ID C3JWB8_RHOER Unreviewed; 705 AA.
AC C3JWB8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EEN84253.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:EEN84253.1};
GN ORFNames=RHOER0001_3415 {ECO:0000313|EMBL:EEN84253.1};
OS Rhodococcus erythropolis SK121.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN84253.1, ECO:0000313|Proteomes:UP000005836};
RN [1] {ECO:0000313|EMBL:EEN84253.1, ECO:0000313|Proteomes:UP000005836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK121 {ECO:0000313|EMBL:EEN84253.1,
RC ECO:0000313|Proteomes:UP000005836};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEN84253.1}.
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DR EMBL; ACNO01000109; EEN84253.1; -; Genomic_DNA.
DR RefSeq; WP_003946035.1; NZ_ACNO01000109.1.
DR AlphaFoldDB; C3JWB8; -.
DR Proteomes; UP000005836; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02803; OYE_like_FMN_family; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:EEN84253.1}.
FT DOMAIN 11..364
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 410..669
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 705 AA; 75151 MW; 75B73E07AA982101 CRC64;
MTIRSQTFPH LLAPGTIGPM TVPNRVVLPA MDMNLCEDGE IEKGDIDHFV ARAAGGTGLI
ITGCCAVAYP LGCTSRKEPG LSEDRFIPGL KALADAVHDA GSKLCVQMTH HGKVARIDTL
DGRPQLVPST PKPPGDMSAM ADCTPEELGK MAAINEGKRA TYHEATKEDL DWLVRMFAEA
AGRVKAAGGD AVEIHCAHNY VLGAFLSRYT NQRSDEYGGS MENRARLACE VIRAVKEEVG
GALAVIVRLA GQEYGETDGL TVDEAAAAAK MFEEAGADAI HVTGTALNAF ANFTDGPLPD
KVGYYTDNAT RIKQAISIPV ITVGRMLPEV GEKMIAEGRT DFAAMGRQLL ADPQLVNKLK
DGVPERVRPC INCYVCVQEN FWDETPLCAV NPALGNEALL PFVRTSTPKH IVVVGAGPGG
LETARVSAER GHRVTVLDKS DRLGGTLWFS SLTTPDNGRL LSWLKVEIER LGVDVRLKTE
ASVASIRALN PDAVVVATGA VRERPSVPGG DLPHVHTGDS LRALMTGAGD VSQVPPFLRT
MAKLGKLSGI TKSPAAIRAV TRKFLPMGKD VVVIGGSLVG LELAEFLAER GRTVTLIEEG
QQLGIPMAMP RRWTAVRHAK HVGVNIHRNS TVQRITKEHV EFRSGDKTLT APADMVVVAS
GVSAQAPLAD SLIGVVSDVH VVGDAVNVDY IEGAMHTAWK VAMDL
//
