[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/S0006-291X(05)80007-5; PubMed=1590782 [NCBI, ExPASy, EBI, Israel, Japan] Chistoserdov A.Y., Boyd J., Mathews F.S., Lidstrom M.E.; "The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans."; Biochem. Biophys. Res. Commun. 184:1181-1189(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69. STRAIN=ATCC 17741 / DSM 413 / IFO 16712 / NCCB 22021 / NCIB 11627; PubMed=7957249 [NCBI, ExPASy, EBI, Israel, Japan] van Spanning R.J.M., van der Palen C.J., Slotboom D.J., Reijnders W.N., Stouthamer A.H., Duine J.A.; "Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator."; Eur. J. Biochem. 226:201-210(1994).
[3]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). DOI=10.1002/prot.340140214; PubMed=1409575 [NCBI, ExPASy, EBI, Israel, Japan] Chen L., Mathews F.S., Davidson V.L., Huizinga E.G., Vellieux F.M.D., Hol W.G.J.; "Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8-A resolution."; Proteins 14:288-299(1992).
[4]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH AMICYANIN. DOI=10.1021/bi00136a006; PubMed=1599920 [NCBI, ExPASy, EBI, Israel, Japan] Chen L., Durley R., Poliks B.J., Hamada K., Chen Z., Mathews F.S., Davidson V.L., Satow Y., Huizinga E.G., Vellieux F.M.D., Hol W.G.J.; "Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin."; Biochemistry 31:4959-4964(1992).
[5]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). PubMed=8140419 [NCBI, ExPASy, EBI, Israel, Japan] Chen L., Durley R., Mathews F.S., Davidson V.L.; "Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i."; Science 264:86-90(1994).

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

M90099; AAA25580.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U12464; AAA56724.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JH0660; JH0660.

3D structure databases

PDB

1MG2; X-ray; 2.25 A; A/E/I/M=28-417.	[ExPASy / RCSB / EBI]
1MG3; X-ray; 2.40 A; A/E/I/M=28-417.	[ExPASy / RCSB / EBI]
2BBK; X-ray; 1.75 A; H=63-417.	[ExPASy / RCSB / EBI]
2GC4; X-ray; 1.90 A; A/E/I/M=32-417.	[ExPASy / RCSB / EBI]
2GC7; X-ray; 1.90 A; A/E/I/M=32-417.	[ExPASy / RCSB / EBI]
2J55; X-ray; 2.15 A; H/J=32-417.	[ExPASy / RCSB / EBI]
2J56; X-ray; 2.10 A; H/J=32-417.	[ExPASy / RCSB / EBI]
2J57; X-ray; 2.25 A; G/H/I/J=32-417.	[ExPASy / RCSB / EBI]
2MTA; X-ray; 2.40 A; H=45-417.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1MG2; -.
1MG3; -.
2BBK; -.
2GC4; -.
2GC7; -.
2J55; -.
2J56; -.
2J57; -.
2MTA; -.

ModBase

P29894.

Protein-protein interaction databases

DIP

DIP:6253N; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3909; -.

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

P29894; -.

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 28`	`28`	`Or 26 (Potential).`
`CHAIN`	`29 417`	`389`	`Methylamine dehydrogenase heavy chain.`	`PRO_0000025580`
`DISULFID`	`212 227`
`HELIX`	`40 59`	`20`
`STRAND`	`77 82`	`6`
`HELIX`	`84 86`	`3`
`STRAND`	`88 96`	`9`
`TURN`	`97 100`	`4`
`STRAND`	`101 108`	`8`
`STRAND`	`113 116`	`4`
`STRAND`	`123 132`	`10`
`STRAND`	`135 145`	`11`
`TURN`	`147 149`	`3`
`STRAND`	`152 158`	`7`
`HELIX`	`170 172`	`3`
`STRAND`	`173 175`	`3`
`STRAND`	`179 186`	`8`
`STRAND`	`188 190`	`3`
`STRAND`	`192 197`	`6`
`TURN`	`198 201`	`4`
`STRAND`	`202 208`	`7`
`STRAND`	`211 219`	`9`
`STRAND`	`222 227`	`6`
`STRAND`	`232 236`	`5`
`STRAND`	`239 241`	`3`
`STRAND`	`244 247`	`4`
`STRAND`	`263 265`	`3`
`TURN`	`266 269`	`4`
`STRAND`	`270 275`	`6`
`STRAND`	`278 284`	`7`
`STRAND`	`296 299`	`4`
`HELIX`	`301 305`	`5`
`STRAND`	`308 310`	`3`
`STRAND`	`312 314`	`3`
`STRAND`	`316 319`	`4`
`TURN`	`320 323`	`4`
`STRAND`	`324 331`	`8`
`STRAND`	`341 348`	`8`
`TURN`	`349 351`	`3`
`STRAND`	`354 364`	`11`
`STRAND`	`366 369`	`4`
`STRAND`	`372 374`	`3`
`STRAND`	`376 381`	`6`
`TURN`	`382 385`	`4`
`STRAND`	`386 391`	`6`
`TURN`	`392 394`	`3`
`STRAND`	`397 401`	`5`
`STRAND`	`410 413`	`4`

Sequence information

Length: 417 AA [This is the length of the unprocessed precursor]

Molecular weight: 45440 Da [This is the MW of the unprocessed precursor]

CRC64: 8187A8B694208BE2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALPPNFMPL FRASLIGLGL GCSALALAAS AQDAPEAETQ AQETQGQAAA RAAAADLAAG 

        70         80         90        100        110        120 
QDDEPRILEA PAPDARRVYV NDPAHFAAVT QQFVIDGEAG RVIGMIDGGF LPNPVVADDG 

       130        140        150        160        170        180 
SFIAHASTVF SRIARGERTD YVEVFDPVTL LPTADIELPD APRFLVGTYP WMTSLTPDGK 

       190        200        210        220        230        240 
TLLFYQFSPA PAVGVVDLEG KAFKRMLDVP DCYHIFPTAP DTFFMHCRDG SLAKVAFGTE 

       250        260        270        280        290        300 
GTPEITHTEV FHPEDEFLIN HPAYSQKAGR LVWPTYTGKI HQIDLSSGDA KFLPAVEALT 

       310        320        330        340        350        360 
EAERADGWRP GGWQQVAYHR ALDRIYLLVD QRDEWRHKTA SRLLVVLDAK TGERLAKFEM 

       370        380        390        400        410 
GHEIDSINVS QDEKPLLYAL STGDKTLYIH DAESGEELRS VNQLGHGPQV ITTADMG

P29894 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