ID   TOXF_COCCA              Reviewed;         357 AA.
AC   Q9Y885;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Putative branched-chain-amino-acid aminotransferase TOXF;
DE            EC=2.6.1.42;
GN   Name=TOXF;
OS   Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=5017 {ECO:0000312|EMBL:AAD45321.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 90305 / SB111 / 2R15;
RX   PubMed=10627051; DOI=10.1099/00221287-145-12-3539;
RA   Cheng Y.-Q., Ahn J.-H., Walton J.D.;
RT   "A putative branched-chain-amino-acid transaminase gene required for HC-
RT   toxin biosynthesis and pathogenicity in Cochliobolus carbonum.";
RL   Microbiology 145:3539-3546(1999).
CC   -!- FUNCTION: Essential role in the production of HC-toxin and required for
CC       pathogenicity of the fungus on maize. May act on a precursor of 2-
CC       amino-9,10-epoxi-8-oxodecanoic acid. Acts on leucine, isoleucine and
CC       valine. {ECO:0000250|UniProtKB:P00510, ECO:0000269|PubMed:10627051,
CC       ECO:0000303|PubMed:10627051}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC         glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC         Evidence={ECO:0000250|UniProtKB:P00510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC         L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC         glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P00510};
CC   -!- PATHWAY: Mycotoxin biosynthesis; HC-toxin biosynthesis.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF157629; AAD45321.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Y885; -.
DR   SMR; Q9Y885; -.
DR   UniPathway; UPA00874; -.
DR   PHI-base; PHI:157; -.
DR   GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR   GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009403; P:toxin biosynthetic process; IDA:UniProtKB.
DR   CDD; cd01557; BCAT_beta_family; 1.
DR   Gene3D; 3.20.10.10; -; 1.
DR   Gene3D; 3.30.470.10; -; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR005786; B_amino_transII.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   InterPro; IPR033939; BCAT_family.
DR   PANTHER; PTHR42825; PTHR42825; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase;
KW   Branched-chain amino acid biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..357
FT                   /note="Putative branched-chain-amino-acid aminotransferase
FT                   TOXF"
FT                   /id="PRO_0000103303"
FT   MOD_RES         188
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  39618 MW;  96C082738746E018 CRC64;
     MAIPLPAFYK WDVYDSKLNN VHGHVECRYT AQTGYWSDPC FVQSPFLSVH GLAPGLNYGQ
     QVYEGIQARR TARNEILIFR PGASADRMAK SATAVSMPPV PYELFVRSVH MAVALNADYV
     PPHDFHGSMY IRPCQFGSSC QIGLQPPDEF IFCVFVQPHI ALHGHGSLRA LIAEDFDRAA
     TRGTGHVKIG GNYAPVIRWT QSAKKEENGG WDVLLHVDSK TQTRIDEFST SAFIGTKYAE
     EQNEPPQIIL PESAAAIQSI TSDSVAWLAK SFGWNIVKQP VTIDELASLS EVMAVGTAAG
     LVPVSCIRHN STNRTFEFPS AGPMYRQLKE TLDNIQRGRS SDSFGWCEKL RYAEFVQ