ID   CITE_MONRU              Reviewed;         292 AA.
AC   A0A162J3X8;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Short chain dehydrogenase citE {ECO:0000303|Ref.1};
DE            EC=1.1.1.- {ECO:0000305|Ref.1};
DE   AltName: Full=Citrinin synthesis protein E {ECO:0000303|Ref.1};
GN   Name=citE {ECO:0000303|Ref.1}; Synonyms=mrl6 {ECO:0000303|Ref.1};
OS   Monascus ruber (Mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Monascus.
OX   NCBI_TaxID=89489;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION,
RP   CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=M7;
RX   DOI=10.1039/C5SC04027B;
RA   He Y., Cox R.J.;
RT   "The molecular steps of citrinin biosynthesis in fungi.";
RL   Chem. Sci. 7:2119-2127(2016).
RN   [2]
RP   FUNCTION.
RX   PubMed=29189834; DOI=10.1039/c7cc07079a;
RA   Storm P.A., Townsend C.A.;
RT   "In trans hydrolysis of carrier protein-bound acyl intermediates by CitA
RT   during citrinin biosynthesis.";
RL   Chem. Commun. (Camb.) 54:50-53(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 (Ref.1). The pathway begins with the synthesis of a keto-aldehyde
CC       intermediate by the citrinin PKS (pksCT also named citS) from
CC       successive condensations of 4 malonyl-CoA units, presumably with a
CC       simple acetyl-CoA starter unit (Ref.1). Release of the keto-aldehyde
CC       intermediate is consistent with the presence of the C-terminal
CC       reductive release domain (Ref.1). CitA collaborates with citS by
CC       catalyzing the hydrolysis of ACP-bound acyl intermediates to free the
CC       ACP from stalled intermediates (PubMed:29189834). CitB then catalyzes
CC       the oxidation of the C-12 methyl of the ketone intermediate to an
CC       alcohol intermediate which is further oxidized by the oxidoreductase
CC       citC to produce a bisaldehyde intermediate (Ref.1). The fourth
CC       catalytic step is catalyzed by the citD aldehyde dehydrogenase (Ref.1).
CC       The final transformation is the reduction of C-3 by citE to provide the
CC       chemically stable citrinin nucleus (Ref.1). CitE appears highly
CC       selective for its substrate as its presence in any context other than a
CC       full complement of citS and citA-D does not result in observable new
CC       compounds (Ref.1). {ECO:0000269|PubMed:29189834, ECO:0000269|Ref.1}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|Ref.1}.
CC   -!- DISRUPTION PHENOTYPE: Leads to complete absence of citrinin production
CC       (Ref.1). {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; KT781075; ALI92649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162J3X8; -.
DR   SMR; A0A162J3X8; -.
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   NAD; Oxidoreductase.
FT   CHAIN           1..292
FT                   /note="Short chain dehydrogenase citE"
FT                   /id="PRO_0000440323"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         36..44
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         63..64
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         94..96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         188..192
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
FT   BINDING         221..223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q92506"
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