ID   G2XV85_BOTF4            Unreviewed;       511 AA.
AC   G2XV85;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Similar to class III aminotransferase {ECO:0000313|EMBL:CCD44405.1};
GN   ORFNames=BofuT4_P059850.1 {ECO:0000313|EMBL:CCD44405.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD44405.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; FQ790270; CCD44405.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2XV85; -.
DR   STRING; 999810.G2XV85; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   HOGENOM; CLU_016922_4_0_1; -.
DR   InParanoid; G2XV85; -.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CCD44405.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW   Transferase {ECO:0000313|EMBL:CCD44405.1}.
SQ   SEQUENCE   511 AA;  55478 MW;  05B7C6E0A39AD6DD CRC64;
     MSATNSSRHF QVLLRHVRKS ALALPSISHT LQAVPCYSSR QAPAAAAFST SALTRNLEQS
     PLGSTSEPSA LLHPILKTAP LNVVAAKGTT VTFFNGKNME DTTCGAAVAC IGYDNERVKT
     SMIKQMDKFS YSNSMFYGHQ VGEELAAELI RGTNGEMSKV YLMCSGAEAM EAAMKMARQY
     YMELNPKQPQ RTNFIAREGS FHGATLGSLS MSGHVGRRKL FEGMLFDNIH RVSAANEYRG
     KADGQTTEDY VQKLADELDL KFQEIGPDTV CAFVAEPVVG ATLGTVSAPA GYFKAMKKIC
     EKYGALLILD EVMCGMGRCG SLHEWEQEGV VPDIQTVAKG LAGGFAPMAA MFINHRVSDA
     LIAGTGVFAH AHTYQGHPVG CAAALEVQRI VREDNLVENV RENGEYLGKL LHEQLDDHPY
     VGNVRGRGFF WSLEFVACKK TKEPFPSSTG ISKKVHLTAF DDVGISFYPG MGTKDGVTGD
     HAWIAPAYTS TKYDIERIVS KVKESVILAL G
//