ID   MTDH_APIGR              Reviewed;         365 AA.
AC   Q38707; O82461;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Mannitol dehydrogenase;
DE            EC=1.1.1.255;
DE   AltName: Full=NAD-dependent mannitol dehydrogenase;
GN   Name=MTD;
OS   Apium graveolens (Celery).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Apium.
OX   NCBI_TaxID=4045;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7638158; DOI=10.1073/pnas.92.16.7148;
RA   Williamson J.D., Stoop J.M.H., Massel M.O., Conkling M.A., Pharr D.M.;
RT   "Sequence analysis of a mannitol dehydrogenase cDNA from plants reveals a
RT   function for the pathogenesis-related protein ELI3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7148-7152(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Williamson J.D., Guo W.-W., Pharr D.M.;
RT   "Cloning and characterization of a genomic clone encoding mannitol
RT   dehydrogenase from celery (Apium graveolens).";
RL   (er) Plant Gene Register PGR98-137(1998).
RN   [3]
RP   CHARACTERIZATION.
RA   Stoop J.M.H., Chilton W.S., Pharr D.M.;
RT   "Substrate specificity of the NAD-dependent mannitol dehydrogenase from
RT   celery.";
RL   Phytochemistry 43:1145-1150(1996).
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.
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; U24561; AAC15467.1; -; mRNA.
DR   EMBL; AF067082; AAC61854.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q38707; -.
DR   SMR; Q38707; -.
DR   KEGG; ag:AAC15467; -.
DR   BioCyc; MetaCyc:MON-9261; -.
DR   BRENDA; 1.1.1.255; 388.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..365
FT                   /note="Mannitol dehydrogenase"
FT                   /id="PRO_0000160807"
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         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        47
FT                   /note="C -> S (in Ref. 2; AAC61854)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="T -> I (in Ref. 2; AAC61854)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   365 AA;  39691 MW;  A46E394F5DCB077F CRC64;
     MAKSSEIEHP VKAFGWAARD TTGLLSPFKF SRRATGEKDV RLKVLFCGVC HSDHHMIHNN
     WGFTTYPIVP GHEIVGVVTE VGSKVEKVKV GDNVGIGCLV GSCRSCESCC DNRESHCENT
     IDTYGSIYFD GTMTHGGYSD TMVADEHFIL RWPKNLPLDS GAPLLCAGIT TYSPLKYYGL
     DKPGTKIGVV GLGGLGHVAV KMAKAFGAQV TVIDISESKR KEALEKLGAD SFLLNSDQEQ
     MKGARSSLDG IIDTVPVNHP LAPLFDLLKP NGKLVMVGAP EKPFELPVFS LLKGRKLLGG
     TINGGIKETQ EMLDFAAKHN ITADVEVIPM DYVNTAMERL VKSDVRYRFV IDIANTMRTE
     ESLGA