[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0014-5793(92)81291-S; PubMed=1505666 [NCBI, ExPASy, EBI, Israel, Japan] Boyd G., Mathews F.S., Packman L.C., Scrutton N.S.; "Trimethylamine dehydrogenase of bacterium W3A1. Molecular cloning, sequence determination and over-expression of the gene."; FEBS Lett. 308:271-276(1992).
[2]	PROTEIN SEQUENCE OF 32-43. DOI=10.1016/0014-5793(78)81265-4; PubMed=620783 [NCBI, ExPASy, EBI, Israel, Japan] Kenney W.C., McIntire W., Steenkamp D.J., Benisek W.F.; "Amino acid sequence of a cofactor peptide from trimethylamine dehydrogenase."; FEBS Lett. 85:137-140(1978).
[3]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND PARTIAL PROTEIN SEQUENCE. PubMed=1551870 [NCBI, ExPASy, EBI, Israel, Japan] Barber M.J., Neame P.J., Lim L.W., White S., Mathews F.S.; "Correlation of X-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase."; J. Biol. Chem. 267:6611-6619(1992).
[4]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ETF. DOI=10.1038/nsb894; PubMed=12567183 [NCBI, ExPASy, EBI, Israel, Japan] Leys D., Basran J., Talfournier F., Sutcliffe M.J., Scrutton N.S.; "Extensive conformational sampling in a ternary electron transfer complex."; Nat. Struct. Biol. 10:219-225(2003).

Comments

CATALYTIC ACTIVITY: Trimethylamine + H₂O + electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein.
COFACTOR: Binds 1 FMN covalently per subunit.
COFACTOR: Binds 1 4Fe-4S cluster per subunit.
SUBUNIT: Homodimer.
SIMILARITY: In the N-terminal section; belongs to the NADH:flavin oxidoreductase/NADH oxidase 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

X68079; CAA48212.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S24124; S24124.

3D structure databases

PDB

1DJN; X-ray; 2.20 A; A/B=1-730.	[ExPASy / RCSB / EBI]
1DJQ; X-ray; 2.20 A; A/B=1-730.	[ExPASy / RCSB / EBI]
1O94; X-ray; 2.00 A; A/B=1-730.	[ExPASy / RCSB / EBI]
1O95; X-ray; 3.70 A; A/B=1-730.	[ExPASy / RCSB / EBI]
2TMD; X-ray; 2.40 A; A/B=1-730.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DJN; -.
1DJQ; -.
1O94; -.
1O95; -.
2TMD; -.

ModBase

P16099.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13313; -.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050470;	Molecular function: trimethylamine dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001155; OxRdtase_FMN_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF00724; Oxidored_FMN; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PR00368; FADPNR.

Other

P16099; -.

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

Keywords

3D-structure; 4Fe-4S; Direct protein sequencing; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 730`	`729`	`Trimethylamine dehydrogenase.`	`PRO_0000194472`
`NP_BIND`	`392 421`	`30`	`ADP (By similarity).`
`REGION`	`170 173`	`4`	`Substrate-binding (By similarity).`
`ACT_SITE`	`175 175`		`Proton donor (By similarity).`
`METAL`	`346 346`		`Iron-sulfur (4Fe-4S).`
`METAL`	`349 349`		`Iron-sulfur (4Fe-4S).`
`METAL`	`352 352`		`Iron-sulfur (4Fe-4S).`
`METAL`	`365 365`		`Iron-sulfur (4Fe-4S).`
`BINDING`	`104 104`		`FMN.`
`BINDING`	`223 223`		`FMN.`
`BINDING`	`268 268`		`FMN.`
`BINDING`	`323 323`		`FMN.`
`MOD_RES`	`31 31`		`S-6-FMN cysteine.`
`HELIX`	`5 11`	`7`
`STRAND`	`14 16`	`3`
`STRAND`	`19 27`	`9`
`TURN`	`35 37`	`3`
`HELIX`	`39 51`	`13`
`STRAND`	`55 65`	`11`
`HELIX`	`81 96`	`16`
`STRAND`	`100 106`	`7`
`HELIX`	`109 111`	`3`
`TURN`	`115 117`	`3`
`STRAND`	`122 125`	`4`
`STRAND`	`130 132`	`3`
`HELIX`	`142 162`	`21`
`STRAND`	`165 171`	`7`
`HELIX`	`176 181`	`6`
`TURN`	`183 185`	`3`
`STRAND`	`193 195`	`3`
`HELIX`	`196 214`	`19`
`TURN`	`215 217`	`3`
`STRAND`	`218 225`	`8`
`TURN`	`237 239`	`3`
`HELIX`	`240 248`	`9`
`TURN`	`249 251`	`3`
`STRAND`	`253 258`	`6`
`HELIX`	`265 267`	`3`
`TURN`	`272 274`	`3`
`TURN`	`277 280`	`4`
`HELIX`	`281 288`	`8`
`STRAND`	`295 297`	`3`
`HELIX`	`304 312`	`9`
`STRAND`	`317 322`	`6`
`HELIX`	`323 327`	`5`
`HELIX`	`331 336`	`6`
`HELIX`	`340 342`	`3`
`HELIX`	`351 358`	`8`
`STRAND`	`359 361`	`3`
`TURN`	`369 373`	`5`
`HELIX`	`374 377`	`4`
`STRAND`	`392 396`	`5`
`HELIX`	`400 411`	`12`
`STRAND`	`415 419`	`5`
`STRAND`	`421 424`	`4`
`TURN`	`425 428`	`4`
`HELIX`	`429 432`	`4`
`HELIX`	`439 442`	`4`
`HELIX`	`443 456`	`14`
`STRAND`	`463 465`	`3`
`HELIX`	`473 477`	`5`
`STRAND`	`482 486`	`5`
`STRAND`	`490 492`	`3`
`TURN`	`499 501`	`3`
`HELIX`	`518 523`	`6`
`STRAND`	`530 536`	`7`
`HELIX`	`542 552`	`11`
`STRAND`	`556 563`	`8`
`TURN`	`565 567`	`3`
`HELIX`	`568 571`	`4`
`HELIX`	`575 584`	`10`
`STRAND`	`588 590`	`3`
`STRAND`	`593 599`	`7`
`STRAND`	`602 607`	`6`
`STRAND`	`632 635`	`4`
`STRAND`	`637 643`	`7`
`STRAND`	`645 647`	`3`
`HELIX`	`650 657`	`8`
`TURN`	`658 660`	`3`
`HELIX`	`661 664`	`4`
`STRAND`	`669 672`	`4`
`HELIX`	`674 676`	`3`
`HELIX`	`682 694`	`13`
`TURN`	`695 697`	`3`

Sequence information

Length: 730 AA [This is the length of the unprocessed precursor]

Molecular weight: 81629 Da [This is the MW of the unprocessed precursor]

CRC64: E5D5D1A91E2667EF [This is a checksum on the sequence]

        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

P16099 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