ID   MTDH_MESCR              Reviewed;         361 AA.
AC   P93257;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable mannitol dehydrogenase;
DE            EC=1.1.1.255;
DE   AltName: Full=NAD-dependent mannitol dehydrogenase;
GN   Name=ELI3;
OS   Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum;
OC   Mesembryanthemum subgen. Cryophytum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Michalowski C.B., Bohnert H.J.;
RL   Submitted (NOV-1996) 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}.
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; U79770; AAB38503.1; -; mRNA.
DR   PIR; T12571; T12571.
DR   AlphaFoldDB; P93257; -.
DR   SMR; P93257; -.
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..361
FT                   /note="Probable mannitol dehydrogenase"
FT                   /id="PRO_0000160813"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
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         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  39068 MW;  3BA2BBF946144D10 CRC64;
     MANSAPENVH PQKAFGWAAR DTSGTLSPLK FSRRATGEQD VTFKVLYCGI CHSDLHYIKN
     EWGNAVYPAI PGHEIVGVVT EVGNKVQNFK VGDKVGVGCM VGSCRSCESC ENHLENYCPK
     MILTYGSTYY DGTLTYGGYS DIMVVEEHFA VRIPDNMALD ATAPLLCAGV TVYSPLKHFE
     LDKPGLHIGV VGLGGLGHMA VKFGKAFGAK VTVISTSPNK KDEAVNRLGA DSFVVSREPE
     QMQSAMGTLD GIIDTVSAAH PLLPLLGLLK SQGKMIMVGV PDKPLELPVF PLLQGRKILA
     GSCIGGMKET QEMIDFAAKH DIKSDIEVVP MDYVNTAMER LLKGDVRYRF VIDVANTLKA
     E