TES1_ALTAL
ID TES1_ALTAL Reviewed; 506 AA.
AC A0A144KPK9;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Cytochrome P450 monooxygenase TES1 {ECO:0000303|PubMed:27490569};
DE EC=1.-.-.- {ECO:0000305|PubMed:27490569};
DE AltName: Full=Tentoxin synthesis protein 1 {ECO:0000303|PubMed:27490569};
GN Name=TES1 {ECO:0000303|PubMed:27490569};
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], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=ZJ33;
RX PubMed=27490569; DOI=10.3390/toxins8080234;
RA Li Y.H., Han W.J., Gui X.W., Wei T., Tang S.Y., Jin J.M.;
RT "Putative nonribosomal peptide synthetase and cytochrome P450 genes
RT responsible for tentoxin biosynthesis in Alternaria alternata ZJ33.";
RL Toxins 8:0-0(2016).
RN [2]
RP FUNCTION.
RX PubMed=7881545; DOI=10.1099/13500872-140-12-3257;
RA Ramm K., Ramm M., Liebermann B., Reuter G.;
RT "Studies of the biosynthesis of tentoxin by Alternaria alternata.";
RL Microbiology 140:3257-3266(1994).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the phytotoxin tentoxin, an inhibitor the
CC F1-ATPase activity of chloroplasts, resulting in chlorosis in sensitive
CC plants (PubMed:27490569, PubMed:7881545). Tentoxin is a cyclic
CC tetrapeptide that consists of four amino acid residues: glycine (Gly),
CC alanine (Ala), leucine (Leu), and dehydrophenylalanine (DPhe)
CC (PubMed:27490569, PubMed:7881545). In addition, both the Ala and DPhe
CC residues are N-methylated (PubMed:27490569, PubMed:7881545). The
CC nonribosomal peptide synthetase TES assembles tentoxin from the four
CC substrate amino acids (PubMed:27490569). The adenylation domains of
CC each of the 4 modules are responsible for the activation of Gly, Ala,
CC Leu and DPhe, respectively (PubMed:27490569). In addition, the N-
CC methyltransferase domains in the second and fourth modules of TES could
CC be responsible for N-methylation of Ala and DPhe residues
CC (PubMed:27490569). Finally, the condensation domain located in the
CC termination module probably catalyzes the formation of the
CC intramolecular macrocyclization and then the release of tentoxin
CC (PubMed:27490569). The cytochrome P450 monooxygenase TES1 is predicted
CC to be involved in the formation of DPhe (PubMed:27490569).
CC {ECO:0000269|PubMed:27490569, ECO:0000269|PubMed:7881545}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Phytotoxin biosynthesis. {ECO:0000269|PubMed:27490569}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of tentoxin
CC (PubMed:27490569). {ECO:0000269|PubMed:27490569}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KT947105; AMT84998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A144KPK9; -.
DR SMR; A0A144KPK9; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..506
FT /note="Cytochrome P450 monooxygenase TES1"
FT /id="PRO_0000438988"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 440
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 506 AA; 58103 MW; C246593632BF8015 CRC64;
MEPEPLDPRA IGFMRRNLAM LRQTPMSVVL AGLILLASIY FPRFMFKSQM ARFPLILEHL
SSEQRRARFL VGAKALYKDG SQKFRGMAYR MQTLDEQQIV LPLSALTELR KAPEEVLSFY
DMFSKVVDTI KRDLTPKLTK ITSKICDEVD AALDTYLPSH GKWTEINVSK TALDIIAKVS
AHLFIGGDVA NDPGYLECTK NFTVHLGEAT RAIKVTRVWL RPFLAPRLPE VKRLLETRTK
LRSYVKRVIE EREAKIKNPD WVPPDDMMQW LLDRADRQKD TLEDCTAAQV LLILGTINAS
MQTLIAILHT LAVTPEYVEP LREEIRNTLN SDGSIPVSAM KEFGKMDSYF KEVGMHFPVI
IEPYFRRVRK GFTLSNGQYL PPGVAIVIAN PLVTDSKYDT FDGFRHYKLR EASAQKDKPN
HRWLIANETE FRWGYDNHVC PGRFYAHNLL KIIFARIVEN YDIKMPGNVE GIEARYPMVE
HGNVVMEPRD KPLLLRRVKS HQGHVD
