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Database: UniProt
Entry: A0A158CUL4_9BURK
LinkDB: A0A158CUL4_9BURK
Original site: A0A158CUL4_9BURK 
ID   A0A158CUL4_9BURK        Unreviewed;       678 AA.
AC   A0A158CUL4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=NADH:flavin oxidoreductase {ECO:0000313|EMBL:SAK85606.1};
GN   ORFNames=AWB79_05947 {ECO:0000313|EMBL:SAK85606.1};
OS   Caballeronia hypogeia.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777140 {ECO:0000313|EMBL:SAK85606.1, ECO:0000313|Proteomes:UP000054851};
RN   [1] {ECO:0000313|Proteomes:UP000054851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Oliw E.H.;
RL   Submitted (JAN-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; FCOA02000028; SAK85606.1; -; Genomic_DNA.
DR   RefSeq; WP_061170997.1; NZ_FCOA02000028.1.
DR   AlphaFoldDB; A0A158CUL4; -.
DR   STRING; 1777140.AWB79_05947; -.
DR   OrthoDB; 8985337at2; -.
DR   Proteomes; UP000054851; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd04734; OYE_like_3_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   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; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
FT   DOMAIN          6..340
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
SQ   SEQUENCE   678 AA;  75028 MW;  833C272071268D20 CRC64;
     MSTDPLLQPF TLKHLTFRNR IMTTSHEPAY AEDGMPKQQY RAYHVERAKA GIALTMTAGS
     AAVSKDSPPA FNNILAYKDE VVGWLRDLAD ECHEHGAKVM IQLTHLGRRT RWDNGDWLPV
     VSPSHKREAA HRAFPKKIED WDIDRIVRDF ADAAERMKAA GLDGLEIESY GHLMDQFWSP
     LTNTLDGPYG GSLDNRMRFT FEVYRAMRER VGDDFLLGIR YTADERLAGG ITKEEGIEIS
     KRLKDSGLID FLNVIRGHLD TDAGLTDVIP VMGMQSAPHL DFAGEIRRAT DFPTFHAARI
     QDVATARFAI ESGKVDMIGM TRAHMTDPHI VRKIIERREE DIRPCVGANY CLDRIYQGGA
     AYCIHNPATG RELSLPQTIA RAPVSKKIVI VGAGPAGLEA ARVAGERGHD VVVYEAMNDP
     GGQIRLAAQS TRRKELMGIV DWRVAQCEKL GVRFAFNAWA EKDDVLAEQP AVVIVATGGM
     PHTEVLSQGN ELVISAWDLI SGDVKPGKNV LVFDDAGDHA ALQAAEVVAQ AGGMVEIMTP
     DRIFSPEVMS MTLVPYMRAL QKLNTRFTVT YRLEAVRRED GMLVATVGSD YGGISREQRY
     DQIVVNHGTV PMDDLYFDLK PLSANTGVVD YDSLIAAPRK DVINNPEGTF QLFRIGDAVS
     ARNIHAAILD ALRLVKDV
//
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