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}.
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; 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