Reviewed, UniProtKB/Swiss-Prot P29898 (DHM2_PARDE)

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

Paracoccus denitrificans

Taxonomic identifier

266 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length	103 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. Ref.2
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
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 (NAD) activity Inferred from electronic annotation. Source: InterPro alcohol dehydrogenase (acceptor) 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 – 20

20

Potential

Chain

21 – 103

83

Methanol dehydrogenase subunit 2

PRO_0000025571

Amino acid modifications

Disulfide bond

26 ↔ 32

Ref.2

Secondary structure

1

.

.

.

.

.

.

.

103

Helix Strand Turn

Details...

Helix

54 – 57

4

Helix

59 – 81

23

Helix

88 – 90

3

Sequences

	Sequence		Length	Mass (Da)
	P29898-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 7AF8E6BD3B8731AA	FASTA	103	11,458
	10 20 30 40 50 60 MKRILTLTVA ALALGTPALA YDGTNCKAPG NCWEPKPDYP AKVEGSKYDP QHDPAELSKQ 70 80 90 100 GESLAVMDAR NEWRVWNMKK TGKFEYDVKK IDGYDETKAP PAE

References

[1]

"Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth." van Spanning R.J.M., Wansell C.W., de Boer T., Hazelaar M.J., Anazawa H., Harms N., Oltmann L.F., Stouthamer A.H. J. Bacteriol. 173:6948-6961(1991) [PubMed: 1657871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

[2]

"X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i." Xia Z.-X., Dai W.W., He Y.-N., White S.A., Mathews F.S., Davidson V.L. J. Biol. Inorg. Chem. 8:843-854(2003) [PubMed: 14505072] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 21-103 IN COMPLEX WITH ALPHA SUBUNIT, SUBUNIT, DISULFIDE BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M57684 Genomic DNA. Translation: AAA25584.1.

PIR

C41377.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LRW	X-ray	2.50	B/D	21-103	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-3924.

BRENDA

1.1.99.8. 59.

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_PARDE

Accession

Primary (citable) accession number: P29898

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	November 24, 2009
This is version 60 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)