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Protein

NAD-dependent methanol dehydrogenase

Gene

mdh

Organism
Bacillus methanolicus
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of methanol to yield formaldehyde. It possesses a NADH-dependent formaldehyde reductase activity and cannot use NADP.6 Publications

Catalytic activityi

Methanol + NAD+ = formaldehyde + NADH.4 Publications

Cofactori

Protein has several cofactor binding sites:

Activity regulationi

Stimulated by the activator protein Act wich requires the presence of magnesium ions. Inhibited by 1,10-phenanthroline.3 Publications

Kineticsi

  1. KM=9 µM for NADH1 Publication
  2. KM=0.02 mM for NAD2 Publications
  3. KM=0.7 mM for formaldehyde (without activator protein at pH 9.5 and 50 degrees Celsius)1 Publication
  4. KM=2 mM for formaldehyde (with activator protein at pH 9.5 and 50 degrees Celsius)1 Publication
  5. KM=57 mM for ethanol (with the activator protein at pH 9.5 and 50 degrees Celsius)1 Publication
  6. KM=94 mM for ethanol (without activator protein at pH 9.5 and 50 degrees Celsius)1 Publication
  7. KM=140 mM for methanol (with the activator protein at pH 9.5 and 50 degrees Celsius)1 Publication
  8. KM=230 mM for methanol (without activator protein at pH 9.5 and 50 degrees Celsius)1 Publication
  1. Vmax=1310 µmol/min/mg enzyme2 Publications

Pathwayi: methanol degradation

This protein is involved in step 1 of the subpathway that synthesizes formaldehyde from methanol.Curated
Proteins known to be involved in this subpathway in this organism are:
  1. NAD-dependent methanol dehydrogenase (mdh)
This subpathway is part of the pathway methanol degradation, which is itself part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes formaldehyde from methanol, the pathway methanol degradation and in One-carbon metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processMethanol utilization
LigandMagnesium, NAD, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15636
SABIO-RKiP31005
UniPathwayi
UPA00928;UER00893

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent methanol dehydrogenase1 Publication (EC:1.1.1.2444 Publications)
Short name:
MDH1 Publication
Short name:
MEDH1 Publication
Alternative name(s):
Type 3 alcohol dehydrogenase1 Publication
Gene namesi
Name:mdh1 Publication
OrganismiBacillus methanolicus
Taxonomic identifieri1471 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13G → A: Shows a reduced dehydrogenase activity. 1 Publication1
Mutagenesisi15G → A: Shows almost the same dehydrogenase activity as the wild-type. 1 Publication1
Mutagenesisi88D → N: Shows almost the same dehydrogenase activity as the wild-type. 1 Publication1
Mutagenesisi95G → A: Shows a 10-fold decreased affinity for NAD and NADH and a strongly reduced dehydrogenase activity. Completely insensitive to the stimulating effect of the activator protein Act. 1 Publication1
Mutagenesisi97S → G: Shows an increase of the dehydrogenase activity and a decrease of the affinity for NAD and NADH. Completely insensitive to the stimulating effect of the activator protein Act. It does not bind NAD. 1 Publication1
Mutagenesisi97S → T: Shows an increase of the dehydrogenase activity and affinity for NAD and NADH. 1 Publication1
Mutagenesisi100D → N: Loss of dehydrogenase activity. It still binds NADH. 1 Publication1
Mutagenesisi103K → R: Loss of dehydrogenase activity. It does not bind NADH. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000878342 – 381NAD-dependent methanol dehydrogenaseAdd BLAST380

Interactioni

Subunit structurei

Homodecamer.2 Publications

Structurei

3D structure databases

ProteinModelPortaliP31005
SMRiP31005
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK00093

Family and domain databases

InterProiView protein in InterPro
IPR001670 ADH_Fe/GldA
IPR018211 ADH_Fe_CS
IPR039697 Alcohol_dehydrogenase_Fe
PANTHERiPTHR11496 PTHR11496, 1 hit
PfamiView protein in Pfam
PF00465 Fe-ADH, 1 hit
PROSITEiView protein in PROSITE
PS00913 ADH_IRON_1, 1 hit
PS00060 ADH_IRON_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P31005-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTNFFIPPAS VIGRGAVKEV GTRLKQIGAK KALIVTDAFL HSTGLSEEVA
60 70 80 90 100
KNIREAGLDV AIFPKAQPDP ADTQVHEGVD VFKQENCDAL VSIGGGSSHD
110 120 130 140 150
TAKAIGLVAA NGGRINDYQG VNSVEKPVVP VVAITTTAGT GSETTSLAVI
160 170 180 190 200
TDSARKVKMP VIDEKITPTV AIVDPELMVK KPAGLTIATG MDALSHAIEA
210 220 230 240 250
YVAKGATPVT DAFAIQAMKL INEYLPKAVA NGEDIEAREA MAYAQYMAGV
260 270 280 290 300
AFNNGGLGLV HSISHQVGGV YKLQHGICNS VNMPHVCAFN LIAKTERFAH
310 320 330 340 350
IAELLGENVS GLSTAAAAER AIVALERYNK NFGIPSGYAE MGVKEEDIEL
360 370 380
LAKNAFEDVC TQSNPRVATV QDIAQIIKNA L
Length:381
Mass (Da):40,045
Last modified:January 23, 2007 - v3
Checksum:i8EA251B36F73749D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18K → L AA sequence (PubMed:1995642).Curated1
Sequence conflicti42S → A AA sequence (PubMed:1995642).Curated1
Sequence conflicti50A → D AA sequence (PubMed:1995642).Curated1
Sequence conflicti59D → N AA sequence (PubMed:1995642).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65004 Genomic DNA Translation: AAA22593.1

Genome annotation databases

KEGGiag:AAA22593

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65004 Genomic DNA Translation: AAA22593.1

3D structure databases

ProteinModelPortaliP31005
SMRiP31005
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA22593

Phylogenomic databases

KOiK00093

Enzyme and pathway databases

UniPathwayi
UPA00928;UER00893

BioCyciMetaCyc:MONOMER-15636
SABIO-RKiP31005

Family and domain databases

InterProiView protein in InterPro
IPR001670 ADH_Fe/GldA
IPR018211 ADH_Fe_CS
IPR039697 Alcohol_dehydrogenase_Fe
PANTHERiPTHR11496 PTHR11496, 1 hit
PfamiView protein in Pfam
PF00465 Fe-ADH, 1 hit
PROSITEiView protein in PROSITE
PS00913 ADH_IRON_1, 1 hit
PS00060 ADH_IRON_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMEDH_BACMT
AccessioniPrimary (citable) accession number: P31005
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 67 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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