ID   OAT_PLAYO               Reviewed;         414 AA.
AC   Q7RT90;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   02-SEP-2026, entry version 117.
DE   RecName: Full=Ornithine aminotransferase {ECO:0000250|UniProtKB:Q6LFH8};
DE            EC=2.6.1.13 {ECO:0000250|UniProtKB:Q6LFH8};
DE   AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000305};
GN   Name=OAT {ECO:0000250|UniProtKB:Q6LFH8}; ORFNames=PY00104;
OS   Plasmodium yoelii yoelii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Vinckeia.
OX   NCBI_TaxID=73239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17XNL;
RX   PubMed=12368865; DOI=10.1038/nature01099;
RA   Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA   Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA   Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA   Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA   Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D.,
RA   Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W.,
RA   Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA   Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA   Carucci D.J.;
RT   "Genome sequence and comparative analysis of the model rodent malaria
RT   parasite Plasmodium yoelii yoelii.";
RL   Nature 419:512-519(2002).
RN   [2] {ECO:0007744|PDB:1Z7D}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
RX   PubMed=17125854; DOI=10.1016/j.molbiopara.2006.10.011;
RA   Vedadi M., Lew J., Artz J., Amani M., Zhao Y., Dong A., Wasney G.A.,
RA   Gao M., Hills T., Brokx S., Qiu W., Sharma S., Diassiti A., Alam Z.,
RA   Melone M., Mulichak A., Wernimont A., Bray J., Loppnau P., Plotnikova O.,
RA   Newberry K., Sundararajan E., Houston S., Walker J., Tempel W.,
RA   Bochkarev A., Kozieradzki I., Edwards A., Arrowsmith C., Roos D., Kain K.,
RA   Hui R.;
RT   "Genome-scale protein expression and structural biology of Plasmodium
RT   falciparum and related Apicomplexan organisms.";
RL   Mol. Biochem. Parasitol. 151:100-110(2007).
CC   -!- FUNCTION: Catalyzes the transamination of alpha-ketoglutarate with
CC       ornithine or N-acetylornithine and of glutamate-5-semialdehyde with
CC       glutamate and alanine. {ECO:0000250|UniProtKB:Q6LFH8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + L-ornithine = L-glutamate 5-semialdehyde
CC         + an L-alpha-amino acid; 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=L-ornithine + 2-oxoglutarate = L-glutamate 5-semialdehyde + L-
CC         glutamate; 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:P04181}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P04181}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABL01000033; EAA20544.1; -; Genomic_DNA.
DR   PDB; 1Z7D; X-ray; 2.10 A; A/B/C/D/E/F=1-414.
DR   AlphaFoldDB; Q7RT90; -.
DR   SMR; Q7RT90; -.
DR   FunCoup; Q7RT90; 153.
DR   STRING; 73239.Q7RT90; -.
DR   PaxDb; 73239-Q7RT90; -.
DR   EnsemblProtists; EAA20544; EAA20544; EAA20544.
DR   KEGG; pyo:PY17X_0109000; -.
DR   VEuPathDB; PlasmoDB:Py17XNL_000104751; -.
DR   InParanoid; Q7RT90; -.
DR   UniPathway; UPA00098; UER00358.
DR   EvolutionaryTrace; Q7RT90; -.
DR   Proteomes; UP000008553; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter.
DR   GO; GO:0004587; F:L-ornithine transaminase activity; ISS:UniProtKB.
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   FunFam; 3.40.640.10:FF:000011; Ornithine aminotransferase; 1.
DR   FunFam; 3.90.1150.10:FF:000152; Ornithine aminotransferase; 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   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR050103; Class-III_PLP-dep_AT.
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   NCBIfam; TIGR01885; Orn_aminotrans; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR   PDBsum; 1Z7D; -.
PE   1: Evidence at protein level;
KW   3D-structure; Aminotransferase; Cytoplasm; Disulfide bond;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..414
FT                   /note="Ornithine aminotransferase"
FT                   /id="PRO_0000233396"
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"
FT   HELIX           10..20
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          28..37
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          47..52
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           53..56
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   TURN            57..60
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           65..75
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           88..101
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          104..111
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           112..129
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          139..143
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           182..189
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          194..199
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          201..204
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   TURN            205..207
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           215..225
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          229..233
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   TURN            235..242
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          243..246
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           247..251
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           262..265
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          272..276
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           278..281
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   TURN            292..295
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           297..312
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           315..334
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          340..346
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          349..354
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   TURN            356..358
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           361..370
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   TURN            379..381
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   STRAND          382..385
FT                   /evidence="ECO:0007829|PDB:1Z7D"
FT   HELIX           393..410
FT                   /evidence="ECO:0007829|PDB:1Z7D"
SQ   SEQUENCE   414 AA;  46267 MW;  65800F4730BD8B84 CRC64;
     MEFVKDLKTP EDYINNELKY GAHNYDPIPV VLKRAKGVFV YDVNDKRYYD FLSAYSSVNQ
     GHCHPNILNA MINQAKNLTI CSRAFFSVPL GICERYLTNL LGYDKVLMMN TGAEANETAY
     KLCRKWGYEV KKIPENMAKI VVCKNNFSGR TLGCISASTT KKCTSNFGPF APQFSKVPYD
     DLEALEEELK DPNVCAFIVE PIQGEAGVIV PSDNYLQGVY DICKKYNVLF VADEVQTGLG
     RTGKLLCVHH YNVKPDVILL GKALSGGHYP ISAVLANDDI MLVIKPGEHG STYGGNPLAA
     SICVEALNVL INEKLCENAE KLGGPFLENL KRELKDSKIV RDVRGKGLLC AIEFKNELVN
     VLDICLKLKE NGLITRDVHD KTIRLTPPLC ITKEQLDECT EIIVKTVKFF DERF
//