ID   ARGD_CANGA              Reviewed;         427 AA.
AC   Q6FXA4;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Acetylornithine aminotransferase, mitochondrial;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
DE   Flags: Precursor;
GN   Name=ARG8; OrderedLocusNames=CAGL0B01507g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-
CC         acetyl-L-glutamate 5-semialdehyde; 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; CR380948; CAG57935.1; -; Genomic_DNA.
DR   RefSeq; XP_445035.1; XM_445035.1.
DR   AlphaFoldDB; Q6FXA4; -.
DR   SMR; Q6FXA4; -.
DR   STRING; 5478.XP_445035.1; -.
DR   EnsemblFungi; CAG57935; CAG57935; CAGL0B01507g.
DR   GeneID; 2886668; -.
DR   KEGG; cgr:CAGL0B01507g; -.
DR   CGD; CAL0127072; ARG8.
DR   VEuPathDB; FungiDB:CAGL0B01507g; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_016922_10_1_1; -.
DR   InParanoid; Q6FXA4; -.
DR   OMA; PFMVPTY; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000002428; Chromosome B.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:EnsemblFungi.
DR   GO; GO:0006592; P:ornithine biosynthetic process; IEA:EnsemblFungi.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01107; ArgD_aminotrans_3; 1.
DR   InterPro; IPR004636; AcOrn/SuccOrn_fam.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00707; argD; 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           ?..427
FT                   /note="Acetylornithine aminotransferase, mitochondrial"
FT                   /id="PRO_0000002077"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   427 AA;  46824 MW;  BF964B26B2221362 CRC64;
     MYKRYFSTSL KTNQQALKKI LEEKTYQVTT YARPSDLCIT RGLNAKLFDD FNNKEYIDFT
     AGIAVTALGH ANPKVAEILQ TQATKLVHSS NLYFTKECLD LSEKLIEKTK KFGGQHDASK
     VFLCNSGTEA NEAALKFAKK HGITKNPKKQ GIIAFENSFH GRTMGALSVT WNKKYRTPFG
     DLVPHVSFLN INDELSKIKD FINTKKDEIA GLIIEPIQGE GGIFPIPIEK LVALKEICQK
     NDIIVIYDEI QCGLGRTGNL WAHAALPKAA HPDIFTSAKA LGNGFPIAAT VVNEKVNNAL
     QVGDHGTTYG GNPLGCAVSN YVLDVIGDQA FLDSVTKKGE LLKKGLLKIK EQHPDKISDV
     RGSGLIWGVE FKDAPGAIVQ KARELGLLVI TAGKTTVRFV PSLTIEDEVV EEGLTIFNKA
     VNDVFSK