[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=AM1 / NCIMB 9133; PubMed=1653226 [NCBI, ExPASy, EBI, Israel, Japan] Chistoserdov A.Y., Tsygankov Y.D., Lidstrom M.E.; "Genetic organization of methylamine utilization genes from Methylobacterium extorquens AM1."; J. Bacteriol. 173:5901-5908(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=AM1 / NCIMB 9133; PubMed=8021187 [NCBI, ExPASy, EBI, Israel, Japan] Chistoserdov A.Y., Chistoserdova L.V., McIntire W.S., Lidstrom M.E.; "Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants."; J. Bacteriol. 176:4052-4065(1994).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-186. STRAIN=AM1 / NCIMB 9133; DOI=10.1016/S0006-291X(05)80195-0; PubMed=2121141 [NCBI, ExPASy, EBI, Israel, Japan] Chistoserdov A.Y., Tsygankov Y.D., Lidstrom M.E.; "Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: evidence for two tryptophan residues involved in the active center."; Biochem. Biophys. Res. Commun. 172:211-216(1990).
[4]	PROTEIN SEQUENCE OF 58-186. STRAIN=AM1 / NCIMB 9133; PubMed=6841324 [NCBI, ExPASy, EBI, Israel, Japan] Ishii Y., Hase T., Fukumori Y., Matsubara H., Tobari J.; "Amino acid sequence studies of the light subunit of methylamine dehydrogenase from Pseudomonas AM1: existence of two residues binding the prosthetic group."; J. Biochem. 93:107-119(1983).
[5]	PRESENCE OF UNUSUAL LEADER SEQUENCE. STRAIN=AM1 / NCIMB 9133; PubMed=1885555 [NCBI, ExPASy, EBI, Israel, Japan] Chistoserdov A.Y., Lidstrom M.E.; "The small-subunit polypeptide of methylamine dehydrogenase from Methylobacterium extorquens AM1 has an unusual leader sequence."; J. Bacteriol. 173:5909-5913(1991).
[6]	CHARACTERIZATION OF COFACTOR. PubMed=2028257 [NCBI, ExPASy, EBI, Israel, Japan] McIntire W.S., Wemmer D.E., Chistoserdov A.Y., Lidstrom M.E.; "A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase."; Science 252:817-824(1991).

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 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

M57963; AAA68894.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L26406; AAB46936.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M58517; AAA25379.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A36676; DEPSNL.

3D structure databases

HSSP

P22619; 2BBK. [HSSP ENTRY / PDB]

SMR

P00372; 63-186.

ModBase

P00372.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3906; -.

Ontologies

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; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Direct protein sequencing; Electron transport; Oxidoreductase; Periplasm; Signal; Transport; TTQ.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 57`	`57`	`Tat-type signal.`
`CHAIN`	`58 186`	`129`	`Methylamine dehydrogenase light chain.`	`PRO_0000025572`
`MOD_RES`	`112 112`		`Tryptophylquinone.`
`DISULFID`	`78 143`		`By similarity.`
`DISULFID`	`84 116`		`By similarity.`
`DISULFID`	`91 176`		`By similarity.`
`DISULFID`	`93 141`		`By similarity.`
`DISULFID`	`101 132`		`By similarity.`
`DISULFID`	`133 164`		`By similarity.`
`CROSSLNK`	`112 163`		`Tryptophan tryptophylquinone (Trp-Trp).`
`VARIANT`	`106 106`	`1`	`K -> L.`
`CONFLICT`	`74 74`		`D -> N (in Ref. 4; AA sequence).`

Sequence information

Length: 186 AA [This is the length of the unprocessed precursor]

Molecular weight: 20085 Da [This is the MW of the unprocessed precursor]

CRC64: 4F8504FEFF0331D9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLGKSQFDDL FEKMSRKVAG HTSRRGFIGR VGTAVAGVAL VPLLPVDRRG RVSRANAAES 

        70         80         90        100        110        120 
AGDPRGKWKP QDNDVQSCDY WRHCSIDGNI CDCSGGSLTS CPPGTKLASS SWVASCYNPT 

       130        140        150        160        170        180 
DKQSYLISYR DCCGANVSGR CACLNTEGEL PVYRPEFGND IIWCFGAEDD AMTYHCTISP 


IVGKAS

P00372 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