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Protein

NADP-dependent mannitol dehydrogenase

Gene

mtdH

Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-mannitol + NADP+ = D-fructose + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei149 – 1491Substrate
Active sitei169 – 1691Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 4426NADP1 PublicationAdd
BLAST
Nucleotide bindingi150 – 17425NADP1 PublicationAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-dependent mannitol dehydrogenase (EC:1.1.1.138)
Short name:
MtDH
Alternative name(s):
Mannitol 2-dehydrogenase [NADP(+)]
Gene namesi
Name:mtdH
OrganismiAgaricus bisporus (White button mushroom)
Taxonomic identifieri5341 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 262261NADP-dependent mannitol dehydrogenasePRO_0000054726Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi12 – 176Combined sources
Turni18 – 203Combined sources
Helixi22 – 3312Combined sources
Beta strandi36 – 449Combined sources
Helixi48 – 5912Combined sources
Beta strandi63 – 675Combined sources
Helixi73 – 8614Combined sources
Beta strandi89 – 957Combined sources
Helixi105 – 1073Combined sources
Helixi110 – 12011Combined sources
Helixi122 – 13817Combined sources
Beta strandi142 – 1476Combined sources
Helixi150 – 1523Combined sources
Beta strandi157 – 1593Combined sources
Helixi167 – 18721Combined sources
Helixi188 – 1903Combined sources
Beta strandi192 – 1998Combined sources
Helixi205 – 2095Combined sources
Helixi212 – 2209Combined sources
Helixi230 – 2334Combined sources
Helixi234 – 2418Combined sources
Helixi243 – 2453Combined sources
Beta strandi252 – 2554Combined sources
Helixi259 – 2613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H5QX-ray1.50A/B/C/D/E/F/G/H/I/J/K/L2-262[»]
ProteinModelPortaliO93868.
SMRiO93868. Positions 3-262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO93868.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O93868-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPGFTISFV NKTIIVTGGN RGIGLAFTRA VAAAGANVAV IYRSAKDAVE
60 70 80 90 100
VTEKVGKEFG VKTKAYQCDV SNTDIVTKTI QQIDADLGAI SGLIANAGVS
110 120 130 140 150
VVKPATELTH EDFKFVYDVN VFGVFNTCRA VAKLWLQKQQ KGSIVVTSSM
160 170 180 190 200
SSQIINQSSL NGSLTQVFYN SSKAACSNLV KGLAAEWASA GIRVNALSPG
210 220 230 240 250
YVNTDQTAHM DKKIRDHQAS NIPLNRFAQP EEMTGQAILL LSDHATYMTG
260
GEYFIDGGQL IW
Length:262
Mass (Da):28,019
Last modified:January 23, 2007 - v3
Checksum:iD92DDC2720CE06EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053764 mRNA. Translation: AAC79985.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053764 mRNA. Translation: AAC79985.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H5QX-ray1.50A/B/C/D/E/F/G/H/I/J/K/L2-262[»]
ProteinModelPortaliO93868.
SMRiO93868. Positions 3-262.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO93868.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of NADP-mannitol dehydrogenase cDNA from the button mushroom, Agaricus bisporus, and its expression in response to NaCl stress."
    Stoop J.M.H., Mooibroek H.
    Appl. Environ. Microbiol. 64:4689-4696(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-20 AND 211-230, CHARACTERIZATION.
    Strain: Horst U1.
  2. "Crystallization and preliminary crystallographic analysis of mannitol dehydrogenase (MtDH) from the common mushroom Agaricus bisporus."
    Sassoon J., Hoerer S., Stoop J., Mooibroek H., Baumann U.
    Acta Crystallogr. D 57:711-713(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  3. "The crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus."
    Horer S., Stoop J., Mooibroek H., Baumann U., Sassoon J.
    J. Biol. Chem. 276:27555-27561(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH NADP, HOMOTETRAMERIZATION.

Entry informationi

Entry nameiMTDH_AGABI
AccessioniPrimary (citable) accession number: O93868
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.