CITC_MONPU
ID CITC_MONPU Reviewed; 622 AA.
AC A0A142PTM2;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Dehydrogenase mpl7 {ECO:0000303|PubMed:27913218};
DE EC=1.1.-.- {ECO:0000305|PubMed:27913218};
DE AltName: Full=Citrinin synthesis protein mpl7 {ECO:0000303|PubMed:27913218};
GN Name=mpl7 {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: Dehydrogenase; 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:27913218, PubMed:19012408, PubMed:19111642, PubMed:28238725).
CC The pathway begins with the synthesis of a keto-aldehyde intermediate
CC by the citrinin PKS (pksCT) from successive condensations of 4 malonyl-
CC CoA units, presumably with a simple acetyl-CoA starter unit
CC (PubMed:28238725). Release of the keto-aldehyde intermediate is
CC consistent with the presence of the C-terminal reductive release domain
CC (PubMed:28238725). Mp11 collaborates with pksCT by catalyzing the
CC hydrolysis of ACP-bound acyl intermediates to free the ACP from stalled
CC intermediates (By similarity). Mpl2 then catalyzes the oxidation of the
CC C-12 methyl of the ketone intermediate to an alcohol intermediate which
CC is further oxidized by the oxidoreductase mpl7 to produce a bisaldehyde
CC intermediate (PubMed:27913218). The fourth catalytic step is catalyzed
CC by the mpl4 aldehyde dehydrogenase (PubMed:27913218). The final
CC transformation is the reduction of C-3 by mpl6 to provide the
CC chemically stable citrinin nucleus (PubMed:27913218).
CC {ECO:0000250|UniProtKB:A0A161CKG1, ECO:0000269|PubMed:19012408,
CC ECO:0000269|PubMed:19111642, ECO:0000269|PubMed:27913218,
CC ECO:0000269|PubMed:28238725}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E4QP00};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:27913218}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q12062}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KU923369; AMU19396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142PTM2; -.
DR SMR; A0A142PTM2; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..622
FT /note="Dehydrogenase mpl7"
FT /id="PRO_0000440318"
FT ACT_SITE 554
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 23..24
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 44..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 102..105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 582
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 593..594
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
SQ SEQUENCE 622 AA; 66811 MW; DA62628BF2519E33 CRC64;
MATVKVIDFI QTPFDFLIVG GGTAGLVLAA RLSEEPGIQV GVIEAGSLRL GDPKVDLPTG
PGQMLGDPGY DWNFESIPQA GANAKAYHIP RGRMLGGSSG INFMSYNRPS AEDIDDWANK
LGVKGWTWSE LLPYFKRSEN LEPIEPSASC PVSPKVHGTG GPIHTSIGPW QAPIEESLLA
AFDEAARLQR PAEPYSGAHL GFYRSLFTLD RTSTPVRSYA VSGYYAPVMG RPNLKVLENA
QVCRILLSDA SDGIPVAEGV ELHHAGARYA VSARREVILS AGSVQSPQLL ELSGIGDPSV
LEGAGIACRV ANTDVGSNLQ EHTMSAVSYE CADGIMSVDS LFKDPALLEE HQSLYAKNHS
GALSGSVSLM GFTPYSSLST ETQVDATMAR IFDAPSVSGR LSQQNASYQR RQQEAVAARM
QNRWSADIQF IGTPAYFNTA AGYASCAKIM SGPPVGYSAC YSIVVSNMYP LSRGSVHVRT
SNPMDAPAID PGFLSHPVDV DVLAAGIVFA DRVFRSTLLN GKVRRRVSPP AGLDLSNMDE
ARQFVRNHIV PYHHALGTCA MGQVVDEKLR VKGVRRLRVV DASVMPMQVS AAIMATVYAI
AERASDIIKK DCGFGRRLRA HI
