ID A0A066WR27_TILAU Unreviewed; 513 AA.
AC A0A066WR27;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=K437DRAFT_218941 {ECO:0000313|EMBL:KDN53449.1};
OS Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN53449.1, ECO:0000313|Proteomes:UP000027361};
RN [1] {ECO:0000313|EMBL:KDN53449.1, ECO:0000313|Proteomes:UP000027361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBC 951 {ECO:0000313|EMBL:KDN53449.1,
RC ECO:0000313|Proteomes:UP000027361};
RG DOE Joint Genome Institute;
RA Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT 951.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDN53449.1}.
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DR EMBL; JMSN01000002; KDN53449.1; -; Genomic_DNA.
DR RefSeq; XP_013246288.1; XM_013390834.1.
DR AlphaFoldDB; A0A066WR27; -.
DR STRING; 1037660.A0A066WR27; -.
DR GeneID; 25262213; -.
DR HOGENOM; CLU_027172_1_0_1; -.
DR InParanoid; A0A066WR27; -.
DR OMA; DYVHENS; -.
DR OrthoDB; 45829at2759; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000027361; 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:UP000027361};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03124}.
FT CHAIN 1..244
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT /id="PRO_5023354717"
FT CHAIN 245..513
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT /id="PRO_5023354716"
FT ACT_SITE 245
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 508
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 513
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT SITE 160
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 161
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 244..245
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
SQ SEQUENCE 513 AA; 53845 MW; 1B965F0DE58D10EA CRC64;
MDNKAARFVL PINKEALPRG FSVSATYGGI KAAISPKLTA PSSTSSPSAP PLDPKPDVAL
IVSAVPASAA GTFTQNAFKA APVLFSSAVL SNPSNKGKVR SVLVNSGCAN AVTGDQGYRD
AQQCANMVQQ LLSPAPGLKS SAEKGETEAK SADDTLVLST GVIGVPLPMP VFKKTLPFLA
SGQILRNDEE AWYQVARAFM TTDTFPKLRT RTFQLAGMEC KMVGIDKGAG MIHPAMSGPS
GLHATLLGLI ATDAPIEAAS LQQALEHAVS RSFNCISVDG DMSTNDTILI LANGQAVNQS
SSSSSTAQLS PSEEISALSH PQEFAHFQSE LTAFCTELSH LIVRDGEGAT KFVSINVRGA
PTYAHAHAIA SSISTSALVK CALHGADANW GRVLCAVGYA KLPPFTGATQ QGSSEAWAID
PTRVTVSFEL PPTLSSSEAR TADVQPLTVL ENGTPQEVDE DAAARLLSLE DISIVVDLQG
GSWGQQQGVR EEATYWTCDF SKEYIAINGD YRS
//
