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MTDH_PETCR
ID   MTDH_PETCR              Reviewed;         337 AA.
AC   P42754;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Mannitol dehydrogenase;
DE            EC=1.1.1.255;
DE   AltName: Full=NAD-dependent mannitol dehydrogenase;
DE   Flags: Fragment;
GN   Name=ELI3;
OS   Petroselinum crispum (Parsley) (Petroselinum hortense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Petroselinum.
OX   NCBI_TaxID=4043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1464303; DOI=10.1002/j.1460-2075.1992.tb05572.x;
RA   Kiedrowski S., Kawalleck P., Hahlbrock K., Somssich I.E., Dangl J.L.;
RT   "Rapid activation of a novel plant defense gene is strictly dependent on
RT   the Arabidopsis RPM1 disease resistance locus.";
RL   EMBO J. 11:4677-4684(1992).
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; X67817; CAA48028.1; -; mRNA.
DR   PIR; S28045; S28045.
DR   AlphaFoldDB; P42754; -.
DR   SMR; P42754; -.
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..337
FT                   /note="Mannitol dehydrogenase"
FT                   /id="PRO_0000160814"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   337 AA;  36210 MW;  8C71A08D8CAD5656 CRC64;
     ILSPFKFSRR ATGDNDVRFK VLYCGVCHSD LHMVKNEWGM TTYPIVPGHE IVGRVTEVGS
     KVEKFKVGDA VGVGCLVGSC LSCENCDDDS ENNCAKQVQT YAFTNVDGSI TYGGYADSMV
     ADQHFVLRWP ENLPLDSGAP LLCAGITTYS PLRYHGLDKP GTKVGVVGLG GLGHVAVKMA
     KAFGAHVTVI STSESKKQEA LEKLGADEFL VSSDSDQMQA ATGTLHGIID TVSALHPVVP
     LLGLLKVNGK LVMVGAPEKP LELPVFPLLM GRKVLAGSNI GGLKETQEML DFAAQHNITA
     DVEVIPVDYV NTAMERLVKS DVRYRFVIDV ANTIKTE
 
 
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