ID   MTDH_MEDSA              Reviewed;         359 AA.
AC   O82515;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable mannitol dehydrogenase;
DE            EC=1.1.1.255;
DE   AltName: Full=NAD-dependent mannitol dehydrogenase;
GN   Name=CAD1;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=cv. Siriver; TISSUE=Stem;
RX   PubMed=10579494; DOI=10.1023/a:1006381630494;
RA   Brill E.M., Abrahams S., Hayes C.M., Jenkins C.L., Watson J.M.;
RT   "Molecular characterization and expression of a wound-inducible cDNA
RT   encoding a novel cinnamyl-alcohol dehydrogenase enzyme in lucerne (Medicago
RT   sativa L.).";
RL   Plant Mol. Biol. 41:279-291(1999).
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}.
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DR   EMBL; AF083333; AAC35846.1; -; mRNA.
DR   AlphaFoldDB; O82515; -.
DR   SMR; O82515; -.
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   1: Evidence at protein level;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..359
FT                   /note="Probable mannitol dehydrogenase"
FT                   /id="PRO_0000160812"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
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;  39027 MW;  D84E383EE0F195A1 CRC64;
     MAKSPETELP LKAFGWAARD TSGTLSPFHF SRRENGDDDV SVKILYCGVC HSDLHTLKND
     WGFTTYPVVP GHEIVGVVTK VGINVKKFRV GDNVGVGVIV ESCQTCENCN QDLEQYCPKP
     VFTYNSPYKG TRTYGGYSDF VVVHQRYVVQ FPDNLPLDAG APLLCAGITV YSPMKYYGMT
     EPGKHLGVAG LGGLGHVAIK FGKAFGLKVT VISTSPNKET EAIDKLGADS FLVSKDPEKM
     KAAMGTMDYI IDTISAAHSL MPLLGLLKLN GKLVTVGLPS KPLELSVFPL VAGRKLIGGS
     NIGGMKETQE MLDFCGKHNI TADIELIKMH EINTAMERLH KADVKYRFVI DVANSFSSL