[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1765062 [NCBI, ExPASy, EBI, Israel, Japan] Ubbink M., van Kleef M.A., Kleinjan D.J., Hoitink C.W., Huitema F., Beintema J.J., Duine J.A., Canters G.W.; "Cloning, sequencing and expression studies of the genes encoding amicyanin and the beta-subunit of methylamine dehydrogenase from Thiobacillus versutus."; Eur. J. Biochem. 202:1003-1012(1991).
[2]	PROTEIN SEQUENCE OF 58-188, AND 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]	PROTEIN SEQUENCE OF 58-66. DOI=10.1016/0014-5793(93)80402-G; PubMed=7901050 [NCBI, ExPASy, EBI, Israel, Japan] Van Beeumen J., Van Driessche G., Huitema F., Duine J.A., Canters G.W.; "N-terminal heterogeneity of methylamine dehydrogenase from Thiobacillus versutus."; FEBS Lett. 333:188-192(1993).
[4]	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.
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

M58001; AAA50570.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S19731; S19731.

3D structure databases

PDB

1MAE; X-ray; 2.80 A; L=64-187.	[ExPASy / RCSB / EBI]
1MAF; X-ray; 2.60 A; L=64-187.	[ExPASy / RCSB / EBI]
2MAD; X-ray; 2.25 A; L=64-187.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

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

ModBase

P22641.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-3902; -.

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

P22641; -.

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

Keywords

3D-structure; 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`	`58 188`	`131`	`Methylamine dehydrogenase light chain.`	`PRO_0000025576`
`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).`
`CONFLICT`	`89 89`		`D -> A (in Ref. 2; AA sequence).`
`CONFLICT`	`97 97`		`G -> A (in Ref. 2; AA sequence).`
`CONFLICT`	`102 102`		`N -> S (in Ref. 2; AA sequence).`
`CONFLICT`	`108 112`		`KLATA -> LVASG (in Ref. 2; AA sequence).`
`CONFLICT`	`116 116`		`A -> G (in Ref. 2; AA sequence).`
`CONFLICT`	`122 129`		`TDGQSYLI -> PDPNKYIT (in Ref. 2; AA sequence).`
`CONFLICT`	`144 144`		`P -> A (in Ref. 2; AA sequence).`
`CONFLICT`	`156 159`		`RPEF -> NKD (in Ref. 2; AA sequence).`
`CONFLICT`	`169 169`		`A -> G (in Ref. 2; AA sequence).`
`CONFLICT`	`172 173`		`DA -> G (in Ref. 2; AA sequence).`
`CONFLICT`	`179 179`		`T -> S (in Ref. 2; AA sequence).`
`CONFLICT`	`183 188`		`IVGKAS -> VSGA (in Ref. 2; AA sequence).`
`STRAND`	`73 75`	`3`
`HELIX`	`83 87`	`5`
`STRAND`	`89 92`	`4`
`HELIX`	`93 96`	`4`
`STRAND`	`100 102`	`3`
`STRAND`	`114 119`	`6`
`TURN`	`121 123`	`3`
`STRAND`	`126 131`	`6`
`STRAND`	`133 137`	`5`
`STRAND`	`142 146`	`5`
`HELIX`	`157 159`	`3`
`STRAND`	`161 163`	`3`
`HELIX`	`170 172`	`3`
`STRAND`	`175 179`	`5`
`STRAND`	`183 186`	`4`

Sequence information

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

Molecular weight: 20358 Da [This is the MW of the unprocessed precursor]

CRC64: 923C5461737C63FA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLGNFRFDDM VEKLSRRVAG RTSRRGAIGR LGTVLAGAAL VPLLPVDRRG RVSRANAAGP 

        70         80         90        100        110        120 
AEGVDPRAKW QPQDNDIQAC DYWRHCSIDG NICDCSGGSL TNCPPGTKLA TASWVASCYN 

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


SPIVGKAS

P22641 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