ID   CITE_MONPU              Reviewed;         292 AA.
AC   A0A144Y7G4;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Short chain dehydrogenase mpl6 {ECO:0000303|PubMed:27913218};
DE            EC=1.1.1.- {ECO:0000305|PubMed:27913218};
DE   AltName: Full=Citrinin synthesis protein mpl6 {ECO:0000303|PubMed:27913218};
GN   Name=mpl6 {ECO:0000303|PubMed:27913218};
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP   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).
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).
CC   -!- FUNCTION: Short chain dehydrogenase; part of the gene cluster that
CC       mediates the biosynthesis of the mycotoxin citrinin, a hepato-
CC       nephrotoxic compound to humans due to inhibition of respiration complex
CC       III (PubMed:27913218, PubMed:19012408, PubMed:19111642,
CC       PubMed:28238725). 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:19012408, ECO:0000269|PubMed:19111642,
CC       ECO:0000269|PubMed:27913218, ECO:0000269|PubMed:28238725}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:27913218}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; KU923369; AMU19397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A144Y7G4; -.
DR   SMR; A0A144Y7G4; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Oxidoreductase.
FT   CHAIN           1..292
FT                   /note="Short chain dehydrogenase mpl6"
FT                   /id="PRO_0000440322"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5BEK1"
SQ   SEQUENCE   292 AA;  31351 MW;  E42D4CB094A808D1 CRC64;
     MAFPPSAGFT WISKTHNDTY PTITAAKCKQ HGRAVFVTGA SKGIGRVTAV AFAQAGAPSL
     ALGARSSLDA AETAVLDAAK SAGHPPPQVL KLTLDVADEQ SVADAAARVE RAFGRLDILV
     NNAGRVEKWV PLAETDPKSW WATWEVNLKG TYLMTRAMLP LLLKGGEKTI VNMNSIGAHL
     TRPGASAYQT GKLAMLRLTQ FTCVEYAAQG VLAFAIHPGA VDTELASNLP EDTKAKLVDS
     PELCADTIVW LTQEKQSWLA GRYLSANWDV AELMARKEEI LQGDKLKVKL VL