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Protein

Methanol dehydrogenase [cytochrome c] subunit 2

Gene

moxI

Organism
Methylophilus methylotrophus (Bacterium W3A1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of primary alcohols including methanol.By similarity

Catalytic activityi

A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L) + 2 H+.

GO - Molecular functioni

  1. 2-chloroethanol cytochrome-c oxidoreductase activity Source: UniProtKB-EC
  2. alcohol dehydrogenase (NAD) activity Source: InterPro
  3. ethanol cytochrome-c oxidoreductase activity Source: UniProtKB-EC
  4. methanol ferricytochrome-c oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. methanol oxidation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanol utilization

Enzyme and pathway databases

BRENDAi1.1.2.7. 3319.
1.2.2.B2. 3319.
SABIO-RKP38540.

Names & Taxonomyi

Protein namesi
Recommended name:
Methanol dehydrogenase [cytochrome c] subunit 2 (EC:1.1.2.7)
Alternative name(s):
MDH small subunit beta
MDH-associated peptide
MEDH
Gene namesi
Name:moxI
OrganismiMethylophilus methylotrophus (Bacterium W3A1)
Taxonomic identifieri17 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylophilus

Subcellular locationi

Cell inner membrane; Peripheral membrane protein; Periplasmic side
Note: Periplasmic, but associated with inner membrane.

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 PublicationAdd
BLAST
Chaini23 – 9169Methanol dehydrogenase [cytochrome c] subunit 2PRO_0000025570Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 34

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterotetramer composed of 2 alpha and 2 beta subunits.

Structurei

Secondary structure

1
91
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 594Combined sources
Helixi61 – 8323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G72X-ray1.90B/D23-91[»]
2AD6X-ray1.50B/D23-91[»]
2AD7X-ray1.50B/D23-91[»]
2AD8X-ray1.60B/D23-91[»]
4AAHX-ray2.40B/D23-91[»]
ProteinModelPortaliP38540.
SMRiP38540. Positions 23-91.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38540.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di4.10.160.10. 1 hit.
InterProiIPR003420. Meth_DH_bsu.
[Graphical view]
PfamiPF02315. MDH. 1 hit.
[Graphical view]
PIRSFiPIRSF029163. Meth_DH_beta. 1 hit.
SUPFAMiSSF48666. SSF48666. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P38540-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHVLTLLAL ASVFAVSNQA LAYDGQNCKE PGNCWENKPG YPEKIAGSKY
60 70 80 90
DPKHDPVELN KQEESIKAMD ARNAKRIANA KSSGNFVFDV K
Length:91
Mass (Da):10,037
Last modified:November 7, 2002 - v2
Checksum:i0123300087E6716A
GO

Sequence cautioni

The sequence AAA83766.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271N → T AA sequence (PubMed:1311606).Curated
Sequence conflicti31 – 311P → A AA sequence (PubMed:1311606).Curated
Sequence conflicti37 – 371N → A AA sequence (PubMed:1311606).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41041 Genomic DNA. Translation: AAA83766.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41041 Genomic DNA. Translation: AAA83766.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G72X-ray1.90B/D23-91[»]
2AD6X-ray1.50B/D23-91[»]
2AD7X-ray1.50B/D23-91[»]
2AD8X-ray1.60B/D23-91[»]
4AAHX-ray2.40B/D23-91[»]
ProteinModelPortaliP38540.
SMRiP38540. Positions 23-91.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.2.7. 3319.
1.2.2.B2. 3319.
SABIO-RKP38540.

Miscellaneous databases

EvolutionaryTraceiP38540.

Family and domain databases

Gene3Di4.10.160.10. 1 hit.
InterProiIPR003420. Meth_DH_bsu.
[Graphical view]
PfamiPF02315. MDH. 1 hit.
[Graphical view]
PIRSFiPIRSF029163. Meth_DH_beta. 1 hit.
SUPFAMiSSF48666. SSF48666. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1."
    Xia Z.-X., Dai W.-W., Zhang Y.-F., White S.A., Boyd G.D., Mathews F.S.
    J. Mol. Biol. 259:480-501(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  2. "The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria."
    Cox J.M., Day D.J., Anthony C.
    Biochim. Biophys. Acta 1119:97-106(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-53.
    Strain: ATCC 53528 / AS1 / DSM 46235 / LMG 6787 / NCIMB 10515.
  3. "The active site structure of the calcium-containing quinoprotein methanol dehydrogenase."
    White S.A., Boyd G.D., Mathews F.S., Xia Z.-X., Dai W.-W., Zhang Y.-F., Davidson V.L.
    Biochemistry 32:12955-12958(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  4. "The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution."
    Xia Z.-X., Dai W.-W., Xiong J.-P., Hao Z.-P., Davidson V.L., White S.A., Mathews F.S.
    J. Biol. Chem. 267:22289-22297(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiDHM2_METME
AccessioniPrimary (citable) accession number: P38540
Secondary accession number(s): Q59541
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1994
Last sequence update: November 7, 2002
Last modified: March 31, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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

External Data

Dasty 3

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 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.