[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 158-188. STRAIN=ATCC 19367 / IFO 13301 / NCIMB 8944 / NRRL B-3785; DOI=10.1016/0014-5793(90)81475-4; PubMed=2261991 [NCBI, ExPASy, EBI, Israel, Japan] van Spanning R.J.M., Wansell C.W., Reijnders W.N.M., Oltmann L.F., Stouthamer A.H.; "Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation."; FEBS Lett. 275:217-220(1990).
[3]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 64-188. 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) OF 64-188 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.
COFACTOR: Contains 1 tryptophan tryptophylquinone per subunit.
PATHWAY: One-carbon metabolism; methylamine degradation; formaldehyde from methylamine: step 1/1 .
SUBUNIT: Heterotetramer of two light and two heavy chains.
SUBCELLULAR LOCATION: Periplasm.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
PTM: Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the indole ring of a tryptophan to form tryptophylquinone followed by covalent cross-linking with another tryptophan residue.
SIMILARITY: Belongs to the aromatic amine dehydrogenase light 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

M90098; AAA25578.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X55665; CAA39198.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JH0661; JH0661.

3D structure databases

PDB

1MG2; X-ray; 2.25 A; B/F/J/N=58-188.	[ExPASy / RCSB / EBI]
1MG3; X-ray; 2.40 A; B/F/J/N=58-188.	[ExPASy / RCSB / EBI]
2BBK; X-ray; 1.75 A; L/M=64-188.	[ExPASy / RCSB / EBI]
2GC4; X-ray; 1.90 A; B/F/J/N=58-188.	[ExPASy / RCSB / EBI]
2GC7; X-ray; 1.90 A; B/F/J/N=58-188.	[ExPASy / RCSB / EBI]
2J55; X-ray; 2.15 A; L/M=58-188.	[ExPASy / RCSB / EBI]
2J56; X-ray; 2.10 A; L/M=58-188.	[ExPASy / RCSB / EBI]
2J57; X-ray; 2.25 A; K/L/M/N=58-188.	[ExPASy / RCSB / EBI]
2MTA; X-ray; 2.40 A; L=64-188.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

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

ModBase

P22619.

Protein-protein interaction databases

DIP

DIP:6254N; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3910; -.

Ontologies

GO:0030288;	Cellular component: outer membrane-bounded periplasmic space (inferred from electronic annotation from InterPro).
GO:0030058;	Molecular function: amine dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0009308;	Biological process: cellular amine metabolic process (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR016008; Amine_DHase_bsu.
IPR004229; MeN_DHase_Ltc.
IPR013504; MeN_DHase_Ltc_C.
IPR006311; Tat.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.30.10; MADH_Lt_C; 1.

Pfam

PF02975; Me-amine-dh_L; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000192; Amine_dh_beta; 1.

TIGRFAMs

TIGR01409; TAT_signal_seq; 1.
TIGR02659; TTQ_MADH_Lt; 1.

PROSITE

PS51318; TAT; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Other

P22619; -.

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 57`	`57`	`Tat-type signal (Potential).`
`CHAIN`	`58 188`	`131`	`Methylamine dehydrogenase light chain.`	`PRO_0000025575`
`MOD_RES`	`114 114`		`Tryptophylquinone.`
`DISULFID`	`80 145`
`DISULFID`	`86 118`
`DISULFID`	`93 178`
`DISULFID`	`95 143`
`DISULFID`	`103 134`
`DISULFID`	`135 166`
`CROSSLNK`	`114 165`		`Tryptophan tryptophylquinone (Trp-Trp).`
`STRAND`	`73 75`	`3`
`HELIX`	`83 85`	`3`
`STRAND`	`89 92`	`4`
`HELIX`	`93 96`	`4`
`STRAND`	`100 103`	`4`
`STRAND`	`114 120`	`7`
`TURN`	`121 124`	`4`
`STRAND`	`125 137`	`13`
`STRAND`	`142 146`	`5`
`HELIX`	`157 159`	`3`
`STRAND`	`161 163`	`3`
`HELIX`	`170 172`	`3`
`STRAND`	`175 180`	`6`
`STRAND`	`183 187`	`5`

Sequence information

Length: 188 AA [This is the length of the unprocessed precursor]

Molecular weight: 20393 Da [This is the MW of the unprocessed precursor]

CRC64: E3D9DE4454268BE8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLGNFRFDDM VEKLSRRVAG QTSRRSVIGK LGTAMLGIGL VPLLPVDRRG RVSRANAADA 

        70         80         90        100        110        120 
PAGTDPRAKW VPQDNDIQAC DYWRHCSIDG NICDCSGGSL TNCPPGTKLA TASWVASCYN 

       130        140        150        160        170        180 
PTDGQSYLIA YRDCCGYNVS GRCPCLNTEG ELPVYRPEFA NDIIWCFGAE DDAMTYHCTI 


SPIVGKAS

P22619 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