ID   A0A0D2C1B6_9EURO        Unreviewed;       485 AA.
AC   A0A0D2C1B6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924};
DE            EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924};
DE   AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000256|ARBA:ARBA00030587};
GN   ORFNames=PV08_04673 {ECO:0000313|EMBL:KIW17479.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW17479.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW17479.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW17479.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-ornithine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004998}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; KN847494; KIW17479.1; -; Genomic_DNA.
DR   RefSeq; XP_016237695.1; XM_016379018.1.
DR   AlphaFoldDB; A0A0D2C1B6; -.
DR   STRING; 91928.A0A0D2C1B6; -.
DR   GeneID; 27331756; -.
DR   VEuPathDB; FungiDB:PV08_04673; -.
DR   HOGENOM; CLU_016922_10_3_1; -.
DR   OrthoDB; 884390at2759; -.
DR   UniPathway; UPA00098; UER00358.
DR   Proteomes; UP000053328; Unassembled WGS sequence.
DR   GO; GO:0004587; F:ornithine aminotransferase 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; 3.90.1150.10; 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; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:KIW17479.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW   Transferase {ECO:0000313|EMBL:KIW17479.1}.
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  52732 MW;  2820952FBC0B1A62 CRC64;
     MAPTAVNGDG VNGVTQVNGH STGTQLKATA PAFHPAGTPD RTKYHASSSD EAIHAEHEYA
     AHNYHPLPVV FARALGTTVW DPEGRQYLDF LSAYSAVNQG HCHPELVKAL VEQASTLTLS
     SRAFYNDVFP RFAEFVTKYF NFDMVLPMNT GAEAVETAIK IARKWGYKCK GIPQNEALVL
     SVAENFHGRT FSAISMSTDP ESRDNYGPYL PGVGSVNPAT GKVIPYNDIS AVREAFESSG
     DKIAGFLVEP IQGEAGIVVP SDNYLSEVRA LCDKYNVLLI CDEIQTGIAR TGKLLCHEWA
     GIKPDMVLLG KAISGGMYPV SCVLGRKDVM LTIEPGTHGS TYGGNPLGCA VAIRALEIIR
     EEKMIERAEK LGQLFRDGLR DLQSPLITTI RGKGLLNAIV IDEEKTNGHS AWDLCMLMKE
     KGLLAKPTHQ NIIRLAPPLV ITEDEIKHAL AIIGEAVVEL PHLKGELEKN IIPPEEKNVK
     ITVDN
//