETV93201.1}.
FT   ACT_SITE    222    222       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     189    189       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     211    211       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     222    222       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     303    303       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   SITE        152    152       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        153    153       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        221    222       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_03124}.
SQ   SEQUENCE   410 AA;  44183 MW;  5D627815023E48FA CRC64;
     MWRLARSAIP RRHLTSSAKL PAFVFNSATE YYNYLNEHHS RLPWGFSVGT TTFKFVPQEA
     PHLPAQMTLT LIKPHKPTPL FGAVFTQNAC PGAPIKVGRK RLAEDTLGAI IVNNKISNVC
     ANGGGVSDAQ EVCDAVAQHL DLRGSQVLPS STGVIGWRLP VEPILHALPN LVESLQDTSI
     LPAAAGIMTT DLYPKIRSVD VCGGRIVGIA KGAGMVEPNM ATMLSYILTD LAVPRDLLRR
     LLADVVDKTY NSMSVDTDES TSDTLAIVSS GEIPFDVEHL DEFRAGLYDV CAGLCEDIVR
     NGEGAHHVMQ VVVKGAMDEV QAKGIGKSIV NSPLLKCAVA GNDPNVGRLV MAVHELHGEA
     NIPLTRGAGE LGRQVHGQAL QGGERRGKHD DQHGRAAHLR VWRVYAQRGC
//
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