ID   MTDH1_STYHU             Reviewed;         354 AA.
AC   Q43137;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Probable mannitol dehydrogenase 1;
DE            EC=1.1.1.255;
DE   AltName: Full=NAD-dependent mannitol dehydrogenase 1;
GN   Name=CAD1;
OS   Stylosanthes humilis (Townsville stylo) (Astyposanthes humilis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Stylosanthes.
OX   NCBI_TaxID=35628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Paterson; TISSUE=Stem;
RA   Nourse J.P., Manners J.M., Curtis M.D., Abrahams S.L., Watson J.M.;
RL   Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Oxidizes mannitol to mannose. Provides the initial step by
CC       which translocated mannitol is committed to central metabolism and, by
CC       regulating mannitol pool size, is important in regulating salt
CC       tolerance at the cellular level (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol + NAD(+) = D-mannose + H(+) + NADH;
CC         Xref=Rhea:RHEA:15029, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16899, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.255;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Was originally (Ref.1) thought to be a cinnamyl-alcohol
CC       dehydrogenase. {ECO:0000305}.
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DR   EMBL; L36823; AAA74882.1; -; mRNA.
DR   AlphaFoldDB; Q43137; -.
DR   SMR; Q43137; -.
DR   GO; GO:0046029; F:mannitol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..354
FT                   /note="Probable mannitol dehydrogenase 1"
FT                   /id="PRO_0000160815"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  38130 MW;  662B93FD38460A34 CRC64;
     MASSKAFGWA AKDASGHLSP FHFTRRQNEA DDVTLKILYC GVCHSDLHTV KNDWGFTTYP
     VVPGHEIAGI VTKVGSNVTK FKEGDRVGVG VIVDSCQECE CCQQDLESYC PKPVFTYNSP
     YKGTRTQGGY SDFVVVHQRF VLQFPDNLPL DAGAPLLCAG ITVYSPMKYY GMTEPGKHLG
     VAGLGGLGHV AIKFGKAFGL KVTVISSSPN KESEAIDVLG ADSFLLSSDP EKMKAATGTM
     DYIIDTISAV HSLVSLLGLL KLNGKLVTVG LPSKPLQLPI FPLVAGRKLI GGSNFGGLKE
     TQEMLDFCGK HNIAANIELI KMDEINTAIE RLSKADVKYR FVIDVANSLS SSNM