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 27-MAR-2024, entry version 120.
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 (Social amoeba).
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.Q54JP5; -.
DR PaxDb; 44689-DDB0231478; -.
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; RSAWDLC; -.
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:0004587; F:ornithine aminotransferase 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; 3.90.1150.10; 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; 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.
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
//