ALT4_ALTAL
ID ALT4_ALTAL Reviewed; 808 AA.
AC A0A3G9HHK2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Aminotransferase ALT4 {ECO:0000303|PubMed:19449880};
DE EC=2.3.1.- {ECO:0000305|PubMed:19449880};
DE AltName: Full=AAL-toxin biosynthesis cluster protein 4 {ECO:0000303|PubMed:19449880};
GN Name=ALT4 {ECO:0000303|PubMed:19449880};
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=As-27;
RA Akagi Y., Akamatsu H., Takao K., Tsuge T., Kodama M.;
RT "AAL-toxin biosynthetic genes cluster in the tomato pathotype of Alternaria
RT alternata.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=18435561; DOI=10.1021/np8000514;
RA Zhu X., Vogeler C., Du L.;
RT "Functional complementation of fumonisin biosynthesis in FUM1-disrupted
RT fusarium verticillioides by the AAL-toxin polyketide synthase gene ALT1
RT from Alternaria alternata f. sp. Lycopersici.";
RL J. Nat. Prod. 71:957-960(2008).
RN [3]
RP FUNCTION.
RX PubMed=19749175; DOI=10.1128/ec.00135-09;
RA Akagi Y., Akamatsu H., Otani H., Kodama M.;
RT "Horizontal chromosome transfer, a mechanism for the evolution and
RT differentiation of a plant-pathogenic fungus.";
RL Eukaryot. Cell 8:1732-1738(2009).
RN [4]
RP FUNCTION.
RX PubMed=19449880; DOI=10.1021/np900193j;
RA Li Y., Shen Y., Zhu X., Du L.;
RT "Introduction of the AAL-toxin polyketide synthase gene ALT1 into FUM1-
RT disrupted Fusarium verticillioides produces metabolites with the fumonisin
RT methylation pattern.";
RL J. Nat. Prod. 72:1328-1330(2009).
RN [5]
RP FUNCTION.
RX DOI=10.4172/2157-7471.S2-001;
RA Kheder A.A., Akagi Y., Tsuge T., Kodama M.;
RT "Functional analysis of the ceramide synthase gene ALT7, a homolog of the
RT disease resistance gene Asc1, in the plant pathogen Alternaria alternata.";
RL J. Plant Pathol. Microbiol. 2:0-0(2012).
CC -!- FUNCTION: Aminotransferase; part of the gene cluster that mediates the
CC biosynthesis of the host-selective toxins (HSTs) AAL-toxins,
CC sphinganine-analog mycotoxins responsible for Alternaria stem canker on
CC tomato by the tomato pathotype (PubMed:18435561, PubMed:19749175,
CC PubMed:19449880). The biosynthesis starts with the polyketide synthase
CC ALT1-catalyzed C-16 carbon chain assembly from one starter acetyl-CoA
CC unit with malonyl-CoA extender units (PubMed:18435561,
CC PubMed:19449880). ALT1 also selectively transfers methyl groups at the
CC first and the third cycle of chain elongation for AAL toxin
CC (PubMed:19449880). The C-16 polyketide chain is released from the
CC enzyme by a nucleophilic attack of a carbanion, which is derived from
CC R-carbon of glycin by decarboxylation, on the carbonyl carbon of
CC polyketide acyl chain (Probable). This step is probably catalyzed by a
CC pyridoxal 5'-phosphate-dependent aminoacyl transferase ALT4 (Probable).
CC The respective functions of the other enzymes encoded by the cluster
CC have still to be elucidated (Probable). The sphingosine N-
CC acyltransferase-like protein ALT7 seems not to act as a
CC resistance/self-tolerance factor against the toxin in the toxin
CC biosynthetic gene cluster, contrary to what is expected (Ref.5).
CC {ECO:0000269|PubMed:18435561, ECO:0000269|PubMed:19449880,
CC ECO:0000269|PubMed:19749175, ECO:0000269|Ref.5,
CC ECO:0000305|PubMed:19449880}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:19449880}.
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 The CDCs are not essential for saprophytic growth but controls host-
CC selective pathogenicity. {ECO:0000269|PubMed:19749175}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily. {ECO:0000305}.
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DR EMBL; AB969680; BBG74270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9HHK2; -.
DR SMR; A0A3G9HHK2; -.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 2.
PE 3: Inferred from homology;
KW Transferase.
FT CHAIN 1..808
FT /note="Aminotransferase ALT4"
FT /id="PRO_0000449853"
SQ SEQUENCE 808 AA; 89164 MW; 6095CFD0F7C5C24A CRC64;
MSVVRPKKVF QTPIDPGVSL RRKKDFYIWA ATIGFAQLWR DIKAFKWYRP LQMADLASHY
FYIPLGRLDP RILSSAPNDR MLIKTIPHEM SQDYDETGIL GCPGREVVNA GSNNYGGFTR
FEYGSASVIK LALRNLPFNP APEELNTLVE REMADYMEAD ACATAISGYG ANLLAFLTVA
ETAKLSDRQC IFLLDEESHS SMFVGAFLNK EAKFHRFKHN DIADLEYKLR TMKETSPNAL
VCVAIEGMYS LAGNVAPIPA ILALRKVFNF CLLVDEAHSF MAIGCKGRGS FEWWQARGYE
CPLSEVDIMT ATLSKSVGCT GGLVMANKIY ASNLQHQARL QREEGDECLS TIVLFRALTL
IRKPLFIERR MKTLEEKARY VAERLDEAGC LLLSPPGSPI ICFPVGTVQQ ASNFVAECLK
KGFAVACGVP PATPIWSCRV RVCIFATTSW GDILALVNTL IAVSCKLRID GVQSMKFDTD
SLPKVSIKED IVSDEGNAAD LALQEYVEQL AAKYPAEDCR AIAPLNVAQA REVFEYGVQS
FEMYGIGASS VRWFYGTFDV FIRLEQRLAG LYPSLISHSG KCRAMLGSDA NVMAVSLLSA
VAGPMYAKDV LNLVLVPQNA PCYVKKGATL DKVQPSTRVT LYEDLRDLEV EGTKLQKHRY
YHVTLYLETV DEDGSILDLS NRIKDILLTL KNAPSLTGLR LILDDSRGLG KIGPRHLGFL
DQMESQHGVS FFSTALGPQL AAITTVVVFG SWFHSLNHQG GYVISSEAFT EAHTVSSKSF
VFSTPPMIVQ AAMSEKTLEL LAGGSGLV