ID   DHDM_HYPSX              Reviewed;         736 AA.
AC   Q48303;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Dimethylamine dehydrogenase;
DE            Short=DMADh;
DE            EC=1.5.8.1;
GN   Name=dmd;
OS   Hyphomicrobium sp. (strain x).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium; unclassified Hyphomicrobium.
OX   NCBI_TaxID=79673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7556160; DOI=10.1111/j.1432-1033.1995.tb20808.x;
RA   Yang C.C., Packman L.C., Scrutton N.S.;
RT   "The primary structure of Hyphomicrobium X dimethylamine dehydrogenase.
RT   Relationship to trimethylamine dehydrogenase and implications for substrate
RT   recognition.";
RL   Eur. J. Biochem. 232:264-271(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylamine + H(+) + H2O + oxidized [electron-transfer
CC         flavoprotein] = formaldehyde + methylamine + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:10204, 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:59338; EC=1.5.8.1;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC       Note=Binds 1 FMN covalently per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
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; X89575; CAA61752.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q48303; -.
DR   SMR; Q48303; -.
DR   BioCyc; MetaCyc:MON-16115; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0047133; F:dimethylamine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   4Fe-4S; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..736
FT                   /note="Dimethylamine dehydrogenase"
FT                   /id="PRO_0000194471"
FT   ACT_SITE        181
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         176..179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         352
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         355
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         371
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         398..427
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         31
FT                   /note="S-6-FMN cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   736 AA;  82655 MW;  A3EE943F5617851B CRC64;
     MARDPRFDIL FTPLKLGSKT IRNRFYQVPH CNGAGTNSPG MNMAHRGIKA EGGWGAVNTE
     QCSIHPECDD TLRITARIWD QGDMRNLRAM VDHVHSHGSL AGCELFYGGP HAPAIESRTI
     SRGPSQYNSE FATVPGCPGF TYNHEADIDE LERLQQQYVD AALRARDTGF DLVNVYGAHA
     YGPMQWLNPY YNRRTDKYGG SFDNRARFWI ETLEKIRRAV NDDVALVTRC ATDTLYGTKG
     VELTEDGLRF IELASPYLDL WDVNIGDIAE WGEDAGPSRF YPIAHENDWI RHIKQATNKP
     VVGVGRYYDP EKMLQVIKAG IIDIIGAARP SIADPWLPRK IDEGRVDDIR TCIGCNVCIS
     RWEMGGVPFI CTQNATAGEE YRRGWHPEKF EPKKSDHDVL IVGAGPAGSE CARVLMERGY
     TVHLVDTREK TGGYVNDVAT LPGLGEWSFH RDYRQTQLEK LLKKNPECQI ALKQKPMTAD
     DILQYGASRV VIATGAKWST TGVNHRTHEP IPGADASLPH VLTPEQVYEG KKAVGKRVMI
     INYDAYYTAP SLAEKFARAG HDVTVATVCG LGAYMEYTLE GANMQRLIHE LGIKVLGETG
     CSRVEQGRVE LFNIWGEGYK RSYKGAGQLP RNENTSHEWH ECDTVILVTS RRSEDTLYRE
     LKARKGEWEA NGITNVFVIG DAESPRIIAD ATFDGHRLAR EIEDADPQHQ KPYKREQRAW
     GTAYNPDENP DLVWRV