OAT_PLAYO
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 25-MAY-2022, entry version 101.
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; 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 = 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: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}.
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DR EMBL; AABL01000033; EAA20544.1; -; Genomic_DNA.
DR PDB; 1Z7D; X-ray; 2.10 A; A/B/C/D/E/F=1-414.
DR PDBsum; 1Z7D; -.
DR AlphaFoldDB; Q7RT90; -.
DR SMR; Q7RT90; -.
DR STRING; 73239.Q7RT90; -.
DR EnsemblProtists; EAA20544; EAA20544; EAA20544.
DR InParanoid; Q7RT90; -.
DR OMA; DVFPRFA; -.
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: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 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 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
