ID A5E4M0_LODEL Unreviewed; 315 AA.
AC A5E4M0;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=NADPH-cytochrome P450 reductase {ECO:0000313|EMBL:EDK46378.1};
GN ORFNames=LELG_04559 {ECO:0000313|EMBL:EDK46378.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK46378.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK46378.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; CH981529; EDK46378.1; -; Genomic_DNA.
DR RefSeq; XP_001524587.1; XM_001524537.1.
DR AlphaFoldDB; A5E4M0; -.
DR STRING; 379508.A5E4M0; -.
DR GeneID; 5231299; -.
DR KEGG; lel:LELG_04559; -.
DR VEuPathDB; FungiDB:LELG_04559; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_882992_0_0_1; -.
DR InParanoid; A5E4M0; -.
DR OMA; FNTKERS; -.
DR OrthoDB; 2786000at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000001996};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..209
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 315 AA; 35154 MW; D2A3C2DCB967ACB3 CRC64;
MALDSLDLYV VIILTLSVAA YFAKGYFFDK PESTGFLNAD GGAGGVGGIN SRNILEVLAK
NNKNALLLFG SQTGTAEDYC NKMSKELSSR FGLHTMVADF ADYDWEKFEE IKEETLVFFL
MATYGEGEPT DNAIEFMEYL ENEADTLSSL RFTVFGLGNS TYEFYNAIGR KLNTTLEEKG
AERFAEYGEG DDGLGTLDED FLSWKDNVFD SLRNNLSLEE KELKYEPSVK VIERDDLTKD
DNSVSLGEPN KKHIAGDVDL TKGPFDHTHP YIAQITATKE LFNTKERSCV HVEFDLSDSN
LKYTTPPAFG CLATE
//