AMT52_ALTAL
ID AMT52_ALTAL Reviewed; 373 AA.
AC C9K7D8;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Transaminase AMT5-2 {ECO:0000250|UniProtKB:K0E3V3};
DE EC=2.6.1.- {ECO:0000250|UniProtKB:K0E3V3};
DE AltName: Full=AM-toxin biosynthesis protein 5-2 {ECO:0000303|Ref.1};
GN Name=AMT5-2 {ECO:0000303|Ref.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 8984;
RA Harimoto Y., Kodama M., Yamamoto M., Otani H., Tsuge T.;
RT "A Zn(II)2Cys6 transcription regulator encoded by the AMT gene cluster
RT negatively controls AM-toxin production in the apple pathotype of
RT Alternaria alternata.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RC STRAIN=M-71;
RX PubMed=10875335; DOI=10.1094/mpmi.2000.13.7.742;
RA Johnson R.D., Johnson L., Itoh Y., Kodama M., Otani H., Kohmoto K.;
RT "Cloning and characterization of a cyclic peptide synthetase gene from
RT Alternaria alternata apple pathotype whose product is involved in AM-toxin
RT synthesis and pathogenicity.";
RL Mol. Plant Microbe Interact. 13:742-753(2000).
RN [3]
RP FUNCTION.
RC STRAIN=NBRC 8984;
RX PubMed=15066029; DOI=10.1111/j.1365-2958.2004.04004.x;
RA Ito K., Tanaka T., Hatta R., Yamamoto M., Akimitsu K., Tsuge T.;
RT "Dissection of the host range of the fungal plant pathogen Alternaria
RT alternata by modification of secondary metabolism.";
RL Mol. Microbiol. 52:399-411(2004).
RN [4]
RP FUNCTION.
RC STRAIN=NBRC 8984;
RX PubMed=17990954; DOI=10.1094/mpmi-20-12-1463;
RA Harimoto Y., Hatta R., Kodama M., Yamamoto M., Otani H., Tsuge T.;
RT "Expression profiles of genes encoded by the supernumerary chromosome
RT controlling AM-toxin biosynthesis and pathogenicity in the apple pathotype
RT of Alternaria alternata.";
RL Mol. Plant Microbe Interact. 20:1463-1476(2007).
RN [5]
RP REVIEW ON HOST-SELECTIVE TOXINS.
RX PubMed=22846083; DOI=10.1111/j.1574-6976.2012.00350.x;
RA Tsuge T., Harimoto Y., Akimitsu K., Ohtani K., Kodama M., Akagi Y.,
RA Egusa M., Yamamoto M., Otani H.;
RT "Host-selective toxins produced by the plant pathogenic fungus Alternaria
RT alternata.";
RL FEMS Microbiol. Rev. 37:44-66(2013).
CC -!- FUNCTION: Transaminase; part of the gene clusters that mediate the
CC biosynthesis of AM-toxins, host-selective toxins (HSTs) causing
CC Alternaria blotch on apple, a worldwide distributed disease (By
CC similarity). AM-toxins are cyclic depsipeptides containing the 3
CC residues 2-hydroxy-isovaleric acid (2-HIV), dehydroalanine, L-alanine
CC which are common for all 3 AM-toxins I to III. The fourth precursor is
CC L-alpha-amino-methoxyphenyl-valeric acid (L-Amv) for AM-toxin I, L-
CC alpha-amino-phenyl-valeric acid (L-Apv) for AM-toxin II, and L-alpha-
CC amino-hydroxyphenyl-valeric acid (L-Ahv) for AM-toxin III (Probable).
CC AM-toxins have two target sites for affecting susceptible apple cells;
CC they cause invagination of the plasma membrane and electrolyte loss and
CC chloroplast disorganization (PubMed:22846083). The non-ribosomal
CC peptide synthetase AMT1 contains 4 catalytic modules and is responsible
CC for activation of each residue in AM-toxin (PubMed:10875335). The aldo-
CC keto reductase AMT2 catalyzes the conversion of 2-keto-isovaleric acid
CC (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV), one of the precursor
CC residues incorporated by AMT1 during AM-toxin biosynthesis, by
CC reduction of its ketone to an alcohol (PubMed:15066029). The cytochrome
CC P450 monooxygenase AMT3 and the thioesterase AMT4 are also important
CC for AM-toxin production, but their exact function within the AM-toxin
CC biosynthesis are not known yet (PubMed:17990954). Up to 21 proteins
CC (including AMT1 to AMT4) are predicted to be involved in AM-toxin
CC biosynthesis since their expression ishighly up-regulated in AM-toxin-
CC producing cultures (PubMed:17990954). {ECO:0000250|UniProtKB:C9K7B6,
CC ECO:0000269|PubMed:10875335, ECO:0000269|PubMed:15066029,
CC ECO:0000269|PubMed:17990954, ECO:0000303|PubMed:22846083,
CC ECO:0000305|PubMed:10875335}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P19938};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:K0E3V3}.
CC -!- MISCELLANEOUS: Gene clusters encoding host-selective toxins (HSTs) are
CC localized on conditionally dispensable chromosomes (CDCs), also called
CC supernumerary chromosomes, where they are present in multiple copies
CC (PubMed:17990954). The CDCs are not essential for saprophytic growth
CC but controls host-selective pathogenicity (PubMed:17990954).
CC {ECO:0000269|PubMed:17990954}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AB525199; BAI44762.1; -; Genomic_DNA.
DR AlphaFoldDB; C9K7D8; -.
DR SMR; C9K7D8; -.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IEA:InterPro.
DR GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
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 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 Aminotransferase; Pyridoxal phosphate; Transferase; Virulence.
FT CHAIN 1..373
FT /note="Transaminase AMT5-2"
FT /id="PRO_0000444823"
FT BINDING 92
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 232
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P19938"
SQ SEQUENCE 373 AA; 40454 MW; F8E86D23DAA6E36F CRC64;
MASYGFPLTA SSLVDWTSLT FSPIEVNGHI QCTYSPEVAE WGAPHFVKDP YLRVHGLAPA
LNYGQQIFEG MKAFRTPTGS IRLFRPKMNA VRFAHSASFV AIPPVPEALF LRAVHLAVGL
NSEFVPPYDS RGSALYIRPI AFASSATANL APADHFTFCV FVMPVAPLST GAGQGLRALV
VEDVDRAAPK GTGSAKVGGN YAPIVTTMQR AKADGYGLTL HLDSATHTMV DEFSASGFIG
VRVDAGKTTM VVPDSPTILR SITVDSMCRI AESFGWQVQR RAVSFTELAE LSEAFAVGTA
FILTPVRAIT RPCTHTCIEY TADYRSSASA YTRLLETLQG IQQGWLDDAW GWTEEVQDPS
SDEFITDTVQ ARR
