[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8407797 [NCBI, ExPASy, EBI, Israel, Japan] Huitema F., van Beeumen J., van Driessche G., Duine J.A., Canters G.W.; "Cloning and sequencing of the gene coding for the large subunit of methylamine dehydrogenase from Thiobacillus versutus."; J. Bacteriol. 175:6254-6259(1993).
[2]	X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). PubMed=2792083 [NCBI, ExPASy, EBI, Israel, Japan] Vellieux F.M.D., Huitema F., Groendijk H., Kalk K.H., Jzn J.F., Jongejan J.A., Duine J.A., Petratos K., Drenth J., Hol W.G.J.; "Structure of quinoprotein methylamine dehydrogenase at 2.25-A resolution."; EMBO J. 8:2171-2178(1989).
[3]	X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). DOI=10.1107/S010876819000636X; PubMed=2085423 [NCBI, ExPASy, EBI, Israel, Japan] Vellieux F.M.D., Kalk K.H., Hol W.G.J.; "Structure determination of quinoprotein methylamine dehydrogenase from Thiobacillus versutus."; Acta Crystallogr. B 46:806-823(1990).

Comments

FUNCTION: Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.
CATALYTIC ACTIVITY: RCH₂NH₂ + H₂O + acceptor = RCHO + NH₃ + reduced acceptor.
SUBUNIT: Tetramer of two light and two heavy chains.
SUBCELLULAR LOCATION: Periplasm.
SIMILARITY: Belongs to the aromatic amine dehydrogenase heavy chain 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

L08575; AAA72335.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A36934; A36934.

3D structure databases

PDB

1MAE; X-ray; 2.80 A; H=59-400.	[ExPASy / RCSB / EBI]
1MAF; X-ray; 2.60 A; H=59-400.	[ExPASy / RCSB / EBI]
2MAD; X-ray; 2.25 A; H=59-400.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1MAE; -.
1MAF; -.
2MAD; -.

SMR

P23006; 72-424.

ModBase

P23006.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3901; -.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from InterPro).
GO:0030058;	Molecular function: amine dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0030416;	Biological process: methylamine metabolic process (inferred from electronic annotation from InterPro).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013476; MeN_DHase_hvc.
IPR009451; Metamine_DHase_Hsu.
IPR015943; WD40/YVTN_repeat-like.
Graphical view of domain structure.

Gene3D

G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.

Pfam

PF06433; Me-amine-dh_H; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF017797; TTQ_MADH_Hv; 1.

TIGRFAMs

TIGR02658; TTQ_MADH_Hv; 1.

Other

P23006; -.

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

Keywords

3D-structure; Electron transport; Oxidoreductase; Periplasm; Signal; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 31`	`31`	`Potential.`
`CHAIN`	`32 426`	`395`	`Methylamine dehydrogenase heavy chain.`	`PRO_0000025581`
`DISULFID`	`221 236`

Sequence information

Length: 426 AA [This is the length of the unprocessed precursor]

Molecular weight: 46388 Da [This is the MW of the unprocessed precursor]

CRC64: 4ECDF8F6A7AE8696 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASARESTPR YLTLIGATLA CSALALGAAQ AQTEPAEPEA PAETAAADAA GQTEGQRGAA 

        70         80         90        100        110        120 
EAAAALAAGE ADEPVILEAP APDARRVYIQ DPAHFAAITQ QFVIDGSTGR ILGMTDGGFL 

       130        140        150        160        170        180 
PHPVAAEDGS FFAQASTVFE RIARGKRTDY VEVFDPVTFL PIADIELPDA PRFLVGTYQW 

       190        200        210        220        230        240 
MNALTPDNKN LLFYQFSPAP AVGVVDLEGK TFDRMLDVPD CYHIFPASPT VFYMNCRDGS 

       250        260        270        280        290        300 
LARVDFADGE TKVTNTEVFH TEDELLINHP AFSLRSGRLV WPTYTGKIFQ ADLTAEGATF 

       310        320        330        340        350        360 
RAPIEALTEA ERADDWRPGG WQQTAYHRQS DRIYLLVDQR DEWKHKAASR FVVVLNAETG 

       370        380        390        400        410        420 
ERINKIELGH EIDSINVSQD AEPLLYALSA GTQTLHIYDA ATGEELRSVD QLGRGPQIIT 


THDMDS

P23006 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