MTDH_DAVTA
ID MTDH_DAVTA Reviewed; 267 AA.
AC P0C0Y5; Q2TV79;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=NADP-dependent mannitol dehydrogenase {ECO:0000303|PubMed:16608840, ECO:0000303|PubMed:20420880};
DE Short=MtDH {ECO:0000303|PubMed:16608840, ECO:0000303|PubMed:20420880};
DE EC=1.1.1.138 {ECO:0000269|PubMed:16608840};
DE AltName: Full=Mannitol 2-dehydrogenase [NADP(+)] {ECO:0000305};
DE AltName: Allergen=Cla h 8 {ECO:0000303|PubMed:16608840};
OS Davidiella tassiana (Mycosphaerella tassiana) (Cladosporium herbarum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Cladosporium.
OX NCBI_TaxID=29918;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-19; 22-31; 81-86; 208-217
RP AND 229-238, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, ALLERGEN, AND CIRCULAR DICHROISM ANALYSIS.
RC STRAIN=280202-Berlin {ECO:0000303|PubMed:16608840};
RC TISSUE=Mycelium {ECO:0000303|PubMed:16608840};
RX PubMed=16608840; DOI=10.1074/jbc.m513638200;
RA Simon-Nobbe B., Denk U., Schneider P.B., Radauer C., Teige M., Crameri R.,
RA Hawranek T., Lang R., Richter K., Schmid-Grendelmeier P., Nobbe S.,
RA Hartl A., Breitenbach M.;
RT "NADP-dependent mannitol dehydrogenase, a major allergen of Cladosporium
RT herbarum.";
RL J. Biol. Chem. 281:16354-16360(2006).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), SUBUNIT, AND REACTION MECHANISM.
RX PubMed=20420880; DOI=10.1016/j.biochi.2010.04.012;
RA Nuess D., Goettig P., Magler I., Denk U., Breitenbach M., Schneider P.B.,
RA Brandstetter H., Simon-Nobbe B.;
RT "Crystal structure of the NADP-dependent mannitol dehydrogenase from
RT Cladosporium herbarum: Implications for oligomerisation and catalysis.";
RL Biochimie 92:985-993(2010).
CC -!- FUNCTION: Interconverts D-mannitol and D-fructose. Not active with
CC fructose 6-phosphate or NADH. {ECO:0000269|PubMed:16608840}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol + NADP(+) = D-fructose + H(+) + NADPH;
CC Xref=Rhea:RHEA:16765, ChEBI:CHEBI:15378, ChEBI:CHEBI:16899,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.138; Evidence={ECO:0000269|PubMed:16608840};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16766;
CC Evidence={ECO:0000269|PubMed:16608840};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16767;
CC Evidence={ECO:0000269|PubMed:16608840};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.17 uM for D-fructose (at pH 7.5) {ECO:0000269|PubMed:16608840};
CC KM=0.23 uM for D-mannitol (at pH 7.5) {ECO:0000269|PubMed:16608840};
CC KM=53 uM for NADPH (at pH 7.5) {ECO:0000269|PubMed:16608840};
CC KM=67 uM for NADP(+) (at pH 7.5) {ECO:0000269|PubMed:16608840};
CC -!- SUBUNIT: Exists as monomer, dimer and tetramer.
CC {ECO:0000269|PubMed:20420880}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 57% of
CC 21 C.herbarum-allergic patients tested. {ECO:0000269|PubMed:16608840}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AY191816; AAO91801.1; -; mRNA.
DR PDB; 3GDF; X-ray; 2.50 A; A/B/C/D=1-267.
DR PDB; 3GDG; X-ray; 2.30 A; A/B/C/D=1-267.
DR PDB; 7KRG; X-ray; 2.04 A; A/B/C/D/E/F/G/H=1-267.
DR PDBsum; 3GDF; -.
DR PDBsum; 3GDG; -.
DR PDBsum; 7KRG; -.
DR AlphaFoldDB; P0C0Y5; -.
DR SMR; P0C0Y5; -.
DR Allergome; 2485; Cla h 8.
DR Allergome; 3207; Cla h 8.0101.
DR PRIDE; P0C0Y5; -.
DR BRENDA; 1.1.1.138; 7286.
DR EvolutionaryTrace; P0C0Y5; -.
DR GO; GO:0050085; F:mannitol 2-dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019594; P:mannitol metabolic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16608840"
FT CHAIN 2..267
FT /note="NADP-dependent mannitol dehydrogenase"
FT /evidence="ECO:0000305|PubMed:16608840"
FT /id="PRO_0000054728"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:20420880"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:20420880"
FT ACT_SITE 179
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000305|PubMed:20420880"
FT BINDING 108
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 179
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:3GDG"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:3GDG"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:3GDG"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:3GDG"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:3GDG"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3GDG"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:3GDG"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3GDF"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:3GDG"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3GDG"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:3GDG"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:3GDG"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:3GDG"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3GDG"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3GDG"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:3GDG"
FT HELIX 173..192
FT /evidence="ECO:0007829|PDB:3GDG"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:3GDG"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:3GDG"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:3GDF"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3GDG"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:3GDG"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:3GDG"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:3GDF"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:3GDG"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3GDG"
SQ SEQUENCE 267 AA; 28464 MW; 4CF5EA012D71D446 CRC64;
MPGQQATKHE SLLDQLSLKG KVVVVTGASG PKGMGIEAAR GCAEMGAAVA ITYASRAQGA
EENVKELEKT YGIKAKAYKC QVDSYESCEK LVKDVVADFG QIDAFIANAG ATADSGILDG
SVEAWNHVVQ VDLNGTFHCA KAVGHHFKER GTGSLVITAS MSGHIANFPQ EQTSYNVAKA
GCIHMARSLA NEWRDFARVN SISPGYIDTG LSDFVPKETQ QLWHSMIPMG RDGLAKELKG
AYVYFASDAS TYTTGADLLI DGGYTTR
