ID DHTM_METME Reviewed; 730 AA. AC P16099; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 128. DE RecName: Full=Trimethylamine dehydrogenase; DE Short=TMADh; DE EC=1.5.8.2; GN Name=tmd; OS Methylophilus methylotrophus (Bacterium W3A1). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylophilus. OX NCBI_TaxID=17; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1505666; DOI=10.1016/0014-5793(92)81291-s; RA Boyd G., Mathews F.S., Packman L.C., Scrutton N.S.; RT "Trimethylamine dehydrogenase of bacterium W3A1. Molecular cloning, RT sequence determination and over-expression of the gene."; RL FEBS Lett. 308:271-276(1992). RN [2] RP PROTEIN SEQUENCE OF 32-43. RX PubMed=620783; DOI=10.1016/0014-5793(78)81265-4; RA Kenney W.C., McIntire W., Steenkamp D.J., Benisek W.F.; RT "Amino acid sequence of a cofactor peptide from trimethylamine RT dehydrogenase."; RL FEBS Lett. 85:137-140(1978). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=1551870; DOI=10.1016/s0021-9258(19)50471-9; RA Barber M.J., Neame P.J., Lim L.W., White S., Mathews F.S.; RT "Correlation of X-ray deduced and experimental amino acid sequences of RT trimethylamine dehydrogenase."; RL J. Biol. Chem. 267:6611-6619(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ETF. RX PubMed=12567183; DOI=10.1038/nsb894; RA Leys D., Basran J., Talfournier F., Sutcliffe M.J., Scrutton N.S.; RT "Extensive conformational sampling in a ternary electron transfer RT complex."; RL Nat. Struct. Biol. 10:219-225(2003). CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + H2O + oxidized [electron-transfer flavoprotein] + CC trimethylamine = dimethylamine + formaldehyde + reduced [electron- CC transfer flavoprotein]; Xref=Rhea:RHEA:11864, Rhea:RHEA-COMP:10685, CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16842, ChEBI:CHEBI:57692, ChEBI:CHEBI:58040, CC ChEBI:CHEBI:58307, ChEBI:CHEBI:58389; EC=1.5.8.2; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Note=Binds 1 FMN covalently per subunit.; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster per subunit.; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12567183}. CC -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin CC oxidoreductase/NADH oxidase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X68079; CAA48212.1; -; Genomic_DNA. DR PIR; S24124; S24124. DR PDB; 1DJN; X-ray; 2.20 A; A/B=2-730. DR PDB; 1DJQ; X-ray; 2.20 A; A/B=2-730. DR PDB; 1O94; X-ray; 2.00 A; A/B=2-730. DR PDB; 1O95; X-ray; 3.70 A; A/B=2-730. DR PDB; 2TMD; X-ray; 2.40 A; A/B=2-730. DR PDBsum; 1DJN; -. DR PDBsum; 1DJQ; -. DR PDBsum; 1O94; -. DR PDBsum; 1O95; -. DR PDBsum; 2TMD; -. DR AlphaFoldDB; P16099; -. DR SMR; P16099; -. DR STRING; 1122236.GCA_000378225_02075; -. DR DrugBank; DB03247; Flavin mononucleotide. DR BioCyc; MetaCyc:MONOMER-13313; -. DR EvolutionaryTrace; P16099; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050470; F:trimethylamine dehydrogenase activity; IEA:UniProtKB-EC. DR CDD; cd02929; TMADH_HD_FMN; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR001155; OxRdtase_FMN_N. DR InterPro; IPR037348; TMADH/HD_FMN-bd. DR PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1. DR PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1. DR Pfam; PF00724; Oxidored_FMN; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00368; FADPNR. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. DR SUPFAM; SSF51971; Nucleotide-binding domain; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Direct protein sequencing; Flavoprotein; FMN; Iron; KW Iron-sulfur; Metal-binding; Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..730 FT /note="Trimethylamine dehydrogenase" FT /id="PRO_0000194472" FT ACT_SITE 175 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 104 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT BINDING 170..173 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 223 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT BINDING 268 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT BINDING 323 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT BINDING 346 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT BINDING 349 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT BINDING 352 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT BINDING 365 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT BINDING 392..421 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250" FT MOD_RES 31 FT /note="S-6-FMN cysteine" FT HELIX 5..11 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 19..27 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 39..51 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 55..65 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 81..95 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 100..106 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 142..161 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 165..171 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 176..181 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 183..185 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 196..199 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 201..214 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 215..217 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 218..227 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 237..239 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 240..248 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 253..259 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 265..267 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 272..274 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 277..280 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 281..284 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 285..290 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:1DJN" FT HELIX 304..312 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 317..322 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 323..327 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 331..336 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 340..342 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 351..358 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 369..373 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 374..377 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 392..396 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 400..411 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 415..419 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 421..424 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 425..428 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 429..432 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 439..442 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 443..458 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 463..465 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 473..477 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 482..486 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 490..492 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 499..501 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 518..523 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 530..536 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 542..552 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 556..563 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 567..571 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 575..584 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 588..590 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 592..599 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 602..607 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 632..635 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 637..643 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 645..647 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 650..657 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 659..661 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 663..665 FT /evidence="ECO:0007829|PDB:1O94" FT STRAND 669..672 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 674..676 FT /evidence="ECO:0007829|PDB:1O94" FT HELIX 682..694 FT /evidence="ECO:0007829|PDB:1O94" FT TURN 695..697 FT /evidence="ECO:0007829|PDB:1O94" SQ SEQUENCE 730 AA; 81629 MW; E5D5D1A91E2667EF CRC64; MARDPKHDIL FEPIQIGPKT LRNRFYQVPH CIGAGSDKPG FQSAHRSVKA EGGWAALNTE YCSINPESDD THRLSARIWD EGDVRNLKAM TDEVHKYGAL AGVELWYGGA HAPNMESRAT PRGPSQYASE FETLSYCKEM DLSDIAQVQQ FYVDAAKRSR DAGFDIVYVY GAHSYLPLQF LNPYYNKRTD KYGGSLENRA RFWLETLEKV KHAVGSDCAI ATRFGVDTVY GPGQIEAEVD GQKFVEMADS LVDMWDITIG DIAEWGEDAG PSRFYQQGHT IPWVKLVKQV SKKPVLGVGR YTDPEKMIEI VTKGYADIIG CARPSIADPF LPQKVEQGRY DDIRVCIGCN VCISRWEIGG PPMICTQNAT AGEEYRRGWH PEKFRQTKNK DSVLIVGAGP SGSEAARVLM ESGYTVHLTD TAEKIGGHLN QVAALPGLGE WSYHRDYRET QITKLLKKNK ESQLALGQKP MTADDVLQYG ADKVIIATGA RWNTDGTNCL THDPIPGADA SLPDQLTPEQ VMDGKKKIGK RVVILNADTY FMAPSLAEKL ATAGHEVTIV SGVHLANYMH FTLEYPNMMR RLHELHVEEL GDHFCSRIEP GRMEIYNIWG DGSKRTYRGP GVSPRDANTS HRWIEFDSLV LVTGRHSECT LWNELKARES EWAENDIKGI YLIGDAEAPR LIADATFTGH RVAREIEEAN PQIAIPYKRE TIAWGTPHMP GGNFKIEYKV //