OAT_PLACH
ID OAT_PLACH Reviewed; 414 AA.
AC Q4XWV5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=PC001183.02.0;
OS Plasmodium chabaudi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5825;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS;
RX PubMed=15637271; DOI=10.1126/science.1103717;
RA Hall N., Karras M., Raine J.D., Carlton J.M., Kooij T.W.A., Berriman M.,
RA Florens L., Janssen C.S., Pain A., Christophides G.K., James K.,
RA Rutherford K., Harris B., Harris D., Churcher C.M., Quail M.A., Ormond D.,
RA Doggett J., Trueman H.E., Mendoza J., Bidwell S.L., Rajandream M.A.,
RA Carucci D.J., Yates J.R. III, Kafatos F.C., Janse C.J., Barrell B.G.,
RA Turner C.M.R., Waters A.P., Sinden R.S.;
RT "A comprehensive survey of the Plasmodium life cycle by genomic,
RT transcriptomic, and proteomic analyses.";
RL Science 307:82-86(2005).
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; CAAJ01002561; CAH78606.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4XWV5; -.
DR SMR; Q4XWV5; -.
DR VEuPathDB; PlasmoDB:PCHAS_0108000; -.
DR eggNOG; KOG1402; Eukaryota.
DR HOGENOM; CLU_016922_10_3_1; -.
DR InParanoid; Q4XWV5; -.
DR UniPathway; UPA00098; UER00358.
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 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Disulfide bond; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..414
FT /note="Ornithine aminotransferase"
FT /id="PRO_0000233394"
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; 46043 MW; 56781653F6E20385 CRC64;
MEFVKDLKTP EDYINNELKY GAHNYDPIPV VLKRAKGVFV YDVNDKRYYD FLSAYSSVNQ
GHCHPDILNA MINQAKNLTI CSRAFFSVSL GICERYLTNL LGYDKVLMMN TGAEANETAY
KLCRKWGYEV KKIPENMAKI VVCKNNFSGR TLGCISASTT NKCTSNFGPF APQFSKVPYN
DLEALEEELK DPNVCGFIVE PVQGEAGVIV PSDNYLPGVY NLCKKYNVLF VADEVQTGLG
RTGKLLCVHH YNVKPDVVLL GKALSGGHYP ISAVLANDSV MLVIKPGEHG STYGGNPLAA
SICVESLNVL INEKLCENAD KLGGPFLEGL KKELKDSKII RDIRGKGLLC AIEFKNELVN
VLDICLKLKE NGLITRDVHD KTIRLTPPLC ITKEQLDECT EIIVKTVKFF DEKF
