ID A0A2C9ULL3_MANES Unreviewed; 710 AA.
AC A0A2C9ULL3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=MANES_14G154000 {ECO:0000313|EMBL:OAY31944.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY31944.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY31944.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY31944.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) 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. {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}.
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; CM004400; OAY31944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9ULL3; -.
DR STRING; 3983.A0A2C9ULL3; -.
DR EnsemblPlants; OAY31944; OAY31944; MANES_14G154000.
DR Gramene; OAY31944; OAY31944; MANES_14G154000.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000091857; Chromosome lg14.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum 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 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; 1.
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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, 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:UP000091857};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03212};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03212}.
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT DOMAIN 102..252
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 308..555
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 73..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..113
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 163..166
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 201..210
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 236
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 328
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
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 506..508
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 522..525
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 569
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 630..631
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 636..640
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 672
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 710
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
SQ SEQUENCE 710 AA; 78844 MW; 34B5DBF93A65C944 CRC64;
MQSSSSSLKV SPLDLMSAII KRNMDPSNAS SESAAEVATL FIENRDFVMI LTTSIAVLIG
CVVVLVWRRS SSPKSKSSAF EPPKPLIVKE PEPEHDDGHK KVTILFGTQT GTAEGFAKAL
AEEGKARYEK AKFKVVDLDD YAADDDEYEE KFKKESLVLF FVATYGDGEP TDNAARFYKW
FTEGKERGEW LQNLQFGVFG LGNKQYEHFN KIAKVLDEMF EQQGAKRLVP VGLGDDDQCI
EDDFAGWRES LWPELDQLLR DEDDATTVST PYTAAVLEYR VVFYDPENAP LEDKNWSNAN
GQAVHDAQHP CRSNVAVRKE LHTSASDRSC THLEFDIAGT GLTYETGDHV GVYCENLDEV
VDEALQLLAL SPDTCFSLHS DKEDGTSLGG SSLPPPFPPC SLRTALTRYA DLLSSPKKSA
LLALAAHATH PAEADRLRHL ASPAGKDEYA QWIVANQRSL LEVMVEFPTA RPPLGVFFAA
VAPRLQPRYY SISSSPRMAP SRIHVTCALV IEKTPAGRVH KGVCSTWMKN SVPLEKSHEC
SWAPIFVRQS NFKLPEDTKV PIIMIGPGTG LAPFRGFLQE RLALKEAGAE LGSSILFFGC
RNSKMDYIYE DELNNFVESG ALSELIVAFS REGPTKQYVQ HKMLEKALDI WNIISQGGYI
YVCGDAKGMA RDVHRTLHTI VQEQGSLNSS KAENMVKNLQ MSGRYLRDVW
//
