ID   CITA_MONPU              Reviewed;         313 AA.
AC   Q1ERH9;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Esterase mpl1 {ECO:0000303|PubMed:27913218};
DE            EC=3.1.2.- {ECO:0000305|PubMed:27913218};
DE   AltName: Full=Citrinin synthesis protein B {ECO:0000303|PubMed:17586673};
GN   Name=mpl1 {ECO:0000303|PubMed:27913218};
GN   Synonyms=ctnB {ECO:0000303|PubMed:17586673};
OS   Monascus purpureus (Red mold) (Monascus anka).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Monascus.
OX   NCBI_TaxID=5098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=17586673; DOI=10.1128/aem.01979-06;
RA   Shimizu T., Kinoshita H., Nihira T.;
RT   "Identification and in vivo functional analysis by gene disruption of ctnA,
RT   an activator gene involved in citrinin biosynthesis in Monascus
RT   purpureus.";
RL   Appl. Environ. Microbiol. 73:5097-5103(2007).
RN   [2]
RP   FUNCTION.
RX   PubMed=19012408; DOI=10.1021/jf802371b;
RA   Chen Y.P., Tseng C.P., Chien I.L., Wang W.Y., Liaw L.L., Yuan G.F.;
RT   "Exploring the distribution of citrinin biosynthesis related genes among
RT   Monascus species.";
RL   J. Agric. Food Chem. 56:11767-11772(2008).
RN   [3]
RP   FUNCTION.
RX   PubMed=19111642; DOI=10.1263/jbb.106.466;
RA   Sakai K., Kinoshita H., Shimizu T., Nihira T.;
RT   "Construction of a citrinin gene cluster expression system in heterologous
RT   Aspergillus oryzae.";
RL   J. Biosci. Bioeng. 106:466-472(2008).
RN   [4]
RP   FUNCTION.
RX   PubMed=28238725; DOI=10.1016/j.chembiol.2017.01.008;
RA   Storm P.A., Herbst D.A., Maier T., Townsend C.A.;
RT   "Functional and structural analysis of programmed C-methylation in the
RT   biosynthesis of the fungal polyketide citrinin.";
RL   Cell Chem. Biol. 24:316-325(2017).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=27913218; DOI=10.1016/j.jbiotec.2016.11.031;
RA   Xue Y., Kong C., Shen W., Bai C., Ren Y., Zhou X., Zhang Y., Cai M.;
RT   "Methylotrophic yeast Pichia pastoris as a chassis organism for polyketide
RT   synthesis via the full citrinin biosynthetic pathway.";
RL   J. Biotechnol. 242:64-72(2017).
CC   -!- FUNCTION: Esterase; part of the gene cluster that mediates the
CC       biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound
CC       to humans due to inhibition of respiration complex III
CC       (PubMed:17586673, PubMed:19012408, PubMed:28238725, PubMed:19111642,
CC       PubMed:27913218). The pathway begins with the synthesis of a keto-
CC       aldehyde intermediate by the citrinin PKS (pksCT) from successive
CC       condensations of 4 malonyl-CoA units, presumably with a simple acetyl-
CC       CoA starter unit (PubMed:28238725). Release of the keto-aldehyde
CC       intermediate is consistent with the presence of the C-terminal
CC       reductive release domain (PubMed:28238725). Mp11 collaborates with
CC       pksCT by catalyzing the hydrolysis of ACP-bound acyl intermediates to
CC       free the ACP from stalled intermediates (By similarity). Mpl2 then
CC       catalyzes the oxidation of the C-12 methyl of the ketone intermediate
CC       to an alcohol intermediate which is further oxidized by the
CC       oxidoreductase mpl7 to produce a bisaldehyde intermediate
CC       (PubMed:27913218). The fourth catalytic step is catalyzed by the mpl4
CC       aldehyde dehydrogenase (PubMed:27913218). The final transformation is
CC       the reduction of C-3 by mpl6 to provide the chemically stable citrinin
CC       nucleus (PubMed:27913218). {ECO:0000250|UniProtKB:A0A161CKG1,
CC       ECO:0000269|PubMed:17586673, ECO:0000269|PubMed:19012408,
CC       ECO:0000269|PubMed:19111642, ECO:0000269|PubMed:27913218,
CC       ECO:0000269|PubMed:28238725}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:27913218}.
CC   -!- SIMILARITY: Belongs to the LovG family. {ECO:0000305}.
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DR   EMBL; AB243687; BAE95339.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1ERH9; -.
DR   SMR; Q1ERH9; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR005645; FSH_dom.
DR   Pfam; PF03959; FSH1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Hydrolase.
FT   CHAIN           1..313
FT                   /note="Esterase mpl1"
FT                   /id="PRO_0000440314"
FT   ACT_SITE        174
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
FT   ACT_SITE        259
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
FT   ACT_SITE        287
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
SQ   SEQUENCE   313 AA;  35226 MW;  561F532C91DFFD49 CRC64;
     MKGQTGLRSL ALLYISPLYI LERLPLKLSA PDTLVVRGSF IVPTEPLYPS ITMVQTNLEV
     VDDTLHLPRI LCLHGGGSNA AIFQAQCRRL IAQLRSEFRF VFAQAPFLSD AEPNVMSVYS
     QWGPFRRWLR WCPDHPEIRP EDAIRAIDDC LEDVKRQDDA KGATGAWVGL LGFSQGAKMC
     ASLLYRQQIR QELRGRSFAG SDYRFGVLLA GRAPLVSLDP DLDLNSSLPD VSQITDAKYH
     GPSQDVLRIP TVHVHGMRDP HVDLHRQLFE EFCAPESRRL VEWDGDHRVP LKYNDVSLVA
     YQIRELATQT GAP