[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8021188 [NCBI, ExPASy, EBI, Israel, Japan] Chistoserdov A.Y., McIntire W.S., Mathews F.S., Lidstrom M.E.; "Organization of the methylamine utilization (mau) genes in Methylophilus methylotrophus W3A1-NS."; J. Bacteriol. 176:4073-4080(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 (By similarity).
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

L26407; AAB46951.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T10073; T10073.

3D structure databases

HSSP

P22619; 2BBK. [HSSP ENTRY / PDB]

SMR

Q59543; 66-187.

ModBase

Q59543.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3908; -.

Family and domain databases

InterPro

IPR016008; Amine_DHase_bsu.
IPR004229; MeN_DHase_Ltc.
IPR013504; MeN_DHase_Ltc_C.
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

TIGR02659; TTQ_MADH_Lt; 1.

PROSITE

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

Other

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

Keywords

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`	`58 187`	`130`	`Methylamine dehydrogenase light chain.`	`PRO_0000025574`
`MOD_RES`	`113 113`		`Tryptophylquinone (By similarity).`
`DISULFID`	`79 144`		`By similarity.`
`DISULFID`	`85 117`		`By similarity.`
`DISULFID`	`92 177`		`By similarity.`
`DISULFID`	`94 142`		`By similarity.`
`DISULFID`	`102 133`		`By similarity.`
`DISULFID`	`134 165`		`By similarity.`
`CROSSLNK`	`113 164`		`Tryptophan tryptophylquinone (Trp-Trp) (By similarity).`

Sequence information

Length: 187 AA [This is the length of the unprocessed precursor]

Molecular weight: 20237 Da [This is the MW of the unprocessed precursor]

CRC64: E33FEBAE30CC5CED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKDTGFDSK IEKLARTTAS KTGRRGFIGR LGGFLVGSAL LPLLPVDRRS RLGGEVQAAT 

        70         80         90        100        110        120 
TGNLTRSGFK PQDKDPKACE YWRHCTIDGN LCDCCGGTLT SCPPGSSLSP SSWVASCYNP 

       130        140        150        160        170        180 
GDQQTYLIAY RDCCGKQTCG RCNCVNTQGE LPVYRPEFNN DIVWCFGADN DAMTYHCTIS 


PIVGKAS

Q59543 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