P00372 (DHML_METEA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylamine dehydrogenase light chain
Short name=MADH
EC=1.4.9.1

Alternative name(s):
Methylamine dehydrogenase (amicyanin)

Gene names

Name:	mauA
Ordered Locus Names:	MexAM1_META1p2773

Organism

Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) [Complete proteome] [HAMAP]

Taxonomic identifier

272630 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium

Protein attributes

Sequence length	186 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.
Catalytic activity	Methylamine + H2O + amicyanin = formaldehyde + ammonia + reduced amicyanin.
Cofactor	Contains 1 tryptophan tryptophylquinone per subunit. Ref.7
Pathway	One-carbon metabolism; methylamine degradation; formaldehyde from methylamine: step 1/1.
Subunit structure	Heterotetramer of two light and two heavy chains.
Subcellular location	Periplasm.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. 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.
Sequence similarities	Belongs to the aromatic amine dehydrogenase light chain family.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Periplasm
Domain	Signal
Molecular function	Oxidoreductase
PTM	Disulfide bond TTQ
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	amine metabolic process Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro
Molecular function	amine dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 57	57	Tat-type signal Ref.5
	Chain	58 – 186	129	Methylamine dehydrogenase light chain		PRO_0000025572
Amino acid modifications
	Modified residue	112	1	Tryptophylquinone
	Disulfide bond	78 ↔ 143		By similarity
	Disulfide bond	84 ↔ 116		By similarity
	Disulfide bond	91 ↔ 176		By similarity
	Disulfide bond	93 ↔ 141		By similarity
	Disulfide bond	101 ↔ 132		By similarity
	Disulfide bond	133 ↔ 164		By similarity
	Cross-link	112 ↔ 163		Tryptophan tryptophylquinone (Trp-Trp)
Natural variations
	Natural variant	106	1	K → L.
Experimental info
	Sequence conflict	74	1	D → N AA sequence Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P00372 [UniParc]. Last modified November 1, 1997. Version 3. Checksum: 4F8504FEFF0331D9	FASTA	186	20,085
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic organization of methylamine utilization genes from Methylobacterium extorquens AM1." Chistoserdov A.Y., Tsygankov Y.D., Lidstrom M.E. J. Bacteriol. 173:5901-5908(1991) [PubMed: 1653226] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants." Chistoserdov A.Y., Chistoserdova L.V., McIntire W.S., Lidstrom M.E. J. Bacteriol. 176:4052-4065(1994) [PubMed: 8021187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources." Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E. , Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C., Lidstrom M.E. PLoS ONE 4:E5584-E5584(2009) [PubMed: 19440302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14718 / DSM 1338 / AM1.
[4]	"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." Chistoserdov A.Y., Tsygankov Y.D., Lidstrom M.E. Biochem. Biophys. Res. Commun. 172:211-216(1990) [PubMed: 2121141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-186.
[5]	"Amino acid sequence studies of the light subunit of methylamine dehydrogenase from Pseudomonas AM1: existence of two residues binding the prosthetic group." Ishii Y., Hase T., Fukumori Y., Matsubara H., Tobari J. J. Biochem. 93:107-119(1983) [PubMed: 6841324] [Abstract] Cited for: PROTEIN SEQUENCE OF 58-186.
[6]	"The small-subunit polypeptide of methylamine dehydrogenase from Methylobacterium extorquens AM1 has an unusual leader sequence." Chistoserdov A.Y., Lidstrom M.E. J. Bacteriol. 173:5909-5913(1991) [PubMed: 1885555] [Abstract] Cited for: PRESENCE OF UNUSUAL LEADER SEQUENCE.
[7]	"A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase." McIntire W.S., Wemmer D.E., Chistoserdov A.Y., Lidstrom M.E. Science 252:817-824(1991) [PubMed: 2028257] [Abstract] Cited for: CHARACTERIZATION OF COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M57963 Genomic DNA. Translation: AAA68894.1. L26406 Genomic DNA. Translation: AAB46936.1. CP001510 Genomic DNA. Translation: ACS40531.1. M58517 Genomic DNA. Translation: AAA25379.1.
PIR	DEPSNL. A36676.
RefSeq	YP_002963808.1. NC_012808.1.
3D structure databases
ProteinModelPortal	P00372.
SMR	P00372. Positions 63-185.
ModBase	Search...
Protein-protein interaction databases
STRING	P00372.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7992662.
PATRIC	22511303. VBIMetExt101010_2720.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	WRHCSID.
ProtClustDB	CLSK939019.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-3906.
Family and domain databases
InterPro	IPR016008. Amine_DH_bsu. IPR004229. MeN_DH_Ltc. IPR013504. MeN_DH_Ltc_C. IPR006311. TAT_signal. IPR019546. TAT_signal_bac_arc. [Graphical view]
Gene3D	G3DSA:2.60.30.10. MADH_Lt_C. 1 hit.
Pfam	PF02975. Me-amine-dh_L. 1 hit. [Graphical view]
PIRSF	PIRSF000192. Amine_dh_beta. 1 hit.
SUPFAM	SSF57561. MADH_Lt_C. 1 hit.
TIGRFAMs	TIGR01409. TAT_signal_seq. 1 hit. TIGR02659. TTQ_MADH_Lt. 1 hit.
PROSITE	PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHML_METEA

Accession

Primary (citable) accession number: P00372
Secondary accession number(s): C5ATK7, Q60146

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program