CITD_MONPU
ID CITD_MONPU Reviewed; 501 AA.
AC Q1ERI2;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Aldehyde dehydrogenase mpl4 {ECO:0000303|PubMed:27913218};
DE EC=1.2.1.3 {ECO:0000255|PROSITE-ProRule:PRU10007};
DE AltName: Full=Citrinin synthesis protein mpl4 {ECO:0000303|PubMed:27913218};
GN Name=mpl4 {ECO:0000303|PubMed:27913218};
GN Synonyms=orf1 {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].
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: Aldehyde 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:17586673, PubMed:19012408, PubMed:19111642,
CC PubMed:28238725, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10007};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:17586673}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255}.
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DR EMBL; AB243687; BAE95336.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1ERI2; -.
DR SMR; Q1ERI2; -.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase.
FT CHAIN 1..501
FT /note="Aldehyde dehydrogenase mpl4"
FT /id="PRO_0000440320"
FT ACT_SITE 253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 231..236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q28399"
SQ SEQUENCE 501 AA; 54135 MW; 294E2D92F88C25F0 CRC64;
MAEAAARILE ALPAVCEYRW SCKDASKRFT VVNPATGEPI TVVQAGNLDT VQGAIQASHR
AFESWRWKTR QERSLYLLQA ADELQKHSHE LAVLLCLENG KPVKDASFDV GFLVQVFRYF
GSIVDKLPSE FFDQGSIYSS VIYEPHGVCV GILPFNWPPV HAGGKLAPCL AAGNTMVLKP
GEQAPLTLMR IVEILQSVFP ADVVQAVPGL GPEIPQALIN HPLVKMVSLT GSTASGSQAA
QTAAVTLTPT VLELGGKNAF VVFEDADLEL VVRDAIDGAF FNKGESCTAA SRILVHKDLY
PTLVSRLTAA VKKLRTGDGL DETTHIGPVV SRERQQEVLS YIEQGKREGA TLAAQGDPPT
AGRLSGGFFV PPTLFTDVTA DMTIAQREIF GPVVTVGSFE TEEEAVKTVN SSQYGLFAGV
YSSDFTRAMR VTRKLDVGVV LVNNYFRALL GTPFGGVKDS GYGREHWIGT LREWSRVKNV
RFPSGLSPIP AWGGAVDVCK L
