ID A0A0V1N0Q6_9BILA Unreviewed; 1304 AA.
AC A0A0V1N0Q6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|HAMAP-Rule:MF_03212};
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};
GN Name=POR {ECO:0000313|EMBL:KRZ77411.1};
GN ORFNames=T10_13418 {ECO:0000313|EMBL:KRZ77411.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ77411.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ77411.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ77411.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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};
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}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ77411.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDO01000019; KRZ77411.1; -; Genomic_DNA.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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 CDD; cd06204; CYPOR; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.630.30; -; 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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR009581; FAM20_C.
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; IPR000182; GNAT_dom.
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; PF13302; Acetyltransf_3; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF06702; Fam20C; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
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:UP000054843};
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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT DOMAIN 78..222
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 277..518
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 84..89
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 136..139
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 171..180
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 206
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 296
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 452..455
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 470..472
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 476
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 486..489
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 532
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 593..594
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 599..603
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 635
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
FT BINDING 673
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03212"
SQ SEQUENCE 1304 AA; 149580 MW; 8A7459471389B3BC CRC64;
MDEQLGSGDA GSWLSLVDWF VLGFGLLVAL AYFWQNKFES RRSQICVSFK PIIPAQTSNG
TLDTHSFVAK MKAAGKNMVV FYGSQTGTAE DLAFRLAKDA VRYGMKAIAL DPEEYDPEDL
YMLAEIPNSL AVFCMATYGE GDPTDNAREF FEYLHRSEAD LSGVNYAVFG LGNKTYEHFN
AMGKYTDKQL AKMGATRLCQ LGIGDDDGNL EEDFIVWREE FWLSVCRHFN ITNVGEDVSI
REYELSIIED CDKKGIFCGE VSRLGAYRNQ KAPYHQKNPF LATVTVNRDL HCGGDRTCRH
IEFNLTGSRL RYEAGDHLAV YPENDGELVE QFGKLFDVDL DTVFTLTNVD PDSSKRNPFP
CPCSFRTALT YYVDISTPPK TNVVKELSQY CSDENEKNFL LSMVTMEEKS RRKYSEWVIH
DHRTLLDILT ELPSCRPPLD LVLELLPRLQ PRFYSISSSP KVDPSLVSIT VIVLKYTTPI
GRPGKGVATN YLASKIAVEN KPHPQVPIYI RRSQFRLPHS PSTPVVMIGP GTGIAPFRGF
IQERAMLKQT GREVGPMILY FGCRKRKEDY LYGQELEAWL KDGTLSELHV AFSRDQPRKV
YVQHLMLERK QSIWSLLQNG AFFYVCGDAR NMARDVHSAL MQIIAEEGDM NADEAAAYFK
QLESQKRYQA DVWSTIEARS KLISIIRDMR LNRRTSVSGR LVVLIPYDKA HVARYHQWMQ
CDILRTQTGS EKLSLEDEYK MQQSWQDDDD KLTFIVVAKQ LWQESRFDDL GAMVGDVMIA
EPAWRGRGLG KEAVKMLLVY AFQHLHIERF VAKIRLDNEP SLALFQSLQF KQFCRVDVFQ
ELHMELILHP DMVNAWKQDT NYAELGYPCA QINDQMKLDD YEFLLENNLA LDPIGKTVRQ
SLLAELGPRL KHNSSRAKIR SLLSLPWTVL LQQPDCSDEV TVYDYLLEHF GDDIQNTTIW
DRYYLSMSSC RMYNSETVVD QLLNLLVTMP IQDVKNMEAG TQLKLLITFQ NNYSALFKPM
RQNRDEETNP NHFYFSDFER HNAEIAAYHL DRILKFYKAI PTVGRRINVT ADIEFNSKLS
PGLNDTFFLS PGSMQIFLPD EEMIPTDYVR SPFRRTYSRN KQLAEWQYNK NFCNEKVVRL
KPYNNGTRLL EMIDAYIFDF LIGNQDRHHF EFFNLTNNGH LGFIMNLDNG RGFGDSKKDD
FDILAPLVQC CMIRPTTLKR LLDYYFGPVS LSTALNRSMA SDPLAPVLAD KHLLAIDRRL
EAVLLQVSKC INDKEGHFDQ VVRTTYSNDL PTIAAETVLV DIQS
//
