Reviewed, UniProtKB/Swiss-Prot P14775 (DHM2_METEX)

Names and origin

Protein names

Recommended name:
    Methanol dehydrogenase subunit 2
    EC=1.1.99.8
Alternative name(s):
    MDH small subunit beta
    MDH-associated peptide
    MEDH

Gene names

Name:

moxI

Organism

Methylobacterium extorquens (Protomonas extorquens)

Taxonomic identifier

408 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium

Protein attributes

Sequence length	96 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)

Catalytic activity	A primary alcohol + acceptor = an aldehyde + reduced acceptor.
Subunit structure	Heterotetramer composed of 2 alpha and 2 beta subunits.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the methanol dehydrogenase subunit 2 family.

Ontologies

Keywords
Biological process	Methanol utilization
Cellular component	Periplasm
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alcohol dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC alcohol dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Chain

23 – 96

74

Methanol dehydrogenase subunit 2

PRO_0000025569

Amino acid modifications

Disulfide bond

28 ↔ 34

Ref.3

Secondary structure

1

.

.

.

.

.

.

.

96

Helix Strand Turn

Details...

Helix

56 – 59

4

Helix

61 – 83

23

Helix

90 – 92

3

Sequences

	Sequence		Length	Mass (Da)
	P14775-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 9C082124F26F3159	FASTA	96	10,512
	10 20 30 40 50 60 MKTTLIAAAI VALSGLAAPA LAYDGTKCKA AGNCWEPKPG FPEKIAGSKY DPKHDPKELN 70 80 90 KQADSIKQME ERNKKRVENF KKTGKFEYDV AKISAN

References

[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: 2504152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: AM1 / NCIMB 9133.
[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: 2842733] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AM1 / NCIMB 9133.
[3]	"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: 7656012] [Abstract] Cited for: DISULFIDE BONDS.
[4]	"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: 7735834] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
[5]	"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: 11502173] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X15792 Genomic DNA. Translation: CAA33796.1.
X07856 Genomic DNA. Translation: CAA30705.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H4I	X-ray	1.94	B/D	23-96	[»]
1H4J	X-ray	3.00	B/D/F/H	23-96	[»]
1W6S	X-ray	1.20	B/D	23-96	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3922.

BRENDA

1.1.99.8. 20440.

Family and domain databases

InterPro

IPR003420. Meth_DH_bsu.
[Graphical view]

Gene3D

G3DSA:4.10.160.10. Meth_DH_beta. 1 hit.

Pfam

PF02315. MDH. 1 hit.
[Graphical view]

PIRSF

PIRSF029163. Meth_DH_beta. 1 hit.

ProtoNet

Search...

Entry information

Entry name

DHM2_METEX

Accession

Primary (citable) accession number: P14775

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)