ID   OAT_DROAN               Reviewed;         432 AA.
AC   P49724;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Ornithine aminotransferase, mitochondrial;
DE            EC=2.6.1.13;
DE   AltName: Full=Ornithine--oxo-acid aminotransferase;
DE   Flags: Precursor;
GN   Name=Oat;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   PubMed=9248043; DOI=10.1266/ggs.72.9;
RA   Yoshida K.M., Hori S.H.;
RT   "Molecular cloning and characterization of Drosophila ornithine
RT   aminotransferase gene.";
RL   Genes Genet. Syst. 72:9-17(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-
CC         glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:46911, ChEBI:CHEBI:58066, ChEBI:CHEBI:59869; EC=2.6.1.13;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; D50331; BAA08868.1; -; mRNA.
DR   AlphaFoldDB; P49724; -.
DR   SMR; P49724; -.
DR   STRING; 7217.FBpp0113910; -.
DR   PRIDE; P49724; -.
DR   eggNOG; KOG1402; Eukaryota.
DR   UniPathway; UPA00098; UER00358.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR010164; Orn_aminotrans.
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; TIGR01885; Orn_aminotrans; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Mitochondrion; Pyridoxal phosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..432
FT                   /note="Ornithine aminotransferase, mitochondrial"
FT                   /id="PRO_0000001267"
FT   MOD_RES         287
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   432 AA;  47376 MW;  242B3BA1326FDE66 CRC64;
     MFSKLSTRGI ATRIGYLAQK AASQETAAPA AGSLSETVFA RENKYGAHNY HPLPVALSKG
     EGVFVWDVEG KRYFDYLSAY SAVNQGHCHP KIVKALTEQA SKLALTSRAF YSDVLGEYEE
     YVTKLFGFDK VLPMNTGVEG GETACKLARK WGYLQKKIPE NQAKIIFARN NFWGRTLSAV
     SASNDPSSYE GFGPFMPGFE LIEYDNVTAL EEALKDPNVC AFMVEPIQGE RGVVVPSDGY
     LKKVRELCSK NNVLWIADEV QTGLARTGKL LAVNYEDVQP DILILGKALS GGLYPVSAVL
     CNDPVMLCIK PGEHGSTYGG NPLGCRVAMA ALEVLQEEKL AENAFKMGEL LRSELSTLPK
     DVVSVVRGKG LLNAIVINEK YDAWKVCLKL KENGLLAKPT HGDIIRFAPP LVIMNPRLRE
     SIEIIKKTIL SM