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ACT22_ALTAL
ID   ACT22_ALTAL             Reviewed;         262 AA.
AC   C9K1M9;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Abhydrolase domain-containing protein ACTT2-2 {ECO:0000303|PubMed:18986255};
DE            EC=3.1.1.- {ECO:0000305|PubMed:18986255};
DE   AltName: Full=ACT-toxin biosynthesis protein 2-2 {ECO:0000303|PubMed:18986255};
GN   Name=ACTT2-2;
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, AND DISRUPTION PHENOTYPE.
RC   STRAIN=BC3-5-1-OS2A;
RX   PubMed=18986255; DOI=10.1094/mpmi-21-12-1591;
RA   Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K., Fukumoto T.,
RA   Gomi K., Peever T.L., Akimitsu K.;
RT   "Functional analysis of a multicopy host-selective ACT-toxin biosynthesis
RT   gene in the tangerine pathotype of Alternaria alternata using RNA
RT   silencing.";
RL   Mol. Plant Microbe Interact. 21:1591-1599(2008).
RN   [2]
RP   FUNCTION.
RX   PubMed=18944496; DOI=10.1094/phyto.2000.90.7.762;
RA   Masunaka A., Tanaka A., Tsuge T., Peever T.L., Timmer L.W., Yamamoto M.,
RA   Yamamoto H., Akimitsu K.;
RT   "Distribution and characterization of AKT homologs in the tangerine
RT   pathotype of Alternaria alternata.";
RL   Phytopathology 90:762-768(2000).
RN   [3]
RP   FUNCTION.
RC   STRAIN=SH20;
RX   PubMed=19271978; DOI=10.1094/phyto-99-4-0369;
RA   Miyamoto M., Ishii Y., Honda A., Masunaka A., Tsuge T., Yamamoto M.,
RA   Ohtani K., Fukumoto T., Gomi K., Peever T.L., Akimitsu K.;
RT   "Function of genes encoding acyl-CoA synthetase and enoyl-CoA hydratase for
RT   host-selective act-toxin biosynthesis in the tangerine pathotype of
RT   Alternaria alternata.";
RL   Phytopathology 99:369-377(2009).
RN   [4]
RP   FUNCTION.
RC   STRAIN=SH20;
RX   PubMed=20055645; DOI=10.1094/phyto-100-2-0120;
RA   Ajiro N., Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K.,
RA   Fukumoto T., Gomi K., Peever T.L., Izumi Y., Tada Y., Akimitsu K.;
RT   "Role of the host-selective ACT-toxin synthesis gene ACTTS2 encoding an
RT   enoyl-reductase in pathogenicity of the tangerine pathotype of Alternaria
RT   alternata.";
RL   Phytopathology 100:120-126(2010).
RN   [5]
RP   FUNCTION.
RC   STRAIN=SH20;
RX   PubMed=20192828; DOI=10.1094/mpmi-23-4-0406;
RA   Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K., Fukumoto T.,
RA   Gomi K., Peever T.L., Tada Y., Ichimura K., Akimitsu K.;
RT   "ACTTS3 encoding a polyketide synthase is essential for the biosynthesis of
RT   ACT-toxin and pathogenicity in the tangerine pathotype of Alternaria
RT   alternata.";
RL   Mol. Plant Microbe Interact. 23:406-414(2010).
RN   [6]
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).
RN   [7]
RP   INDUCTION.
RX   PubMed=29616013; DOI=10.3389/fmicb.2018.00508;
RA   Wang M., Yang X., Ruan R., Fu H., Li H.;
RT   "Csn5 is required for the conidiogenesis and pathogenesis of the Alternaria
RT   alternata tangerine pathotype.";
RL   Front. Microbiol. 9:508-508(2018).
CC   -!- FUNCTION: Abhydrolase domain-containing protein; part of the gene
CC       clusters that mediate the biosynthesis of the host-selective toxins
CC       (HSTs) ACT-toxins responsible for brown spot of tangerine disease by
CC       the tangerine pathotype which affects tangerines and mandarins
CC       (PubMed:18944496, PubMed:18986255). ACT-toxins consist of three
CC       moieties, 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA), valine
CC       and a polyketide (PubMed:22846083). ACT-toxin I is toxic to both citrus
CC       and pear; toxin II the 5''-deoxy derivative of ACT-toxin I, is highly
CC       toxic to pear and slightly toxic to citrus (PubMed:22846083). On
CC       cellular level, ACT-toxins affect plasma membrane of susceptible cells
CC       and cause a sudden increase in loss of K(+) after a few minutes of
CC       toxin treatment (PubMed:22846083). The acyl-CoA ligase ACTT1, the
CC       hydrolase ACTT2, the enoyl-CoA hydratases ACTT3 and ACTT6, and the
CC       acyl-CoA synthetase ACTT5 are all involved in the biosynthesis of the
CC       AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-
CC       decatrienoic acid (EDA) structural moiety (PubMed:18944496,
CC       PubMed:18986255, PubMed:19271978). The exact role of each enzyme, and
CC       of additional enzymes identified within the AF-toxin clusters have
CC       still to be determined (PubMed:18944496, PubMed:18986255,
CC       PubMed:19271978). On the other hand, ACTTS1 to ACTTS4 are specific to
CC       the tangerine pathotype (PubMed:22846083). The function of ACTTS3 is to
CC       elongate the polyketide chain portion of ACT-toxin that is unique to
CC       this toxin (PubMed:20192828). The enoyl-reductase ACTTS2 might
CC       complement the missing enoyl-reductase (ER) domain in ACTTS3 in the
CC       synthesis of the polyketide portion of ACT-toxin (PubMed:20055645). The
CC       roles of the nonribosomal peptide synthetases-related proteins ACTTS1
CC       and ACTTS4 have also still not been elucidated (PubMed:22846083).
CC       {ECO:0000269|PubMed:18944496, ECO:0000269|PubMed:18986255,
CC       ECO:0000269|PubMed:19271978, ECO:0000269|PubMed:20055645,
CC       ECO:0000269|PubMed:20192828, ECO:0000303|PubMed:22846083}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:18986255}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O93801}.
CC       Note=The peroxisomal location requires the C-terminal tripeptide
CC       peroxisomal targeting signal. {ECO:0000250|UniProtKB:O93801}.
CC   -!- INDUCTION: Expression is positively regulated by CSN5 during infection.
CC       {ECO:0000269|PubMed:29616013}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of ACT-toxin and impairs
CC       the formation of lesions on leaves sprayed with conidia
CC       (PubMed:18986255). Does not affect growth rate of cultures,
CC       sporulation, and spore germination (PubMed:18986255).
CC       {ECO:0000269|PubMed:18986255}.
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:18986255). The CDCs are not essential for saprophytic growth
CC       but controls host-selective pathogenicity (PubMed:18986255). Although
CC       conventional disruption of ACTT2 could not be accomplished due to the
CC       high number of the copies identified in the genome, the high sequence
CC       identity among these copies of ACTT2 is likely an advantage for RNA
CC       silencing, because it allows knockdown of all copies of this gene
CC       simultaneously (PubMed:18986255). {ECO:0000269|PubMed:18986255}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AKT2 hydrolase
CC       family. {ECO:0000305}.
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DR   EMBL; AB432916; BAI44323.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9K1M9; -.
DR   SMR; C9K1M9; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Peroxisome; Virulence.
FT   CHAIN           1..262
FT                   /note="Abhydrolase domain-containing protein ACTT2-2"
FT                   /id="PRO_0000444828"
FT   MOTIF           260..262
FT                   /note="Peroxisomal targeting signal type 1"
FT                   /evidence="ECO:0000250|UniProtKB:O93801"
SQ   SEQUENCE   262 AA;  29589 MW;  71013A68943826A7 CRC64;
     MQQPIVGVGH SMGGCQIATL SVTSRRIFST MILLDPAIGP PEMGLATLGL GQLTLRRRTQ
     WLTREDAEKA LRTSFSTWDP QVLDLLIKHS IHSDKQSVEM EDGPVSLVTG RYQELVNYIK
     PSFIRSGKVV GQELVHQTGP VDMYHMLGLV TCSTLYLCGG ESTLSTPRAR ELWLSRTAEL
     SYSKDPGEMR KVDERIVPDT GHFLPMEEPK ECADIIADWI DKDECMIWNC HIGKQGKIWR
     DLSNTNRKMN AEVWIEYLQS KL
 
 
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