DHTM_METME
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 03-AUG-2022, entry version 123.
DE RecName: Full=Trimethylamine dehydrogenase;
DE Short=TMADh;
DE EC=1.5.8.2;
GN Name=tmd;
OS Methylophilus methylotrophus (Bacterium W3A1).
OC Bacteria; Proteobacteria; 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}.
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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.KB905144_gene2344; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR BioCyc; MetaCyc:MON-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; -; 1.
DR Gene3D; 3.50.50.60; -; 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 Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 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
