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Database: UniProt
Entry: Q6L8F1_YARLL
LinkDB: Q6L8F1_YARLL
Original site: Q6L8F1_YARLL 
ID   Q6L8F1_YARLL            Unreviewed;       722 AA.
AC   Q6L8F1; Q6CAA8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 118.
DE   RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|HAMAP-Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208};
DE            Short=CPR {ECO:0000256|HAMAP-Rule:MF_03212};
DE            Short=P450R {ECO:0000256|HAMAP-Rule:MF_03212};
DE            EC=1.6.2.4 {ECO:0000256|HAMAP-Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208};
GN   Name=YlCPR1 {ECO:0000313|EMBL:BAD20195.1};
GN   Synonyms=NCP1 {ECO:0000256|HAMAP-Rule:MF_03212};
GN   ORFNames=YALI1_D05474g {ECO:0000313|EMBL:AOW03570.1};
OS   Yarrowia lipolytica (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=4952 {ECO:0000313|EMBL:BAD20195.1};
RN   [1] {ECO:0000313|EMBL:BAD20195.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Sumita T., Iida T.;
RT   "Isolation of NADPH-cytochrome P-450 reductase gene from Yarrowia
RT   lipolytica.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOW03570.1, ECO:0000313|Proteomes:UP000182444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB89 {ECO:0000313|EMBL:AOW03570.1}, and CLIB89(W29)
RC   {ECO:0000313|Proteomes:UP000182444};
RX   PubMed=27603307;
RA   Magnan C., Yu J., Chang I., Jahn E., Kanomata Y., Wu J., Zeller M.,
RA   Oakes M., Baldi P., Sandmeyer S.;
RT   "Sequence Assembly of Yarrowia lipolytica Strain W29/CLIB89 Shows
RT   Transposable Element Diversity.";
RL   PLoS ONE 11:E0162363-E0162363(2016).
CC   -!- FUNCTION: This enzyme is required for electron transfer from NADP to
CC       cytochrome P450 in microsomes. It can also provide electron transfer to
CC       heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_03212}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC         reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC         COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03212};
CC       Note=Binds 1 FAD per monomer. {ECO:0000256|HAMAP-Rule:MF_03212};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03212};
CC       Note=Binds 1 FMN per monomer. {ECO:0000256|HAMAP-Rule:MF_03212};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|HAMAP-Rule:MF_03212}; Single-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_03212}. Mitochondrion outer membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03212}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03212}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_03212}.
CC       Cell membrane {ECO:0000256|HAMAP-Rule:MF_03212}; Single-pass membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_03212}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_03212}.
CC   -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03212}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family. {ECO:0000256|HAMAP-
CC       Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       family. {ECO:0000256|HAMAP-Rule:MF_03212}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03212}.
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DR   EMBL; CP017556; AOW03570.1; -; Genomic_DNA.
DR   EMBL; AB126598; BAD20195.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6L8F1; -.
DR   VEuPathDB; FungiDB:YALI0_D04422g; -.
DR   VEuPathDB; FungiDB:YALI1_D05474g; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   OMA; QKRYQRD; -.
DR   OrthoDB; 2786000at2759; -.
DR   Proteomes; UP000182444; Chromosome 1d.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06204; CYPOR; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_03212; NCPR; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR023208; P450R.
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   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF000208; P450R; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_03212};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW   Rule:MF_03212};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_03212};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_03212};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_03212};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_03212};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_03212};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03212};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03212};
KW   Mitochondrion outer membrane {ECO:0000256|HAMAP-Rule:MF_03212};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03212};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_03212};
KW   Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955, ECO:0000256|HAMAP-
KW   Rule:MF_03212};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221, ECO:0000256|HAMAP-
KW   Rule:MF_03212};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011, ECO:0000256|HAMAP-
KW   Rule:MF_03212};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166, ECO:0000256|HAMAP-
KW   Rule:MF_03212}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          77..235
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          303..551
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          249..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83..88
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         134..137
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         183..192
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         218
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         322
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         477..480
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         495..497
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         510..513
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         579
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         641..642
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         648..652
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         684
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT   BINDING         722
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
SQ   SEQUENCE   722 AA;  80177 MW;  4840425F619ACB7D CRC64;
     MALLDSLDFI VLVLVGVATL AFFTKGKLWA KEPETDPYAG GLGSQGFGST TSFGSFGGNS
     NKTRDITKKL EQTGKNVIIF YGSQTGTAED YANRLSKEAT QRYGLKSMTA DLEDYDYENL
     NSLGDDIVVG FVMATYGEGE PTDNAVNFYE FINDDSSEWA ESDEPSADPD SPLSSLNYVI
     FGLGNNTYEH YNEIGRNLDK RLKKLGAKRI GDYGEGDDGQ GTMEEDYLAW KDDLFSAWKE
     AKGLDEHEAK YEPSVKISET GETASSEDSS SVAEPDAEAM SVYLGEPNKK ILRGEIKGPY
     NAGNPFLANV SETRELFHDP KRSCIHVEFD VGTNVKYTTG DHLALHIQNS DEEVERFLKV
     IGLWDKRHNV IKAKPIDPTY KPSFPVPTTY DTVVRYYLEI NGAVSRQLLA FIAPFAPTET
     AKKEALRLGS DKNAFADEVA KHYTNIAHVL SKLSGGEPWT NVPFSFLVES LPHLIPRYYS
     ISSSSLVDKS KISITAVVES LEAPEYAIKG VATNLLLDMK IKKDGVDPSK SKDPQAVHYE
     LSGPRGKFGG HKLPVHIRRS NFKLPSDPKK PIIMIGPGTG LAPFRAFVME RAKQAESGTD
     VGQQLLFFGC RNPNEDFIYK EQWAGIEKEL GDKFTMVTAF SRVDPVQKVY VQHRMQEYAK
     QINDLMQQGA YFYVCGDASR MAREVQATLA KILSDQRGIP LSSAEQLVKS LKVQNVYQED
     VW
//
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