ID   OAT_PLAFD               Reviewed;         414 AA.
AC   Q07805;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000303|PubMed:8264733};
DE            Short=PfOAT {ECO:0000303|PubMed:8264733};
DE            EC=2.6.1.13 {ECO:0000250|UniProtKB:Q6LFH8};
DE   AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000305};
GN   Name=OAT {ECO:0000303|PubMed:8264733};
OS   Plasmodium falciparum (isolate CDC / Honduras).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5836;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8264733; DOI=10.1016/0166-6851(93)90076-a;
RA   Schmid S.R., Linder P., Reese R.T., Stanley H.A.;
RT   "Characterization of a putative ornithine aminotransferase gene of
RT   Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 61:311-314(1993).
CC   -!- FUNCTION: The enzyme has a very narrow substrate specificity and can
CC       only catalyze the transamination of alpha-ketoglutarate with ornithine
CC       or N-acetylornithine and, to a lesser extent, of glutamate-5-
CC       semialdehyde with glutamate and alanine.
CC       {ECO:0000250|UniProtKB:Q6LFH8}.
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:Q6LFH8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-ornithine = L-glutamate + L-glutamate 5-
CC         semialdehyde; Xref=Rhea:RHEA:25160, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066; EC=2.6.1.13;
CC         Evidence={ECO:0000250|UniProtKB:Q6LFH8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25161;
CC         Evidence={ECO:0000250|UniProtKB:Q6LFH8};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P04181};
CC   -!- ACTIVITY REGULATION: Unlike for mammalian OATs, activity is increased
CC       by TRX1-mediated reduction of the disulfide bond between Cys-154 and
CC       Cys-163. Binding to TRX1 may also induce conformational changes that
CC       facilitate substrate binding. {ECO:0000250|UniProtKB:Q6LFH8}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC       {ECO:0000250|UniProtKB:Q6LFH8}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6LFH8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: The disulfide bond between Cys-154 and Cys-163 is reduced by TRX1
CC       which increases OAT catalytic activity. {ECO:0000250|UniProtKB:Q6LFH8}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; L15426; AAA16481.1; -; mRNA.
DR   AlphaFoldDB; Q07805; -.
DR   SMR; Q07805; -.
DR   PRIDE; Q07805; -.
DR   UniPathway; UPA00098; UER00358.
DR   EvolutionaryTrace; Q07805; -.
DR   GO; GO:0005737; C:cytoplasm; 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   PANTHER; PTHR11986:SF18; PTHR11986:SF18; 1.
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; Cytoplasm; Disulfide bond; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..414
FT                   /note="Ornithine aminotransferase"
FT                   /id="PRO_0000120495"
FT   MOD_RES         262
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04181"
FT   DISULFID        154..163
FT                   /note="Reversible"
FT                   /evidence="ECO:0000250|UniProtKB:Q6LFH8"
SQ   SEQUENCE   414 AA;  46055 MW;  EA2264D1FA264DBF CRC64;
     MDFVKELKSS QDYMNNELTY GAHNYDPIPV VLKRGKGVFV YDIEDRRYYD FLSAYSSVNQ
     GHCHPDILNA MINQAKKLTI CSRAFFSDSL GVCERYLTNL FGYDKVLMMN TGAEASETAY
     KLCRKWGYEV KKIPENSAKI IVCNNNFSGR TLGCVSASTD KKCKNNFGPF VPNFLKVPYD
     DLEALEKELQ DPNVCAFIVE PVQGEAGVIV PSDSYFPGVA SLCKKYNVLF VADEVQTGLG
     RTGKLLCTHH YGVKPDVILL GKALSGGHYP ISAILANDDV MLVLKPGEHG STYGGNPLAA
     AICVEALKVL INEKLCENAD KLGAPFLQNL KEQLKDSKVV REVRGKGLLC AIEFKNDLVN
     VWDICLKFKE NGLITRSVHD KTVRLTPPLC ITKEQLDECT EIIVKTVKFF DDNL