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Database: UniProt
Entry: A0A1I0QHW3_9RHOB
LinkDB: A0A1I0QHW3_9RHOB
Original site: A0A1I0QHW3_9RHOB 
ID   A0A1I0QHW3_9RHOB        Unreviewed;       689 AA.
AC   A0A1I0QHW3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Dimethylamine/trimethylamine dehydrogenase {ECO:0000313|EMBL:SEW26663.1};
GN   ORFNames=SAMN05444851_2582 {ECO:0000313|EMBL:SEW26663.1};
OS   Aliiroseovarius sediminilitoris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Aliiroseovarius.
OX   NCBI_TaxID=1173584 {ECO:0000313|EMBL:SEW26663.1, ECO:0000313|Proteomes:UP000199650};
RN   [1] {ECO:0000313|EMBL:SEW26663.1, ECO:0000313|Proteomes:UP000199650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29439 {ECO:0000313|EMBL:SEW26663.1,
RC   ECO:0000313|Proteomes:UP000199650};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; FOJB01000001; SEW26663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0QHW3; -.
DR   STRING; 1173584.SAMN05444851_2582; -.
DR   OrthoDB; 9784632at2; -.
DR   Proteomes; UP000199650; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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; PF13450; NAD_binding_8; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199650}.
FT   DOMAIN          9..338
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
SQ   SEQUENCE   689 AA;  76640 MW;  2186B4AC9939BB6A CRC64;
     MRDKRYEVLF EPMQIGPVTA KNRFYQVPHC NGGGYRDPSA AAEMRRSKAE GGWGVIFTEQ
     TEMHHTSEIT PFIELRLWED KDIPMLRKMS ERMKEYGALA GIQLAYSGVN GPNLYTKEVP
     LAVSAQPIRT FTNDPVQARA LDKSDIRDLR RWFVNAAKRS QDAGFDLICL YGAHGFGIFQ
     HFLSRATNHR TDEYGGSLEN RSRFVNEVIA DIKDAVGDSM GITLRVSLDE TIGELGFSNA
     EVREFVEMNR NLPDLWDLAQ GTWEDCSGPS RFKEEAAQEQ LVKGIHELTD KPIVGVGRFT
     SPDVMAKMVR TGTLDFIGCA RPSIADPFLP KKIEEGRVED IRECIGCNIC ITGDMTMSIS
     RCTQNPTFME EWRKGWHPER MNAKGDSSNV LVVGAGPAGL EATRALAERG YDVALAESGT
     AIGGRVSRER LLPGLSAWGR VVDYREYQIG QKPNVETYFD SELDAESILE FGFENVCIAT
     GAKWRRDGVA RQHVIPFPTD AAMPLYSPDD LMDGAAPSGH VVIYDDDHYY MGGVMAELLI
     QKGCTVTLVT PAAYVSEWTL NTLEQHEIHR RLVGMGVVIE LNRGVMSIGK DHVETNCMFT
     DQRRAIECDG VLLVSSKLEN NSVYNDLKAR EAEWADAGIK SVKLIGDANA PGPIAWATYA
     GHRYARELDS EDIGDALPFR REITALAVD
//
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