ID   B5VRC1_YEAS6            Unreviewed;       423 AA.
AC   B5VRC1;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Acetylornithine aminotransferase, mitochondrial {ECO:0000256|ARBA:ARBA00021753};
DE            EC=2.6.1.11 {ECO:0000256|ARBA:ARBA00012919};
GN   ORFNames=AWRI1631_150230 {ECO:0000313|EMBL:EDZ69516.1};
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ69516.1, ECO:0000313|Proteomes:UP000008988};
RN   [1] {ECO:0000313|EMBL:EDZ69516.1, ECO:0000313|Proteomes:UP000008988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ69516.1,
RC   ECO:0000313|Proteomes:UP000008988};
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00005024}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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:EDZ69516.1}.
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DR   EMBL; ABSV01002077; EDZ69516.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VRC1; -.
DR   UniPathway; UPA00068; UER00109.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00707; argD; 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; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ   SEQUENCE   423 AA;  46706 MW;  F460D6ED11AA880B CRC64;
     MFKRYLSSTS SRRFTSILEE KAFQVTTYSR PEDLCITRGK NAKLYDDVNG KEYIDFTAGI
     AVTALGHANP KVAEILHHQA NKLIHSSNLY FTKECLDLSE KIVEKTKQFG GQHDASRVFL
     CNSGTEANEA ALKFAKKHGI MKNPSKQGIV AFENSFHGRT MGALSVTWNS KYRTPFGDLV
     PHVSFLNLND EMTKLQSYIE TKKDEIAGLI VEPIQGEGGV FPVEVEKLTG LKKICQNNDV
     IVIHDEIQCG LGRSGKLWAH AYLPSEAHPD IFTSAKALGN GFPIAATIVN EKVNNALRVG
     DHGTTYGGNP LACSVSNYVL DTIADETFLK QVSKKSDILQ KRLREIQAKY PNQIKTIRGK
     GLILGAEFVE PPTEVIKKAR ELGLLIITAG KSTVRFVPAL TIEDELIEEG MDAFEKAIEA
     VYA
//