ID   ARGD_EREGS              Reviewed;         423 AA.
AC   Q75AW1;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 123.
DE   RecName: Full=Acetylornithine aminotransferase, mitochondrial;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
DE   Flags: Precursor;
GN   Name=ARG8; OrderedLocusNames=ADL191W;
OS   Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Ashbya gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-
CC         glutamate 5-semialdehyde + L-glutamate; Xref=Rhea:RHEA:18049,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57805; EC=2.6.1.11;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 4/4.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AE016817; AAS51729.1; -; Genomic_DNA.
DR   RefSeq; NP_983905.1; NM_209258.1.
DR   AlphaFoldDB; Q75AW1; -.
DR   SMR; Q75AW1; -.
DR   FunCoup; Q75AW1; 300.
DR   STRING; 284811.Q75AW1; -.
DR   EnsemblFungi; AAS51729; AAS51729; AGOS_ADL191W.
DR   GeneID; 4620047; -.
DR   KEGG; ago:AGOS_ADL191W; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_016922_10_1_1; -.
DR   InParanoid; Q75AW1; -.
DR   OMA; MVPGFKY; -.
DR   OrthoDB; 5419315at2759; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000004; Acetylornithine aminotransferase; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR   InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR050103; Class-III_PLP-dep_AT.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00707; argD; 1.
DR   NCBIfam; NF002325; PRK01278.1; 1.
DR   PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis;
KW   Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..423
FT                   /note="Acetylornithine aminotransferase, mitochondrial"
FT                   /id="PRO_0000002076"
FT   MOD_RES         276
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   423 AA;  46111 MW;  BF6D07FEC096BCBB CRC64;
     MVNQRVVHLC AKRSFSLTAS MQKYFVDVYA KPDLVLTRGR GSRLFDDVNK REYIDFVAGI
     AVTSLGHSDP AIAEVIAAQS ATLVHTSNLF HNSEALKFAE KLVESTKRFG GQQDAEKVYF
     CNSGTEANEA ALKFSRRRAL RTDPQKQGFI AFENSFHGRT MGSLSVTSKA KYRLPFGDMV
     PHVTFLNIHD PVEKLVSFIV ENAPKTAAMI LEPIQGEGGV HRVPEDKLVA LGRLCKKHDI
     VLIYDEIQCG LGRTGKLWAH SNLPADAHPD IFTTAKALGN GFPMGATVVN SKVNEVLSVG
     DHGTTYGGNP LACAVGNHVL DRIAQQPFLD DVKAKANVFT AGLLALQKKY PFIREIRGDG
     LLIGVEFTVD VSDIISKSRE RGLLITAAGP NTLRIIPALT IEEDTIRQGL EILESVVGEI
     SSS
//