ID   ARGD_KLULA              Reviewed;         423 AA.
AC   O14433; Q6CMD6;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   25-MAY-2022, entry version 143.
DE   RecName: Full=Acetylornithine aminotransferase, mitochondrial;
DE            Short=ACOAT;
DE            EC=2.6.1.11;
DE   Flags: Precursor;
GN   Name=ARG8; OrderedLocusNames=KLLA0E21153g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CK56-7A;
RX   PubMed=9544247;
RX   DOI=10.1002/(sici)1097-0061(199802)14:3<281::aid-yea212>3.0.co;2-e;
RA   Janssen A., Chen X.J.;
RT   "Cloning, sequencing and disruption of the ARG8 gene encoding
RT   acetylornithine aminotransferase in the petite-negative yeast Kluyveromyces
RT   lactis.";
RL   Yeast 14:281-285(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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   -!- 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; U93209; AAC49934.1; -; Genomic_DNA.
DR   EMBL; CR382125; CAG99990.1; -; Genomic_DNA.
DR   PIR; T50923; T50923.
DR   RefSeq; XP_454903.1; XM_454903.1.
DR   AlphaFoldDB; O14433; -.
DR   SMR; O14433; -.
DR   STRING; 28985.XP_454903.1; -.
DR   PRIDE; O14433; -.
DR   EnsemblFungi; CAG99990; CAG99990; KLLA0_E21077g.
DR   GeneID; 2894291; -.
DR   KEGG; kla:KLLA0_E21077g; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_016922_10_1_1; -.
DR   InParanoid; O14433; -.
DR   OMA; PFMVPTY; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000000598; Chromosome E.
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           ?..423
FT                   /note="Acetylornithine aminotransferase, mitochondrial"
FT                   /id="PRO_0000002079"
FT   MOD_RES         276
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        227
FT                   /note="T -> S (in Ref. 1; AAC49934)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   423 AA;  46641 MW;  AF0495431184440D CRC64;
     MRVIRQLHTS KRLLQSLVDK QKYQATTYAR PNHLVLTRGK NAILYDDVNN KEYIDFTAGI
     AVTALGHANP EVAEIMYKQS KKLIHSSNLY YNEECLKLSE NLVEATKSFG GQYDASRVFL
     CNSGTEANEA ALKFAKRYGI LKSPSKQGII AFQNSFHGRT MGALSVTSNP KYREPFGSLI
     PGVEFLNIND ELTKLDQQVS SLKEKTAGLI VEPIQGEGGV FPIPLDTLVG LKKICEDHDI
     IVIYDEIQCG LGRSGKLWAH SYLPKEAHPD IFTTAKALGN GFPIAATVTN DKVNDILKVG
     DHGTTYGGNP LGSAVGNYVV NVIAEQKFLD EVNKKGEIIT NRLRKLQERF PEHIKDIRGK
     GLMIGCDFDE APAKIVDAAR DSGLLIITAG KTTVRFVPAL TIEDNLLEKG LNIFEKAVEK
     VYS