ID   MTDH_FRAAN              Reviewed;         359 AA.
AC   Q9ZRF1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Probable mannitol dehydrogenase;
DE            EC=1.1.1.255;
DE   AltName: Full=NAD-dependent mannitol dehydrogenase;
GN   Name=CAD;
OS   Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC   Fragaria.
OX   NCBI_TaxID=3747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Chandler;
RX   PubMed=12147722; DOI=10.1093/jxb/erf029;
RA   Blanco-Portales R., Medina-Escobar N., Lopez-Raez J.A.,
RA   Gonzalez-Reyes J.A., Villalba J.M., Moyano E., Caballero J.L.,
RA   Munoz-Blanco J.;
RT   "Cloning, expression and immunolocalization pattern of a cinnamyl alcohol
RT   dehydrogenase gene from strawberry (Fragaria x ananassa cv. Chandler).";
RL   J. Exp. Bot. 53:1723-1734(2002).
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 thought to be a cinnamyl-alcohol dehydrogenase.
CC       {ECO:0000305|PubMed:12147722}.
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; U63534; AAD10327.1; -; mRNA.
DR   AlphaFoldDB; Q9ZRF1; -.
DR   SMR; Q9ZRF1; -.
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..359
FT                   /note="Probable mannitol dehydrogenase"
FT                   /id="PRO_0000160811"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   359 AA;  39137 MW;  BAB1D6B3AF086DAB CRC64;
     MAIEQEHRKK ASGWAARDSS GVLSPFNFYR RETGEKDVTF KVLYCGICHS DLHMVKNEWG
     FSTYPLVPGH EIVGEVTEVG SKVQKFKVGD RVGVGCIVGS CRSCENCTDH LENYCPKQIL
     TYGAKYYDGS TTYGGYSDIM VADEHFIVRI PDNLPLDGAA PLLCAGITTY SPLRYFGLDK
     PGMHVGVVGL GGLGHVAVKF AKAMGVKVTV ISTSPKKEEE ALKHLGADSF LVSRDQDQMQ
     AAIGTMDGII DTVSAQHPLL PLIGLLNSHG KLVMVGAPEK PLELPVFPLL MGRKMVAGSG
     IGGMKETQEM IDFAARHNIT ADIEVIPIDY LNTAMERLVK ADVRYRFVID IGNTLKVRS