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Database: UniProt
Entry: A0A395SC02_9HYPO
LinkDB: A0A395SC02_9HYPO
Original site: A0A395SC02_9HYPO 
ID   A0A395SC02_9HYPO        Unreviewed;       441 AA.
AC   A0A395SC02;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Ornithine aminotransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FLONG3_7598 {ECO:0000313|EMBL:RGP69941.1};
OS   Fusarium longipes.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP69941.1, ECO:0000313|Proteomes:UP000266234};
RN   [1] {ECO:0000313|EMBL:RGP69941.1, ECO:0000313|Proteomes:UP000266234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP69941.1,
RC   ECO:0000313|Proteomes:UP000266234};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RGP69941.1}.
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DR   EMBL; PXOG01000176; RGP69941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395SC02; -.
DR   STRING; 694270.A0A395SC02; -.
DR   Proteomes; UP000266234; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266234}.
SQ   SEQUENCE   441 AA;  47979 MW;  B610D4B1F322F4E5 CRC64;
     MAHPFVASSH LLHRSFAHKP EKVVSASGVS LFLESGREVL DASAGPAVSC LGFGRPEIAQ
     AVTNQINQLA YLYSGARFTC DATEDLASTL LQEQPGGLSK AIFVNSGSEA ADTAIKLATQ
     YWYERGMPQK CHVIARKQSY HGNTIGALCI SGHDSRRTMY RPWLSENVSF VDPCFPYRLQ
     GDESDEVYVK RLAGQLEAEI IRVGPENVSA FVAETVSGTT LGCVPAVPGY FKAVRKICDD
     YDVLLILDEI MCGMGKTGTM HAWEQEGISG PDIQMIGKAL GGGFIPLSGV LLRSYIFDAI
     AEGSGGLAHG HTFQKMGAVL ERLLKDRIEP LETVGDIRGR GLFWAVEFIQ DRQRKTPFPA
     SMRLCHRIVD KSLDLGLNIL GNLGQTGSVH VDHVIVCPPY VVTEPELKRM VGILQEAIEA
     VTSELVGTRQ ANIYTGRVKV V
//
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