P38540 (DHM2_METME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

moxI

Organism

Methylophilus methylotrophus (Bacterium W3A1)

Taxonomic identifier

17 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Methylophilales › Methylophilaceae › Methylophilus

Protein attributes

Sequence length	91 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the oxidation of primary alcohols including methanol By similarity.
Catalytic activity	A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L) + 2 H+.
Subunit structure	Heterotetramer composed of 2 alpha and 2 beta subunits.
Subcellular location	Cell inner membrane; Peripheral membrane protein; Periplasmic side. Note: Periplasmic, but associated with inner membrane.
Sequence similarities	Belongs to the methanol dehydrogenase subunit 2 family.
Sequence caution	The sequence AAA83766.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Methanol utilization
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Signal
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	methanol oxidation Inferred from electronic annotation. Source: InterPro
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2-chloroethanol cytochrome-c oxidoreductase activity Inferred from electronic annotation. Source: EC alcohol dehydrogenase (NAD) activity Inferred from electronic annotation. Source: InterPro ethanol cytochrome-c oxidoreductase activity Inferred from electronic annotation. Source: EC methanol ferricytochrome-c oxidoreductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.2

Chain

23 – 91

69

Methanol dehydrogenase [cytochrome c] subunit 2

PRO_0000025570

Amino acid modifications

Disulfide bond

28 ↔ 34

Experimental info

Sequence conflict

27

1

N → T AA sequence Ref.2

Sequence conflict

31

1

P → A AA sequence Ref.2

Sequence conflict

37

1

N → A AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

91

Helix Strand Turn

Details...

Helix

56 – 59

4

Helix

61 – 83

23

Sequences

	Sequence		Length	Mass (Da)
	P38540 [UniParc]. Last modified November 8, 2002. Version 2. Checksum: 0123300087E6716A	FASTA	91	10,037
	10 20 30 40 50 60 MKHVLTLLAL ASVFAVSNQA LAYDGQNCKE PGNCWENKPG YPEKIAGSKY DPKHDPVELN 70 80 90 KQEESIKAMD ARNAKRIANA KSSGNFVFDV K

References

[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(1996) [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(1992) [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(1993) [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(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U41041 Genomic DNA. Translation: AAA83766.1. Different initiation.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G72	X-ray	1.90	B/D	23-91	[»]
2AD6	X-ray	1.50	B/D	23-91	[»]
2AD7	X-ray	1.50	B/D	23-91	[»]
2AD8	X-ray	1.60	B/D	23-91	[»]
4AAH	X-ray	2.40	B/D	23-91	[»]

ProteinModelPortal

P38540.

SMR

P38540. Positions 23-91.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P38540.

Family and domain databases

Gene3D

4.10.160.10. 1 hit.

InterPro

IPR003420. Meth_DH_bsu.
[Graphical view]

Pfam

PF02315. MDH. 1 hit.
[Graphical view]

PIRSF

PIRSF029163. Meth_DH_beta. 1 hit.

SUPFAM

SSF48666. Meth_DH_beta. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P38540.

Entry information

Entry name

DHM2_METME

Accession

Primary (citable) accession number: P38540
Secondary accession number(s): Q59541

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	November 8, 2002
Last modified:	April 3, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program