位置:首页 > 蛋白库 > PATD_PENEN
PATD_PENEN
ID   PATD_PENEN              Reviewed;         340 AA.
AC   A0A075TMP0;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Alcohol dehydrogenase patD {ECO:0000303|PubMed:25120234};
DE            EC=1.1.1.- {ECO:0000269|PubMed:30680886};
DE   AltName: Full=Patulin biosynthesis cluster protein D {ECO:0000303|PubMed:25120234};
GN   Name=patD {ECO:0000303|PubMed:25120234}; ORFNames=PEX2_082780;
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, INDUCTION, AND
RP   PATHWAY.
RC   STRAIN=NRRL 35695;
RX   PubMed=25120234; DOI=10.1016/j.ijfoodmicro.2014.07.028;
RA   Tannous J., El Khoury R., Snini S.P., Lippi Y., El Khoury A., Atoui A.,
RA   Lteif R., Oswald I.P., Puel O.;
RT   "Sequencing, physical organization and kinetic expression of the patulin
RT   biosynthetic gene cluster from Penicillium expansum.";
RL   Int. J. Food Microbiol. 189C:51-60(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8;
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=15082620; DOI=10.1093/ije/dyh028;
RG   Patulin Clinical Trials Committee, Medical Research Council;
RT   "Clinical trial of patulin in the common cold. 1944.";
RL   Int. J. Epidemiol. 33:243-246(2004).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=22222931; DOI=10.1016/j.fct.2011.12.022;
RA   de Melo F.T., de Oliveira I.M., Greggio S., Dacosta J.C., Guecheva T.N.,
RA   Saffi J., Henriques J.A., Rosa R.M.;
RT   "DNA damage in organs of mice treated acutely with patulin, a known
RT   mycotoxin.";
RL   Food Chem. Toxicol. 50:3548-3555(2012).
RN   [5]
RP   BIOTECHNOLOGY.
RX   PubMed=26619846; DOI=10.1007/s13277-015-4474-z;
RA   Boussabbeh M., Ben Salem I., Rjiba-Touati K., Bouyahya C., Neffati F.,
RA   Najjar M.F., Bacha H., Abid-Essefi S.;
RT   "The potential effect of patulin on mice bearing melanoma cells: an anti-
RT   tumour or carcinogenic effect?";
RL   Tumor Biol. 37:6285-6295(2016).
RN   [6]
RP   INDUCTION.
RX   PubMed=27528575; DOI=10.1111/mpp.12469;
RA   Kumar D., Barad S., Chen Y., Luo X., Tannous J., Dubey A., Glam Matana N.,
RA   Tian S., Li B., Keller N., Prusky D.;
RT   "LaeA regulation of secondary metabolism modulates virulence in Penicillium
RT   expansum and is mediated by sucrose.";
RL   Mol. Plant Pathol. 18:1150-1163(2017).
RN   [7]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=30100914; DOI=10.3389/fpls.2018.01094;
RA   Kumar D., Tannous J., Sionov E., Keller N., Prusky D.;
RT   "Apple intrinsic factors modulating the global regulator, LaeA, the patulin
RT   gene cluster and patulin accumulation during fruit colonization by
RT   Penicillium expansum.";
RL   Front. Plant Sci. 9:1094-1094(2018).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=25625822; DOI=10.1094/mpmi-12-14-0398-fi;
RA   Li B., Zong Y., Du Z., Chen Y., Zhang Z., Qin G., Zhao W., Tian S.;
RT   "Genomic characterization reveals insights into patulin biosynthesis and
RT   pathogenicity in Penicillium species.";
RL   Mol. Plant Microbe Interact. 28:635-647(2015).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
RP   INDUCTION, AND PATHWAY.
RX   PubMed=30680886; DOI=10.1111/1462-2920.14542;
RA   Li B., Chen Y., Zong Y., Shang Y., Zhang Z., Xu X., Wang X., Long M.,
RA   Tian S.;
RT   "Dissection of patulin biosynthesis, spatial control and regulation
RT   mechanism in Penicillium expansum.";
RL   Environ. Microbiol. 21:1124-1139(2019).
CC   -!- FUNCTION: Alcohol dehydrogenase; part of the gene cluster that mediates
CC       the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin
CC       produced by several fungal species that shows antimicrobial properties
CC       against several bacteria (PubMed:30100914, PubMed:25625822,
CC       PubMed:30680886). PatD catalyzes the conversion of neopatulin into E-
CC       ascladiol (PubMed:30680886). The pathway begins with the synthesis of
CC       6-methylsalicylic acid by the polyketide synthase (PKS) patK via
CC       condensation of acetate and malonate units. The 6-methylsalicylic acid
CC       decarboxylase patG then catalyzes the decarboxylation of 6-
CC       methylsalicylic acid to yield m-cresol (also known as 3-methylphenol).
CC       These first reactions occur in the cytosol. The intermediate m-cresol
CC       is then transported into the endoplasmic reticulum where the cytochrome
CC       P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which
CC       is further converted to gentisyl alcohol by the cytochrome P450
CC       monooxygenase patI. The oxidoreductases patJ and patO further convert
CC       gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the
CC       transformation of isoepoxydon into phyllostine. The cluster protein
CC       patF is responsible for the conversion from phyllostine to neopatulin
CC       whereas the alcohol dehydrogenase patD converts neopatulin to E-
CC       ascladiol. The steps between isoepoxydon and E-ascladiol occur in the
CC       cytosol, and E-ascladiol is probably secreted to the extracellular
CC       space by one of the cluster-specific transporters patC or patM.
CC       Finally, the secreted patulin synthase patE catalyzes the conversion of
CC       E-ascladiol to patulin (PubMed:30680886) (Probable).
CC       {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914,
CC       ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + neopatulin = (E)-ascladiol + NADP(+);
CC         Xref=Rhea:RHEA:62224, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:145111, ChEBI:CHEBI:145112;
CC         Evidence={ECO:0000269|PubMed:30680886};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62225;
CC         Evidence={ECO:0000269|PubMed:30680886};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q96533};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q96533};
CC   -!- PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis.
CC       {ECO:0000269|PubMed:30680886}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
CC   -!- INDUCTION: Expression is correlated with the production of patulin
CC       (PubMed:25120234). Expression is positively regulated by the secondary
CC       metabolism regulator laeA (PubMed:27528575, PubMed:30100914).
CC       Expression is strongly decreased with increased sucrose concentrations.
CC       This decrease is lost in the presence of malic acid (PubMed:30100914).
CC       Expression is increased with pH changes from 2.5 to 3.5 in the presence
CC       of a limiting concentration of sucrose, 50 mM (PubMed:30100914).
CC       Natural phenols present in apple fruits such as chlorogenic acid or the
CC       flavonoid epicatechin modulate patulin biosynthesis. They increase
CC       expression in the absence of sucrose, have little impact in the
CC       presence of 15 mM sucrose, and decrease expression in 175 mM sucrose
CC       (PubMed:30100914). Expression is positively regulated by the patulin
CC       cluster-specific transcription factor patL (PubMed:25625822). Finally,
CC       expression is also positively regulated by the velvet family proteins
CC       transcription regulators veA, velB, velC, but not vosA
CC       (PubMed:30680886). {ECO:0000269|PubMed:25120234,
CC       ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:27528575,
CC       ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886}.
CC   -!- DISRUPTION PHENOTYPE: Strongly reduces the production of patulin.
CC       {ECO:0000269|PubMed:30680886}.
CC   -!- BIOTECHNOLOGY: Patulin was originally used as an antibiotic and
CC       specifically trialed to be used against the common cold, but it is no
CC       longer used for that purpose since it has been shown to induce
CC       immunological, neurological and gastrointestinal effects
CC       (PubMed:15082620). Genotoxic effects of patulin with dose-dependent
CC       increase in DNA strand breaks in brain, liver and kidneys have been
CC       detected in mice (PubMed:22222931). However, more recently, it has been
CC       proposed that patulin might also have anti-tumor properties
CC       (PubMed:26619846). {ECO:0000269|PubMed:15082620,
CC       ECO:0000269|PubMed:22222931, ECO:0000269|PubMed:26619846}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       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; KF899892; AIG62135.1; -; Genomic_DNA.
DR   EMBL; JQFZ01000262; KGO52631.1; -; Genomic_DNA.
DR   RefSeq; XP_016595361.1; XM_016745548.1.
DR   AlphaFoldDB; A0A075TMP0; -.
DR   SMR; A0A075TMP0; -.
DR   EnsemblFungi; KGO43535; KGO43535; PEXP_094360.
DR   EnsemblFungi; KGO52631; KGO52631; PEX2_082780.
DR   EnsemblFungi; KGO61364; KGO61364; PEX1_005110.
DR   GeneID; 27680968; -.
DR   HOGENOM; CLU_026673_20_1_1; -.
DR   OrthoDB; 1186407at2759; -.
DR   PhylomeDB; A0A075TMP0; -.
DR   BioCyc; MetaCyc:MON-21162; -.
DR   UniPathway; UPA00918; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IDA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:GO_Central.
DR   GO; GO:0140723; P:patulin biosynthetic process; IDA:GO_Central.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; NAD; NADP; Oxidoreductase; Reference proteome;
KW   Zinc.
FT   CHAIN           1..340
FT                   /note="Alcohol dehydrogenase patD"
FT                   /id="PRO_0000445920"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         47
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00327"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         178..183
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         198..203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         206
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         265..267
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         289..291
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
FT   BINDING         297..299
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q96533"
SQ   SEQUENCE   340 AA;  36280 MW;  9196D9417176D438 CRC64;
     MASTTPSTYK QAVFKEQGAG LTLEEVALTL PKRDEILVKV EACGVCHSDH FAQTNLMGGG
     FPLVPGHEII GRVAAVGEGE TVWKEGDRIG GAWHGGHDGT CGACKKGFFQ MCDNEQVNGI
     SRNGGYAEYC IIRREAAVHI PDHVNAAKYA PMLCAGVTVF NAMRHMKIPP GELVAIQGLG
     GLGHLALQYA NKFGYRVVAL SRDSTKEEFA RKLGAHEYID TSREDPVAAL QKLGGASLIV
     STAPVPEIIN PLIQGLGVMG KLLILSIVGG IEVHTGLLVG KGKSIWSWPS GHATDSEDAI
     AFADLHGIDC LIEEFPLDKC NEAFAAMMEG SVRFRAVITM
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024