ID A0A3N2PXH8_9PEZI Unreviewed; 460 AA.
AC A0A3N2PXH8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 13-SEP-2023, entry version 12.
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=SODALDRAFT_332615 {ECO:0000313|EMBL:ROT39192.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT39192.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT39192.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT39192.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
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: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; EC=2.3.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00000498, ECO:0000256|HAMAP-
CC 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:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_03124}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000256|HAMAP-
CC 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 from a
CC single precursor protein within the mitochondrion. {ECO:0000256|HAMAP-
CC Rule:MF_03124}.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|ARBA:ARBA00006774,
CC ECO:0000256|HAMAP-Rule:MF_03124}.
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DR EMBL; ML119054; ROT39192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2PXH8; -.
DR STRING; 1314773.A0A3N2PXH8; -.
DR OrthoDB; 45829at2759; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000272025; 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; 3.30.2330.10; arginine biosynthesis bifunctional protein suprefamily; 1.
DR Gene3D; 3.10.20.340; ArgJ beta chain, C-terminal domain; 1.
DR Gene3D; 3.60.70.12; L-amino peptidase D-ALA esterase/amidase; 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 NCBIfam; TIGR00120; ArgJ; 1.
DR PANTHER; PTHR23100; ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ; 1.
DR PANTHER; PTHR23100:SF0; ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ, MITOCHONDRIAL; 1.
DR Pfam; PF01960; ArgJ; 1.
DR SUPFAM; SSF56266; DmpA/ArgJ-like; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_03124};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_03124};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_03124};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW Rule:MF_03124};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03124};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_03124}; Reference proteome {ECO:0000313|Proteomes:UP000272025};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03124}.
FT CHAIN 1..228
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT /id="PRO_5023531369"
FT CHAIN 229..460
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT /id="PRO_5023531368"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 460
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT SITE 150
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT SITE 151
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT SITE 228..229
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
SQ SEQUENCE 460 AA; 48580 MW; 51860A438F560B5A CRC64;
MPGSLNVFPS QLTRFVRCYS VAAESIPAAK KKYVPSEGTY PLGFKASGIL VGVKPGNTTK
PDLALISSDR PCAAAAVFTK NKFQAAPVTF SRDVLKKKGN QGIRSVLINS GCANAVTGKG
GLEDASLMAR AADETVGNSE DGSSTIVMST GVIGQRLPID KIIKNVPAAH DVLGSSHKDW
LACATAICTT DTFPKLMSKT FTLPSSPGVE YRIAGMTKGA GMIHPNMATL LGVAATDAPI
SPTVMPTVLK QAVDRSFNSI TIDGDTSTND TVALLANGAA GGKEIRSEDS PDFAAFQEVL
TDFAVDLAKL IVRDGEGATK FVTIRVTEAA SEDAARKIAS TIARSPLVKT ALYGRDANWG
RILCATGYSL ISEPGHAVAE VPEIIPENTN VSFIPTDGTA ELKLLVNGEP ELVDESRASE
ILELEDLEIL VRLGTGGKEA TYWTCDYSHE YITINGDYRT
//
