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Database: UniProt
Entry: F8Q9S5_SERL3
LinkDB: F8Q9S5_SERL3
Original site: F8Q9S5_SERL3 
ID   F8Q9S5_SERL3            Unreviewed;       472 AA.
AC   F8Q9S5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   05-JUN-2019, entry version 51.
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=SERLA73DRAFT_125549 {ECO:0000313|EMBL:EGN95330.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Coniophorineae;
OC   Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M.,
RA   Blumentritt M., Coutinho P.M., Cullen D., de Vries R.P., Gathman A.,
RA   Goodell B., Henrissat B., Ihrmark K., Kauserud H., Kohler A.,
RA   LaButti K., Lapidus A., Lavin J.L., Lee Y.-H., Lindquist E., Lilly W.,
RA   Lucas S., Morin E., Murat C., Oguiza J.A., Park J., Pisabarro A.G.,
RA   Riley R., Rosling A., Salamov A., Schmidt O., Schmutz J., Skrede I.,
RA   Stenlid J., Wiebenga A., Xie X., Kuees U., Hibbett D.S.,
RA   Hoffmeister D., Hoegberg N., Martin F., Grigoriev I.V.,
RA   Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(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}.
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DR   EMBL; GL945486; EGN95330.1; -; Genomic_DNA.
DR   STRING; 85982.XP_007322830.1; -.
DR   MEROPS; T05.001; -.
DR   EnsemblFungi; EGN95330; EGN95330; SERLA73DRAFT_125549.
DR   OrthoDB; 934513at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000008063; 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:UP000008063};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03124}.
FT   ACT_SITE    246    246       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     199    199       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     225    225       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     246    246       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     337    337       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     467    467       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     472    472       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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:0000256|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:0000256|HAMAP-
FT                                Rule:MF_03124}.
FT   SITE        245    246       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_03124}.
SQ   SEQUENCE   472 AA;  49918 MW;  30369A2C695C828C CRC64;
     MPVMQHYRAA LALSSSDDAG RFASTITIKP APSKSHLHAS IPDSSFPKNF VVAGSHCGVK
     KNAGVNDLAV ILSTSSRPAA AAACFTRNAF KAAPVLVSQE VLEKGAGRAR ALVVNSGCAN
     AVTGKQGMED AWAMVKATDA LLEPSSPSSS GTHETLVMST GVIGQNLPIS KIIAGIESKA
     LTLDSNFSAW ESAAKAFMTT DTFPKLRART FTINGQTFRM AGIDKGAGMI HPDMGPPASA
     KQLHATLLAC ILTDAAISPR SLQSALTYAV DRSFNSISVD GEMSTNDTII VLANGAAADQ
     SAKEIDEEHD RKAYETFREE LTSFATDLAQ LVVRDGEGAT KFVTVNVQGA SSFSDAHRVA
     SKISTSALVK TALYGEDANW GRVLAASGSV QLSIPLDPTR VSVTFVPADG STPLPVLVEG
     EPEQVDEVRA KEILSEEDFE IKVELGLGKE SAKYWTCDFS YEYVSINGDY RS
//
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