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Database: UniProt
Entry: E3RUF5_PYRTT
LinkDB: E3RUF5_PYRTT
Original site: E3RUF5_PYRTT 
ID   E3RUF5_PYRTT            Unreviewed;       400 AA.
AC   E3RUF5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN   ORFNames=PTT_12716 {ECO:0000313|EMBL:EFQ90634.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ90634.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ90634.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; GL535127; EFQ90634.1; -; Genomic_DNA.
DR   RefSeq; XP_003301260.1; XM_003301212.1.
DR   AlphaFoldDB; E3RUF5; -.
DR   STRING; 861557.E3RUF5; -.
DR   EnsemblFungi; EFQ90634; EFQ90634; PTT_12716.
DR   KEGG; pte:PTT_12716; -.
DR   eggNOG; KOG0257; Eukaryota.
DR   HOGENOM; CLU_017584_4_4_1; -.
DR   OrthoDB; 5474881at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43510; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 1.
DR   PANTHER; PTHR43510:SF1; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT   DOMAIN          48..383
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   400 AA;  44023 MW;  DFC2B2D40FA05AF4 CRC64;
     MVKVDDFAVE SWMDAHETKC KYNIAETCCA SVSIDQLRDL SDKKETPVFD TSRILNYGDI
     RGSQELRSNL ARLYSAKVTT PLSPENILTT PGAIQANYLA TYALVGPGDH VICHYPTYQS
     LYSVPEQLGA SVSLWKASPE NAWIPSMTDL EALIQPTTKL IIINNPNNPT GAVLGKSFLQ
     SLIDLASTHN ITILSDEVYR PLFHSLSPFD KDFPPSLLSM GYENVVVTGS LSKAYSLAGL
     RIGWIASRTS SLIEKMASAR HYTTISVSAL SEHYAAFALS PTTVHGLLAR NIQLAKTNLA
     LLERFMVKNE DEATWVRPVA GTTAFIKFHR DGKAVDDVDF CKKLLESTGV LFVPGSMCFG
     GEWKGYVRVG FVNQTEVVKE GLDAVTRFVR KQLDEVALAE
//
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