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P00372 (DHML_METEA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) [Complete proteome] [HAMAP]
Taxonomic identifier272630 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length186 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5757Tat-type signal Ref.5
Chain58 – 186129Methylamine dehydrogenase light chain
PRO_0000025572

Amino acid modifications

Modified residue1121Tryptophylquinone
Disulfide bond78 ↔ 143 By similarity
Disulfide bond84 ↔ 116 By similarity
Disulfide bond91 ↔ 176 By similarity
Disulfide bond93 ↔ 141 By similarity
Disulfide bond101 ↔ 132 By similarity
Disulfide bond133 ↔ 164 By similarity
Cross-link112 ↔ 163Tryptophan tryptophylquinone (Trp-Trp)

Natural variations

Natural variant1061K → L.

Experimental info

Sequence conflict741D → N AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P00372 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 4F8504FEFF0331D9

FASTA18620,085
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF COFACTOR.

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.
PIRDEPSNL. A36676.
RefSeqYP_002963808.1. NC_012808.1.

3D structure databases

ProteinModelPortalP00372.
SMRP00372. Positions 63-185.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS40531; ACS40531; MexAM1_META1p2773.
GeneID7992662.
KEGGmea:Mex_1p2773.
PATRIC22511303. VBIMetExt101010_2720.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG86149.
HOGENOMHOG000217536.
KOK15228.
OMAWRHCSID.
ProtClustDBCLSK939019.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3906.
UniPathwayUPA00895; UER00870.

Family and domain databases

Gene3D2.60.30.10. 1 hit.
InterProIPR016008. Amine_DH_Ltc.
IPR013504. MADH/AADH_Ltc_C_dom.
IPR004229. MeN_DH_Ltc.
IPR006311. TAT_signal.
IPR019546. TAT_signal_bac_arc.
[Graphical view]
PfamPF02975. Me-amine-dh_L. 1 hit.
[Graphical view]
PIRSFPIRSF000192. Amine_dh_beta. 1 hit.
SUPFAMSSF57561. MADH_Lt_C. 1 hit.
TIGRFAMsTIGR01409. TAT_signal_seq. 1 hit.
TIGR02659. TTQ_MADH_Lt. 1 hit.
PROSITEPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHML_METEA
AccessionPrimary (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: April 3, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families