MTDH_AGABI
ID MTDH_AGABI Reviewed; 262 AA.
AC O93868;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=NADP-dependent mannitol dehydrogenase;
DE Short=MtDH {ECO:0000303|PubMed:11335726};
DE EC=1.1.1.138 {ECO:0000269|PubMed:11335726};
DE AltName: Full=Mannitol 2-dehydrogenase [NADP(+)] {ECO:0000303|PubMed:11335726};
GN Name=mtdH;
OS Agaricus bisporus (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX NCBI_TaxID=5341;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-20 AND 211-230, AND
RP CHARACTERIZATION.
RC STRAIN=Horst U1;
RX PubMed=9835550; DOI=10.1128/aem.64.12.4689-4696.1998;
RA Stoop J.M.H., Mooibroek H.;
RT "Cloning and characterization of NADP-mannitol dehydrogenase cDNA from the
RT button mushroom, Agaricus bisporus, and its expression in response to NaCl
RT stress.";
RL Appl. Environ. Microbiol. 64:4689-4696(1998).
RN [2]
RP CRYSTALLIZATION.
RX PubMed=11320313; DOI=10.1107/s0907444901002542;
RA Sassoon J., Hoerer S., Stoop J., Mooibroek H., Baumann U.;
RT "Crystallization and preliminary crystallographic analysis of mannitol
RT dehydrogenase (MtDH) from the common mushroom Agaricus bisporus.";
RL Acta Crystallogr. D 57:711-713(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=11335726; DOI=10.1074/jbc.m102850200;
RA Horer S., Stoop J., Mooibroek H., Baumann U., Sassoon J.;
RT "The crystallographic structure of the mannitol 2-dehydrogenase NADP+
RT binary complex from Agaricus bisporus.";
RL J. Biol. Chem. 276:27555-27561(2001).
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:11335726};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29.3 mM for mannitol (at pH 9.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11335726};
CC KM=58.7 mM for fructose (at pH 9.0 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:11335726};
CC Note=kcat is 2.20 sec(-1) for mannitol. kcat is 7.31 sec(-1) for
CC fructose. {ECO:0000269|PubMed:11335726};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11335726}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF053764; AAC79985.1; -; mRNA.
DR PDB; 1H5Q; X-ray; 1.50 A; A/B/C/D/E/F/G/H/I/J/K/L=2-262.
DR PDBsum; 1H5Q; -.
DR AlphaFoldDB; O93868; -.
DR SMR; O93868; -.
DR EvolutionaryTrace; O93868; -.
DR GO; GO:0050085; F:mannitol 2-dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; 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 PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9835550"
FT CHAIN 2..262
FT /note="NADP-dependent mannitol dehydrogenase"
FT /id="PRO_0000054726"
FT ACT_SITE 149
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:11335726"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:11335726"
FT ACT_SITE 173
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000305|PubMed:11335726"
FT BINDING 20..23
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11335726,
FT ECO:0007744|PDB:1H5Q"
FT BINDING 43..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11335726,
FT ECO:0007744|PDB:1H5Q"
FT BINDING 69..70
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11335726,
FT ECO:0007744|PDB:1H5Q"
FT BINDING 96
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11335726,
FT ECO:0007744|PDB:1H5Q"
FT BINDING 169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11335726,
FT ECO:0007744|PDB:1H5Q"
FT BINDING 173
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11335726,
FT ECO:0007744|PDB:1H5Q"
FT BINDING 202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11335726,
FT ECO:0007744|PDB:1H5Q"
FT BINDING 206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11335726,
FT ECO:0007744|PDB:1H5Q"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1H5Q"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:1H5Q"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:1H5Q"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:1H5Q"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:1H5Q"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 122..138
FT /evidence="ECO:0007829|PDB:1H5Q"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1H5Q"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 167..187
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1H5Q"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1H5Q"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:1H5Q"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1H5Q"
SQ SEQUENCE 262 AA; 28019 MW; D92DDC2720CE06EC CRC64;
MAPGFTISFV NKTIIVTGGN RGIGLAFTRA VAAAGANVAV IYRSAKDAVE VTEKVGKEFG
VKTKAYQCDV SNTDIVTKTI QQIDADLGAI SGLIANAGVS VVKPATELTH EDFKFVYDVN
VFGVFNTCRA VAKLWLQKQQ KGSIVVTSSM SSQIINQSSL NGSLTQVFYN SSKAACSNLV
KGLAAEWASA GIRVNALSPG YVNTDQTAHM DKKIRDHQAS NIPLNRFAQP EEMTGQAILL
LSDHATYMTG GEYFIDGGQL IW
