ID   OAT_DICDI               Reviewed;         416 AA.
AC   Q54JP5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Probable ornithine aminotransferase;
DE            EC=2.6.1.13;
DE   AltName: Full=Ornithine--oxo-acid aminotransferase;
GN   Name=oatA; ORFNames=DDB_G0287913;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AAFI02000104; EAL63485.1; -; Genomic_DNA.
DR   RefSeq; XP_636989.1; XM_631897.1.
DR   AlphaFoldDB; Q54JP5; -.
DR   SMR; Q54JP5; -.
DR   STRING; 44689.DDB0231478; -.
DR   PaxDb; Q54JP5; -.
DR   EnsemblProtists; EAL63485; EAL63485; DDB_G0287913.
DR   GeneID; 8626361; -.
DR   KEGG; ddi:DDB_G0287913; -.
DR   dictyBase; DDB_G0287913; oatA.
DR   eggNOG; KOG1402; Eukaryota.
DR   HOGENOM; CLU_016922_10_3_1; -.
DR   InParanoid; Q54JP5; -.
DR   OMA; DVFPRFA; -.
DR   PhylomeDB; Q54JP5; -.
DR   Reactome; R-DDI-8964539; Glutamate and glutamine metabolism.
DR   UniPathway; UPA00098; UER00358.
DR   PRO; PR:Q54JP5; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004587; F:ornithine-oxo-acid transaminase activity; ISS:dictyBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IBA:GO_Central.
DR   GO; GO:0010121; P:arginine catabolic process to proline via ornithine; IBA:GO_Central.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006591; P:ornithine metabolic process; IC:dictyBase.
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; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..416
FT                   /note="Probable ornithine aminotransferase"
FT                   /id="PRO_0000327775"
FT   MOD_RES         267
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  45752 MW;  3C7765B82E5073D3 CRC64;
     MDPISSQIQE CTSKELIEME SEFAAHTYHP IPVVFKKASG VHVWDVEEKQ YFDFLSAYSA
     VNQGHSHPKI VSALITQAQK CALSSRAFYN EVFPQYAKYI TEYFGYEMVL PMNTGAEAVE
     TSIKLARRWG YVKKGIAEDQ AIVISCKGCF HGRTIGVISM SDDPSSYNKY GPLMNGIIKI
     DYNSTQQLEE VLSQHADRVC GFIVEPIQGE AGVVVPDEGY LKKCYELCKK YNVLLVADEI
     QTGLCRTGRM LCSDWDGIKP DLVLLGKAIS GGLLPISAVL GGKDVMLTIK PGEHGSTYGG
     SPLASAVAMA ALDVLRDENL AENAQKLGEH FRAQISNINH PAIQLVRGKG LLNAIVIDPN
     FTVSAWDICI KFAENGLLAK PTHDNIIRLA PPLTITLEQI DQCVSIIKKV FDSFKN