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   05-MAY-2009, entry version 59.
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; Rhizobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=79673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96048056; PubMed=7556160;
RX   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
RT   dehydrogenase. Relationship to trimethylamine dehydrogenase and
RT   implications for substrate recognition.";
RL   Eur. J. Biochem. 232:264-271(1995).
CC   -!- CATALYTIC ACTIVITY: Dimethylamine + H(2)O + electron-transferring
CC       flavoprotein = methylamine + formaldehyde + reduced electron-
CC       transferring flavoprotein.
CC   -!- COFACTOR: Binds 1 FMN covalently per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC       oxidoreductase/NADH oxidase family.
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DR   EMBL; X89575; CAA61752.1; -; Genomic_DNA.
DR   HSSP; P16099; 1O94.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0047133; F:dimethylamine dehydrogenase activity; IEA:EC.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
PE   3: Inferred from homology;
KW   4Fe-4S; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    736       Dimethylamine dehydrogenase.
FT                                /FTId=PRO_0000194471.
FT   NP_BIND     398    427       ADP (By similarity).
FT   REGION      176    179       Substrate-binding (By similarity).
FT   ACT_SITE    181    181       Proton donor (By similarity).
FT   METAL       352    352       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       355    355       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       358    358       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       371    371       Iron-sulfur (4Fe-4S) (By similarity).
FT   BINDING     229    229       FMN (By similarity).
FT   BINDING     329    329       FMN (By similarity).
FT   MOD_RES      31     31       S-6-FMN cysteine (By similarity).
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
//