CITB_MONPU
ID CITB_MONPU Reviewed; 329 AA.
AC Q1ERI0;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase mpl2 {ECO:0000303|PubMed:27913218};
DE EC=1.14.-.- {ECO:0000269|PubMed:27913218};
DE AltName: Full=Citrinin synthesis protein A {ECO:0000303|PubMed:17586673};
GN Name=mpl2 {ECO:0000303|PubMed:27913218};
GN Synonyms=ctnA {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: 2-oxoglutarate-dependent dioxygenase; part of the gene
CC cluster that mediates the biosynthesis of the mycotoxin citrinin, a
CC hepato-nephrotoxic compound to humans due to inhibition of respiration
CC complex III (PubMed:17586673, PubMed:19012408, PubMed:28238725,
CC PubMed:19111642, PubMed:27913218). The pathway begins with the
CC synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT)
CC from successive condensations of 4 malonyl-CoA units, presumably with a
CC simple acetyl-CoA starter unit (PubMed:28238725). Release of the keto-
CC aldehyde 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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:27913218}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB243687; BAE95338.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1ERI0; -.
DR SMR; Q1ERI0; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..329
FT /note="2-oxoglutarate-dependent dioxygenase mpl2"
FT /id="PRO_0000440316"
FT DOMAIN 183..288
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 269
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 279
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 329 AA; 36894 MW; 08E466646DCF4C59 CRC64;
MPISTKSSFY LPAVDISPYL QDPNSDAARK VIDDVRAACT STGFFQLLGH GISPALQQSV
FAAAAKFFAL PSDVKSRCRN VGFRGYDPMA SQSYELGVLP DLKEGFIAGK DIPLDDPRVA
SQRFFMGQNA WPPSELLPEA NFRRPIEEYY QAMLKLCWVV LDLVAATLPY GPHVFDEFKE
NDPACPLRLL HYPPAPAPDV AKGRQLGSSA HTDFGAITLL LQDDHSGLEV QDCETGEWIG
VPPNKDAYVV NLGDMMSRIT RGHYKSSIHR VINQNLTDRY SVVFFFDGNL DYRLRPLDRV
GQNWDEEDTL TVEEHMLERT TTTYNLKVK
