ID   DTDH_MUCMU              Reviewed;         321 AA.
AC   Q01213; Q659V0;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=4-dihydromethyl-trisporate dehydrogenase;
DE            Short=4-dihydromethyl-TA dehydrogenase;
DE            EC=1.1.1.-;
GN   Name=tdh;
OS   Mucor mucedo (Common pinmould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=29922 {ECO:0000312|EMBL:CAA98021.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 40-52; 72-88;
RP   233-244 AND 255-272.
RC   STRAIN=ATCC 38694 / DSM 810 / CBS 109.16 / NBRC 5776 / NRRL 3634;
RC   TISSUE=Mycelium;
RX   PubMed=8828234; DOI=10.1099/00221287-142-9-2647;
RA   Czempinski K., Kruft V., Woestemeyer J., Burmester A.;
RT   "4-dihydromethyltrisporate dehydrogenase from Mucor mucedo, an enzyme of
RT   the sexual hormone pathway: purification, and cloning of the corresponding
RT   gene.";
RL   Microbiology 142:2647-2654(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 38693 / DSM 809 / CBS 144.24 / NRRL 3635 / VKM F-1356;
RA   Petzold A., Burmester A., Wolschendorf F., Schultze K., Woestemeyer J.,
RA   Schimek C.;
RT   "4-dihydromethyltrisporate dehydrogenase, an enzyme of the sex hormone
RT   pathway is posttranscriptionally regulated in Mucor mucedo.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   FUNCTION.
RA   Werkman B.A.;
RT   "Localization and partial characterization of a sex-specific enzyme in
RT   homothallic and heterothallic mucorales.";
RL   Arch. Microbiol. 109:209-213(1976).
CC   -!- FUNCTION: Catalyzes the NADP-dependent oxidation of (+) mating-type
CC       specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
CC       {ECO:0000269|Ref.3}.
CC   -!- PATHWAY: Pheromone biosynthesis; trisporate biosynthesis.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; Z73640; CAA98021.1; -; Genomic_DNA.
DR   EMBL; AJ831376; CAH40839.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01213; -.
DR   SMR; Q01213; -.
DR   UniPathway; UPA00170; -.
DR   GO; GO:0016696; F:oxidoreductase activity, acting on hydrogen as donor, NAD or NADP as acceptor; NAS:UniProtKB.
DR   GO; GO:0046842; P:trisporic acid biosynthetic process; NAS:UniProtKB.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase.
FT   CHAIN           1..321
FT                   /note="4-dihydromethyl-trisporate dehydrogenase"
FT                   /id="PRO_0000124677"
FT   ACT_SITE        51
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            80
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        40
FT                   /note="T -> M (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="C -> E (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255
FT                   /note="G -> N (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="P -> I (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   321 AA;  36484 MW;  AA64AED8DC95EC37 CRC64;
     MSTDYLTLNR TGDKMPIRGF GCWKIDTKDC EETVYQAIKT GYRLFDGACD YGNEVEVGRG
     INKAINEGLV KREDLFIVTK LWNTFHSKKH VRALFDRQLK DTGLEYFDLY LIHFPVPLQY
     VDPATVYPPG WYVGDAKSLQ FEQSPIHECW AELEKIVDAG LARNIGVANF NCQAILDLLT
     YARIKPAVLQ IELHPYLPQE RLVKWVKEQG IQITAYSSFG PTSYVDLTES GKTYTSLLEH
     ASVKSVADKH NVSTGQVLLR WALDREFAVI PKSVNAGRMK ANLEILDIKL DAEDNKTLDS
     LKTNQRFNDP MTYGFGLPLF D