NCPR2_ORYSJ
ID NCPR2_ORYSJ Reviewed; 719 AA.
AC Q0J705; A0A0P0XE14; Q6Z0U4;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=NADPH--cytochrome P450 reductase 2 {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000303|PubMed:23053415};
DE Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212};
DE Short=OsCPR2 {ECO:0000303|PubMed:23053415};
DE Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212};
DE EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:23053415};
GN Name=CPR2 {ECO:0000303|PubMed:23053415};
GN OrderedLocusNames=Os08g0243500 {ECO:0000312|EMBL:BAT04511.1},
GN LOC_Os08g14570 {ECO:0000305};
GN ORFNames=OSJNBb0070J06.25 {ECO:0000312|EMBL:BAD05639.1},
GN P0437G01.10 {ECO:0000312|EMBL:BAD05443.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-719.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23053415; DOI=10.1007/s00449-012-0787-0;
RA Park S., Kim Y.S., Rupasinghe S.G., Schuler M.A., Back K.;
RT "Rice P450 reductases differentially affect P450-mediated metabolism in
RT bacterial expression systems.";
RL Bioprocess Biosyst. Eng. 36:325-331(2013).
CC -!- FUNCTION: This enzyme is required for electron transfer from NADP to
CC cytochrome P450 in microsomes (By similarity) (PubMed:23053415). It can
CC also provide electron transfer to heme oxygenase and cytochrome B5 (By
CC similarity). Can reduce cytochrome c in vitro (PubMed:23053415).
CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:23053415}.
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:0000255|HAMAP-
CC Rule:MF_03212, ECO:0000269|PubMed:23053415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24041;
CC Evidence={ECO:0000269|PubMed:23053415};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212};
CC Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212};
CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 uM for cytochrome c {ECO:0000269|PubMed:23053415};
CC Vmax=6.47 umol/min/mg enzyme with cytochrome c as substrate
CC {ECO:0000269|PubMed:23053415};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:23053415}; Single-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic
CC side {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- INDUCTION: Induced by methyl viologen, acifluorfen and cadmium.
CC {ECO:0000269|PubMed:23053415}.
CC -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_03212}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000255|HAMAP-Rule:MF_03212}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD05443.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD05639.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF23260.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAT04511.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP004690; BAD05443.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP005478; BAD05639.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008214; BAF23260.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014964; BAT04511.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK099083; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015650780.1; XM_015795294.1.
DR AlphaFoldDB; Q0J705; -.
DR SMR; Q0J705; -.
DR STRING; 4530.OS08T0243500-01; -.
DR PaxDb; Q0J705; -.
DR PRIDE; Q0J705; -.
DR EnsemblPlants; Os08t0243500-01; Os08t0243500-01; Os08g0243500.
DR GeneID; 4345047; -.
DR Gramene; Os08t0243500-01; Os08t0243500-01; Os08g0243500.
DR KEGG; osa:4345047; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_17_3_1; -.
DR InParanoid; Q0J705; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; Q0J705; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 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 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; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..719
FT /note="NADPH--cytochrome P450 reductase 2"
FT /id="PRO_0000451429"
FT TOPO_DOM 1..42
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TOPO_DOM 64..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 111..261
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 316..564
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 117..122
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 172..175
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 210..219
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 245
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 336
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 497..500
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 515..517
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 531..534
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 578
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 639..640
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 645..649
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 681
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 719
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
SQ SEQUENCE 719 AA; 78690 MW; FD603292099877A7 CRC64;
MESSAGPMEL VAALLRGLTP RAEQLLQLSS GGGEAAAGGA AEARAAVATV AAALLGCAFL
VLWRRVSAGR KRKREEAERS AAAVAGVGKG GKNASAAAGE EAGGADGRKR VTVFFGTQTG
TAEGFAKALA EEAKSRYDKA IFKVVDLDEY AMEDEEYEER LKKEKISLFF VATYGDGEPT
DNAARFYKWF TEGNERGVWL NDFQYAIFGL GNRQYEHFNK VAKVVDELLV EQGGKRLVPV
GLGDDDQCIE DDFNAWKETL WPELDQLLRD ENDVSTGTTY TAAIPEYRVE FVKPDEAAHL
ERNFSLANGY AVHDAQHPCR ANVAVRRELH TPASDRSCTH LEFDIAGTGL TYETGDHVGV
YTENCLEVVE EAERLLGYSP EAFFTIHADK EDGTPLGGGS LAPPFPSPIT VRNALARYAD
LLNSPKKSAL VALATYASDS TEADRLRFLA SPAGKDEYAQ WVVASQRSLL EVMAEFPSAK
PPLGVFFAAV APRLQPRYYS ISSSPSMAPT RIHVTCALVH EKTPAGRVHK GVCSTWIKNA
IPSEETKDCS WAPVFVRQSN FKLPADPSVP VIMIGPGTGL APFRGFLQER LSQKQSGAEL
GRSVFFFGCR NSKMDFIYED ELNTFLEEGA LSELVLAFSR EGPTKEYVQH KMSQKASEIW
DMISQGGYIY VCGDAKGMAR DVHRVLHTIV QEQGSLDSSK AESFVKSLQT EGRYLRDVW
