NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1657871 [NCBI, ExPASy, EBI, Israel, Japan]
van Spanning R.J.M., Wansell C.W., de Boer T., Hazelaar M.J., Anazawa H., Harms N., Oltmann L.F., Stouthamer A.H.;
"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.";
J. Bacteriol. 173:6948-6961(1991).

[2]

X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 21-103 IN COMPLEX WITH ALPHA SUBUNIT, SUBUNIT, AND DISULFIDE BOND.
DOI=10.1007/s00775-003-0485-0; PubMed=14505072 [NCBI, ExPASy, EBI, Israel, Japan]
Xia Z.-X., Dai W.W., He Y.-N., White S.A., Mathews F.S., Davidson V.L.;
"X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i.";
J. Biol. Inorg. Chem. 8:843-854(2003).

Comments

CATALYTIC ACTIVITY: A primary alcohol + acceptor = an aldehyde + reduced acceptor.
SUBUNIT: Heterotetramer composed of 2 alpha and 2 beta subunits.
SUBCELLULAR LOCATION: Periplasm.
SIMILARITY: Belongs to the methanol dehydrogenase subunit 2 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M57684; AAA25584.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C41377; C41377.

3D structure databases

PDB

1LRW; X-ray; 2.50 A; B/D=21-103.

[ExPASy / RCSB / EBI]

PDBsum

1LRW; -.

ModBase

P29898.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3924; -.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0018468;	Molecular function: alcohol dehydrogenase (acceptor) activity (inferred from electronic annotation from EC).
GO:0004022;	Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0015946;	Biological process: methanol oxidation (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003420; Meth_DHase_bsu.
Graphical view of domain structure.

Gene3D

G3DSA:4.10.160.10; Meth_DH_beta; 1.

Pfam

PF02315; MDH; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF029163; Meth_DH_beta; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Methanol utilization; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`CHAIN`	`21 103`	`83`	`Methanol dehydrogenase subunit 2.`	`PRO_0000025571`
`DISULFID`	`26 32`
`HELIX`	`54 57`	`4`
`HELIX`	`59 81`	`23`
`HELIX`	`88 90`	`3`

Sequence information

Length: 103 AA [This is the length of the unprocessed precursor]

Molecular weight: 11458 Da [This is the MW of the unprocessed precursor]

CRC64: 7AF8E6BD3B8731AA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKRILTLTVA ALALGTPALA YDGTNCKAPG NCWEPKPDYP AKVEGSKYDP QHDPAELSKQ 

        70         80         90        100 
GESLAVMDAR NEWRVWNMKK TGKFEYDVKK IDGYDETKAP PAE

P29898 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools