ID A0A0D1CA24_USTMA Unreviewed; 722 AA.
AC A0A0D1CA24;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 ORFNames=UMAG_06273 {ECO:0000313|EMBL:KIS70182.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS70182.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS70182.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003143; KIS70182.1; -; Genomic_DNA.
DR RefSeq; XP_011388283.1; XM_011389981.1.
DR AlphaFoldDB; A0A0D1CA24; -.
DR STRING; 237631.A0A0D1CA24; -.
DR EnsemblFungi; KIS70182; KIS70182; UMAG_06273.
DR GeneID; 23565916; -.
DR KEGG; uma:UMAG_06273; -.
DR VEuPathDB; FungiDB:UMAG_06273; -.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; A0A0D1CA24; -.
DR OMA; QKRYQRD; -.
DR OrthoDB; 2786000at2759; -.
DR Proteomes; UP000000561; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
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 Coiled coil {ECO:0000256|SAM:Coils};
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}; Lipid metabolism {ECO:0000256|HAMAP-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}; Reference proteome {ECO:0000313|Proteomes:UP000000561};
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 64..214
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 267..531
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT COILED 693..720
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 70..75
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 121..124
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 163..172
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 198
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 288
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 453..456
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 471..473
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 477
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 488..491
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 562
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 637..638
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 647..651
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 721
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
SQ SEQUENCE 722 AA; 80136 MW; CB073758706A8293 CRC64;
MASQLDLFVL GLGGLLAVLY LFRDSLFGGA KDTGSKLANG APLAATDQGG ADFVSKLKSQ
NKRIAIFYGS QTGTAEEYAT KLAKEAKARF GTSSLVLDPE EYEFDKLDQM PQDTVAVFVM
ATYGEGEPTD NAVGLMEFIE NESPEFSNGS ERLENLNYVI FGLGNRTYEH FNAVARKLDA
RLQSLGAKRI GERGEGDDDK SMEEDYLAWK DSMFEALATS LNFEEGGGGD VPDFKVTELA
NHPDDKVYHG ELSARALLGT KGIHDAKNPY NAVVKEAREL FVQGTADRTC VHIEFDIDGS
GISYQHGDHI AVWAHNPEPE VDRVLAVFGL LDKRTTVIDV ESLDPTLAKV PFPVPTTYEA
VFRHYIDITS HASRQTLNSF AKFAPSPDIQ AKLEKVCANK DIFQAEIGSR LLKTTEAMQW
IAGDDLQADV SSIKPWNVPF DRVISDLPRV GPRFYSISSS PKMHPKSVHI TAVVLRYQAN
KSAPWVHGLA TNLISSIKMA KNGEQPTGPS DPRYGTPKYL LDGPRGAYTK DGAFRAPIHI
RRSNFRLPTS PKIPVIMVGP GTGVAPFRSF VQDRVCSAEK ALEKSNGKSA QEALKDWGNL
WLFYGCRKAD EDFLYRDEWP QYAQKLGGKF IMETSLSREK FKPDGSKLYV QDLIWERRKQ
IAEDILERKA YIYICGEAKG MAHDVEAIFG KILEEAKGSA EEAKKEIKLL KERSRLLLDV
WS
//
