ID   OAT_VIGAC               Reviewed;         426 AA.
AC   P31893;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Ornithine aminotransferase;
DE            EC=2.6.1.13;
DE   AltName: Full=Ornithine--oxo-acid aminotransferase;
OS   Vigna aconitifolia (Moth bean) (Phaseolus aconitifolius).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8103048; DOI=10.1016/s0021-9258(17)46682-8;
RA   Delauney A.J., Hu C.A.A., Kishor P.B.K., Verma D.P.S.;
RT   "Cloning of ornithine delta-aminotransferase cDNA from Vigna aconitifolia
RT   by trans-complementation in Escherichia coli and regulation of proline
RT   biosynthesis.";
RL   J. Biol. Chem. 268:18673-18678(1993).
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   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; L08400; AAA02916.1; -; mRNA.
DR   PIR; A48515; A48515.
DR   AlphaFoldDB; P31893; -.
DR   SMR; P31893; -.
DR   PRIDE; P31893; -.
DR   BRENDA; 2.6.1.13; 6650.
DR   UniPathway; UPA00098; UER00358.
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   2: Evidence at transcript level;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..426
FT                   /note="Ornithine aminotransferase"
FT                   /id="PRO_0000120496"
FT   MOD_RES         291
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   426 AA;  48139 MW;  F648041B3093FE87 CRC64;
     MFKPHLLAVV SRCNSFFGCV DICCNWGNSA PRTLKGLKSV TSEQVFEREQ KYGAHNYHHC
     SAYRAKGVSL DMEGKRYFDF LSAYSAVNQG HCHPKIVNTM VEQAQRLTLT SRAFYTDVLG
     EYEEFLTKLF NYDKVLPMNT GVEGGETACK IARCWAYMKK KVPENQAKII FAENNFWGRT
     LSAISASTDP MSYDELRPYM PGFEIVKYND TAALEKAFQD PNVCAYMVEP IQGEAGVVAL
     DAGYLTEVRE LCTKYNVLFI ADEVQTGLAR TGRMLAVDHE DVKPDLLILG KALSGGLYPV
     SAVLRDDHIM DCIQPGLHTA MDVMDPRMRI LAASRYYVRV ARERCENAQI QATYLRKELN
     TLPKDVVPVV RGKGLLNAIV INKKFDAWDV CLNLCKPTHG DIIRFATTGH HRGTDPRMCQ
     YYQKYH