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P16099

- DHTM_METME

UniProt

P16099 - DHTM_METME

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Protein
Trimethylamine dehydrogenase
Gene
tmd
Organism
Methylophilus methylotrophus (Bacterium W3A1)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 FMN covalently per subunit.
Binds 1 4Fe-4S cluster per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041FMN
Active sitei175 – 1751Proton donor By similarity
Binding sitei223 – 2231FMN
Binding sitei268 – 2681FMN
Binding sitei323 – 3231FMN
Metal bindingi346 – 3461Iron-sulfur (4Fe-4S)
Metal bindingi349 – 3491Iron-sulfur (4Fe-4S)
Metal bindingi352 – 3521Iron-sulfur (4Fe-4S)
Metal bindingi365 – 3651Iron-sulfur (4Fe-4S)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi392 – 42130ADP By similarity
Add
BLAST

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. FMN binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. trimethylamine dehydrogenase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13313.

Names & Taxonomyi

Protein namesi
Recommended name:
Trimethylamine dehydrogenase (EC:1.5.8.2)
Short name:
TMADh
Gene namesi
Name:tmd
OrganismiMethylophilus methylotrophus (Bacterium W3A1)
Taxonomic identifieri17 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylophilus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 730729Trimethylamine dehydrogenase
PRO_0000194472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311S-6-FMN cysteine

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 117
Beta strandi14 – 163
Beta strandi19 – 279
Turni35 – 373
Helixi39 – 5113
Beta strandi55 – 6511
Helixi81 – 9515
Turni96 – 983
Beta strandi100 – 1067
Helixi109 – 1113
Turni115 – 1173
Beta strandi122 – 1254
Beta strandi130 – 1323
Helixi142 – 16120
Beta strandi165 – 1717
Helixi176 – 1816
Turni183 – 1853
Beta strandi193 – 1953
Helixi196 – 1994
Helixi201 – 21414
Turni215 – 2173
Beta strandi218 – 22710
Turni237 – 2393
Helixi240 – 2489
Helixi249 – 2513
Beta strandi253 – 2597
Helixi265 – 2673
Turni272 – 2743
Turni277 – 2804
Helixi281 – 2844
Turni285 – 2906
Beta strandi295 – 2973
Helixi304 – 3129
Beta strandi317 – 3226
Helixi323 – 3275
Helixi331 – 3366
Helixi340 – 3423
Helixi351 – 3588
Beta strandi359 – 3613
Turni369 – 3735
Helixi374 – 3774
Beta strandi392 – 3965
Helixi400 – 41112
Beta strandi415 – 4195
Beta strandi421 – 4244
Turni425 – 4284
Helixi429 – 4324
Helixi439 – 4424
Helixi443 – 45816
Beta strandi463 – 4653
Helixi473 – 4775
Beta strandi482 – 4865
Beta strandi490 – 4923
Turni499 – 5013
Helixi518 – 5236
Beta strandi530 – 5367
Helixi542 – 55211
Beta strandi556 – 5638
Helixi567 – 5715
Helixi575 – 58410
Beta strandi588 – 5903
Beta strandi592 – 5998
Beta strandi602 – 6076
Beta strandi632 – 6354
Beta strandi637 – 6437
Beta strandi645 – 6473
Helixi650 – 6578
Helixi659 – 6613
Helixi663 – 6653
Beta strandi669 – 6724
Helixi674 – 6763
Helixi682 – 69413
Turni695 – 6973

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJNX-ray2.20A/B2-730[»]
1DJQX-ray2.20A/B2-730[»]
1O94X-ray2.00A/B2-730[»]
1O95X-ray3.70A/B2-730[»]
2TMDX-ray2.40A/B2-730[»]
ProteinModelPortaliP16099.
SMRiP16099. Positions 2-730.

Miscellaneous databases

EvolutionaryTraceiP16099.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni170 – 1734Substrate-binding By similarity

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.40.50.720. 2 hits.
InterProiIPR013785. 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]
PfamiPF00724. Oxidored_FMN. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16099-1 [UniParc]FASTAAdd to Basket

« Hide

MARDPKHDIL FEPIQIGPKT LRNRFYQVPH CIGAGSDKPG FQSAHRSVKA    50
EGGWAALNTE YCSINPESDD THRLSARIWD EGDVRNLKAM TDEVHKYGAL 100
AGVELWYGGA HAPNMESRAT PRGPSQYASE FETLSYCKEM DLSDIAQVQQ 150
FYVDAAKRSR DAGFDIVYVY GAHSYLPLQF LNPYYNKRTD KYGGSLENRA 200
RFWLETLEKV KHAVGSDCAI ATRFGVDTVY GPGQIEAEVD GQKFVEMADS 250
LVDMWDITIG DIAEWGEDAG PSRFYQQGHT IPWVKLVKQV SKKPVLGVGR 300
YTDPEKMIEI VTKGYADIIG CARPSIADPF LPQKVEQGRY DDIRVCIGCN 350
VCISRWEIGG PPMICTQNAT AGEEYRRGWH PEKFRQTKNK DSVLIVGAGP 400
SGSEAARVLM ESGYTVHLTD TAEKIGGHLN QVAALPGLGE WSYHRDYRET 450
QITKLLKKNK ESQLALGQKP MTADDVLQYG ADKVIIATGA RWNTDGTNCL 500
THDPIPGADA SLPDQLTPEQ VMDGKKKIGK RVVILNADTY FMAPSLAEKL 550
ATAGHEVTIV SGVHLANYMH FTLEYPNMMR RLHELHVEEL GDHFCSRIEP 600
GRMEIYNIWG DGSKRTYRGP GVSPRDANTS HRWIEFDSLV LVTGRHSECT 650
LWNELKARES EWAENDIKGI YLIGDAEAPR LIADATFTGH RVAREIEEAN 700
PQIAIPYKRE TIAWGTPHMP GGNFKIEYKV 730
Length:730
Mass (Da):81,629
Last modified:January 23, 2007 - v3
Checksum:iE5D5D1A91E2667EF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68079 Genomic DNA. Translation: CAA48212.1.
PIRiS24124.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68079 Genomic DNA. Translation: CAA48212.1 .
PIRi S24124.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DJN X-ray 2.20 A/B 2-730 [» ]
1DJQ X-ray 2.20 A/B 2-730 [» ]
1O94 X-ray 2.00 A/B 2-730 [» ]
1O95 X-ray 3.70 A/B 2-730 [» ]
2TMD X-ray 2.40 A/B 2-730 [» ]
ProteinModelPortali P16099.
SMRi P16099. Positions 2-730.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-13313.

Miscellaneous databases

EvolutionaryTracei P16099.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
3.40.50.720. 2 hits.
InterProi IPR013785. 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 ]
Pfami PF00724. Oxidored_FMN. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiDHTM_METME
AccessioniPrimary (citable) accession number: P16099
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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