ID   CITA_MONRU              Reviewed;         261 AA.
AC   A0A161CKG1;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Esterase citA {ECO:0000303|Ref.1};
DE            EC=3.1.2.- {ECO:0000269|PubMed:29189834};
DE   AltName: Full=Citrinin synthesis protein A {ECO:0000303|Ref.1};
GN   Name=citA {ECO:0000303|Ref.1}; Synonyms=mrl1 {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], FUNCTION, DISRUPTION PHENOTYPE,
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   INDUCTION.
RC   STRAIN=M7;
RX   PubMed=27998068; DOI=10.1021/acs.jafc.6b04056;
RA   Wang L., Dai Y., Chen W., Shao Y., Chen F.;
RT   "Effects of light intensity and color on the biomass, extracellular red
RT   pigment, and citrinin production of Monascus ruber.";
RL   J. Agric. Food Chem. 64:9506-9514(2016).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF SER-122, AND
RP   PATHWAY.
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: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of the mycotoxin citrinin, a hepato-
CC       nephrotoxic compound to humans due to inhibition of respiration complex
CC       III (Ref.1, PubMed:29189834). The pathway begins with the synthesis of
CC       a keto-aldehyde intermediate by the citrinin PKS (pksCT also named
CC       citS) from successive condensations of 4 malonyl-CoA units, presumably
CC       with a simple acetyl-CoA starter unit (Ref.1, PubMed:29189834). Release
CC       of the keto-aldehyde intermediate is consistent with the presence of
CC       the C-terminal reductive release domain (Ref.1). CitA collaborates with
CC       citS by catalyzing the hydrolysis of ACP-bound acyl intermediates to
CC       free the ACP from stalled intermediates (PubMed:29189834). CitB 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 citC to produce a bisaldehyde intermediate (Ref.1). The
CC       fourth catalytic step is catalyzed by the citD aldehyde dehydrogenase
CC       (Ref.1). The final transformation is the reduction of C-3 by citE to
CC       provide the chemically stable citrinin nucleus (Ref.1). CitE appears
CC       highly selective for its substrate as its presence in any context other
CC       than a full complement of citS and citA-D does not result in observable
CC       new compounds (Ref.1). {ECO:0000269|PubMed:29189834,
CC       ECO:0000269|Ref.1}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|Ref.1}.
CC   -!- INDUCTION: Expression is stimulated under green light conditions
CC       (PubMed:27998068). {ECO:0000269|PubMed:27998068}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a significant reduction (over 95%), but
CC       not abolition, of citrinin biosynthesis (Ref.1). {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the LovG family. {ECO:0000305}.
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DR   EMBL; KT781075; ALI92654.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161CKG1; -.
DR   SMR; A0A161CKG1; -.
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..261
FT                   /note="Esterase citA"
FT                   /id="PRO_0000440315"
FT   ACT_SITE        122
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:29189834"
FT   ACT_SITE        207
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
FT   ACT_SITE        235
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P38777"
FT   MUTAGEN         122
FT                   /note="S->A: Impairs the catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29189834"
SQ   SEQUENCE   261 AA;  29501 MW;  A66EE7B079413CAE CRC64;
     MVQTNLEVVD DTLHLPRILC LHGGGSNAAI FQAQCRRLIA QLRSEFRFVF AQAPFLSDAE
     PNVMSVYSQW GPFRRWLRWC PDHPEIRPED AIRAIDDCLE DVKRQDDAKG ATGAWVGLLG
     FSQGAKMCAS LLYRQQIRQE LRGRSFAGSD YRFGVLLAGR APLVSLDPDL DLNSSLPDVS
     QITDAKYHGP SQDVLRIPTV HVHGMRDPHV DLHRQLFEEF CAPESRRLVE WDGDHRVPLK
     YNDVSLVAYQ IRELATQTGA P