ID   OAT_CAEEL               Reviewed;         422 AA.
AC   Q18040;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 3.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Probable ornithine aminotransferase, mitochondrial;
DE            EC=2.6.1.13 {ECO:0000250|UniProtKB:Q6CWC1};
DE   AltName: Full=Ornithine--oxo-acid aminotransferase;
DE   Flags: Precursor;
GN   Name=oatr-1 {ECO:0000312|WormBase:C16A3.10};
GN   ORFNames=C16A3.10 {ECO:0000312|WormBase:C16A3.10};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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         Evidence={ECO:0000250|UniProtKB:Q6CWC1};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P04181};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC       {ECO:0000250|UniProtKB:Q6CWC1}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P04181}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; FO080367; CCD63230.1; -; Genomic_DNA.
DR   PIR; G88481; G88481.
DR   RefSeq; NP_741194.1; NM_171877.3.
DR   AlphaFoldDB; Q18040; -.
DR   SMR; Q18040; -.
DR   BioGRID; 41126; 3.
DR   IntAct; Q18040; 1.
DR   STRING; 6239.C16A3.10a.1; -.
DR   EPD; Q18040; -.
DR   PaxDb; Q18040; -.
DR   PeptideAtlas; Q18040; -.
DR   EnsemblMetazoa; C16A3.10.1; C16A3.10.1; WBGene00015814.
DR   EnsemblMetazoa; C16A3.10.2; C16A3.10.2; WBGene00015814.
DR   GeneID; 175908; -.
DR   KEGG; cel:CELE_C16A3.10; -.
DR   UCSC; C16A3.10c.2; c. elegans.
DR   CTD; 175908; -.
DR   WormBase; C16A3.10; CE04010; WBGene00015814; oatr-1.
DR   eggNOG; KOG1402; Eukaryota.
DR   GeneTree; ENSGT00630000089895; -.
DR   HOGENOM; CLU_016922_10_3_1; -.
DR   InParanoid; Q18040; -.
DR   OMA; DVFPRFA; -.
DR   OrthoDB; 145181at2759; -.
DR   PhylomeDB; Q18040; -.
DR   Reactome; R-CEL-8964539; Glutamate and glutamine metabolism.
DR   UniPathway; UPA00098; UER00358.
DR   PRO; PR:Q18040; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00015814; Expressed in adult organism and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IBA:GO_Central.
DR   GO; GO:0010121; P:arginine catabolic process to proline via ornithine; IBA:GO_Central.
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   3: Inferred from homology;
KW   Aminotransferase; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..422
FT                   /note="Probable ornithine aminotransferase, mitochondrial"
FT                   /id="PRO_0000001266"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04181"
SQ   SEQUENCE   422 AA;  46454 MW;  E8FE04CB307CC464 CRC64;
     MLSSLRRVVP SLPRGSRSLT SQQIFDREKK FGCHNYKPLP VALSKGEGCF VWDVEGKKYF
     DFLAAYSAVN QGHCHPKLLK VVQEQASTLT LTSRAFYNNV LGEYEEYVTK LFKYDKVLPM
     NTGVEACESA VKLARRWAYD VKGVKDNEAV VVFAENNFWG RSIAAISAST DPDSFARFGP
     FVPGFKTVPY NNLKAVEDAI KDKNVAAFMV EPIQGEAGVV LPDPGYLKGV SDLCKKYNVL
     FITDEVQSGL GRSGKLLAHY HDNVRPDIVV LGKALSGGFY PVSAVLCDDN VMMNIKPGEH
     GSTYGGNPLA CKVAIAALEI LQEEKLVENS AVMGDLLMSK LKTLPKDIVS TVRGKGLFCA
     IVINKKYDAW KVCLKLKENG LLAKNTHGDI IRFAPPLCIN KEQVEQAADI IIKTVTDFAK
     QN