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
//