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Protein

Methanol dehydrogenase [cytochrome c] subunit 2

Gene

moxI

Organism
Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of primary alcohols including methanol.

Catalytic activityi

A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L) + 2 H+.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanol utilization

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3922.
MEXT272630:GBY6-4280-MONOMER.
BRENDAi1.1.2.7. 3296.

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
Synonyms:mxaI
Ordered Locus Names:MexAM1_META1p4535
OrganismiMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1)
Taxonomic identifieri272630 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
Proteomesi
  • UP000009081 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 9674Methanol dehydrogenase [cytochrome c] subunit 2PRO_0000025569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 341 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterotetramer composed of 2 alpha and 2 beta subunits.

Protein-protein interaction databases

STRINGi272630.MexAM1_META1p4535.

Structurei

Secondary structure

1
96
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 594Combined sources
Helixi61 – 8323Combined sources
Helixi90 – 923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H4IX-ray1.94B/D23-96[»]
1H4JX-ray3.00B/D/F/H23-96[»]
1W6SX-ray1.20B/D23-96[»]
ProteinModelPortaliP14775.
SMRiP14775. Positions 23-95.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14775.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105P0N. Bacteria.
ENOG4111V4Q. LUCA.
HOGENOMiHOG000144327.
KOiK14029.
OMAiPGNCWEP.
OrthoDBiEOG66F0B8.

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.

P14775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTTLIAAAI VALSGLAAPA LAYDGTKCKA AGNCWEPKPG FPEKIAGSKY
60 70 80 90
DPKHDPKELN KQADSIKQME ERNKKRVENF KKTGKFEYDV AKISAN
Length:96
Mass (Da):10,512
Last modified:April 1, 1990 - v1
Checksum:i9C082124F26F3159
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15792 Genomic DNA. Translation: CAA33796.1.
X07856 Genomic DNA. Translation: CAA30705.1.
CP001510 Genomic DNA. Translation: ACS42166.1.
RefSeqiWP_003599120.1. NC_012808.1.

Genome annotation databases

EnsemblBacteriaiACS42166; ACS42166; MexAM1_META1p4535.
KEGGimea:Mex_1p4535.
PATRICi22514713. VBIMetExt101010_4411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15792 Genomic DNA. Translation: CAA33796.1.
X07856 Genomic DNA. Translation: CAA30705.1.
CP001510 Genomic DNA. Translation: ACS42166.1.
RefSeqiWP_003599120.1. NC_012808.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H4IX-ray1.94B/D23-96[»]
1H4JX-ray3.00B/D/F/H23-96[»]
1W6SX-ray1.20B/D23-96[»]
ProteinModelPortaliP14775.
SMRiP14775. Positions 23-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272630.MexAM1_META1p4535.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACS42166; ACS42166; MexAM1_META1p4535.
KEGGimea:Mex_1p4535.
PATRICi22514713. VBIMetExt101010_4411.

Phylogenomic databases

eggNOGiENOG4105P0N. Bacteria.
ENOG4111V4Q. LUCA.
HOGENOMiHOG000144327.
KOiK14029.
OMAiPGNCWEP.
OrthoDBiEOG66F0B8.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3922.
MEXT272630:GBY6-4280-MONOMER.
BRENDAi1.1.2.7. 3296.

Miscellaneous databases

EvolutionaryTraceiP14775.

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

« Hide 'large scale' publications
  1. "The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1."
    Nunn D.N., Day D., Anthony C.
    Biochem. J. 260:857-862(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "The nucleotide sequence and deduced amino acid sequence of the genes for cytochrome cL and a hypothetical second subunit of the methanol dehydrogenase of Methylobacterium AM1."
    Nunn D.N., Anthony C.
    Nucleic Acids Res. 16:7722-7722(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14718 / DSM 1338 / AM1.
  4. "The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues."
    Blake C.C.F., Ghosh M., Harlos K., Avezoux A., Anthony C.
    Nat. Struct. Biol. 1:102-105(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  5. "The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A."
    Ghosh M., Anthony C., Harlos K., Goodwin M.G., Blake C.
    Structure 3:177-187(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
  6. "Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L)."
    Afolabi P.R., Mohammed F., Amaratunga K., Majekodunmi O., Dales S.L., Gill R., Thompson D., Cooper J.B., Wood S.P., Goodwin P.M., Anthony C.
    Biochemistry 40:9799-9809(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), CATALYTIC ACTIVITY, REACTION MECHANISM.

Entry informationi

Entry nameiDHM2_METEA
AccessioniPrimary (citable) accession number: P14775
Secondary accession number(s): C5AQA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: December 9, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.