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P16099 (DHTM_METME) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trimethylamine dehydrogenase

Short name=TMADh
EC=1.5.8.2
Gene names
Name:tmd
OrganismMethylophilus methylotrophus (Bacterium W3A1)
Taxonomic identifier17 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylophilus

Protein attributes

Sequence length730 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Trimethylamine + H2O + electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein.

Cofactor

Binds 1 FMN covalently per subunit.

Binds 1 4Fe-4S cluster per subunit.

Subunit structure

Homodimer.

Sequence similarities

In the N-terminal section; belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 730729Trimethylamine dehydrogenase
PRO_0000194472

Regions

Nucleotide binding392 – 42130ADP By similarity
Region170 – 1734Substrate-binding By similarity

Sites

Active site1751Proton donor By similarity
Metal binding3461Iron-sulfur (4Fe-4S)
Metal binding3491Iron-sulfur (4Fe-4S)
Metal binding3521Iron-sulfur (4Fe-4S)
Metal binding3651Iron-sulfur (4Fe-4S)
Binding site1041FMN
Binding site2231FMN
Binding site2681FMN
Binding site3231FMN

Amino acid modifications

Modified residue311S-6-FMN cysteine

Secondary structure

.................................................................................................................................... 730
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16099 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E5D5D1A91E2667EF

FASTA73081,629
        10         20         30         40         50         60 
MARDPKHDIL FEPIQIGPKT LRNRFYQVPH CIGAGSDKPG FQSAHRSVKA EGGWAALNTE 

        70         80         90        100        110        120 
YCSINPESDD THRLSARIWD EGDVRNLKAM TDEVHKYGAL AGVELWYGGA HAPNMESRAT 

       130        140        150        160        170        180 
PRGPSQYASE FETLSYCKEM DLSDIAQVQQ FYVDAAKRSR DAGFDIVYVY GAHSYLPLQF 

       190        200        210        220        230        240 
LNPYYNKRTD KYGGSLENRA RFWLETLEKV KHAVGSDCAI ATRFGVDTVY GPGQIEAEVD 

       250        260        270        280        290        300 
GQKFVEMADS LVDMWDITIG DIAEWGEDAG PSRFYQQGHT IPWVKLVKQV SKKPVLGVGR 

       310        320        330        340        350        360 
YTDPEKMIEI VTKGYADIIG CARPSIADPF LPQKVEQGRY DDIRVCIGCN VCISRWEIGG 

       370        380        390        400        410        420 
PPMICTQNAT AGEEYRRGWH PEKFRQTKNK DSVLIVGAGP SGSEAARVLM ESGYTVHLTD 

       430        440        450        460        470        480 
TAEKIGGHLN QVAALPGLGE WSYHRDYRET QITKLLKKNK ESQLALGQKP MTADDVLQYG 

       490        500        510        520        530        540 
ADKVIIATGA RWNTDGTNCL THDPIPGADA SLPDQLTPEQ VMDGKKKIGK RVVILNADTY 

       550        560        570        580        590        600 
FMAPSLAEKL ATAGHEVTIV SGVHLANYMH FTLEYPNMMR RLHELHVEEL GDHFCSRIEP 

       610        620        630        640        650        660 
GRMEIYNIWG DGSKRTYRGP GVSPRDANTS HRWIEFDSLV LVTGRHSECT LWNELKARES 

       670        680        690        700        710        720 
EWAENDIKGI YLIGDAEAPR LIADATFTGH RVAREIEEAN PQIAIPYKRE TIAWGTPHMP 

       730 
GGNFKIEYKV 

« Hide

References

[1]"Trimethylamine dehydrogenase of bacterium W3A1. Molecular cloning, sequence determination and over-expression of the gene."
Boyd G., Mathews F.S., Packman L.C., Scrutton N.S.
FEBS Lett. 308:271-276(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Amino acid sequence of a cofactor peptide from trimethylamine dehydrogenase."
Kenney W.C., McIntire W., Steenkamp D.J., Benisek W.F.
FEBS Lett. 85:137-140(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-43.
[3]"Correlation of X-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase."
Barber M.J., Neame P.J., Lim L.W., White S., Mathews F.S.
J. Biol. Chem. 267:6611-6619(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), PARTIAL PROTEIN SEQUENCE.
[4]"Extensive conformational sampling in a ternary electron transfer complex."
Leys D., Basran J., Talfournier F., Sutcliffe M.J., Scrutton N.S.
Nat. Struct. Biol. 10:219-225(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ETF.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68079 Genomic DNA. Translation: CAA48212.1.
PIRS24124.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJNX-ray2.20A/B2-729[»]
1DJQX-ray2.20A/B2-729[»]
1O94X-ray2.00A/B2-730[»]
1O95X-ray3.70A/B2-730[»]
2TMDX-ray2.40A/B2-730[»]
ProteinModelPortalP16099.
SMRP16099. Positions 2-730.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13313.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.40.50.720. 2 hits.
InterProIPR013785. Aldolase_TIM.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR016040. NAD(P)-bd_dom.
IPR001155. OxRdtase_FMN_N.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
[Graphical view]
PfamPF00724. Oxidored_FMN. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProtoNetSearch...

Other

EvolutionaryTraceP16099.

Entry information

Entry nameDHTM_METME
AccessionPrimary (citable) accession number: P16099
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references