UniProtKB - Q00141 (NCPR_ASPNG)
Protein
NADPH--cytochrome P450 reductase
Gene
cprA
Organism
Aspergillus niger
Status
Functioni
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.UniRule annotation
Catalytic activityi
- NADPH + 2 oxidized [cytochrome P450] = H+ + NADP+ + 2 reduced [cytochrome P450]UniRule annotation2 PublicationsEC:1.6.2.4UniRule annotation2 Publications
Cofactori
Protein has several cofactor binding sites:- FADUniRule annotation2 PublicationsNote: Binds 1 FAD per monomer.UniRule annotation
- FMNUniRule annotation2 PublicationsNote: Binds 1 FMN per monomer.UniRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 203 | FMNUniRule annotation | 1 | |
Binding sitei | 295 | NADPUniRule annotation | 1 | |
Binding sitei | 551 | NADPUniRule annotation | 1 | |
Binding sitei | 655 | NADPUniRule annotation | 1 | |
Binding sitei | 693 | FADUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 72 – 77 | FMNUniRule annotation | 6 | |
Nucleotide bindingi | 123 – 126 | FMNUniRule annotation | 4 | |
Nucleotide bindingi | 168 – 177 | FMNUniRule annotation | 10 | |
Nucleotide bindingi | 450 – 453 | FADUniRule annotation | 4 | |
Nucleotide bindingi | 468 – 470 | FADUniRule annotation | 3 | |
Nucleotide bindingi | 485 – 488 | FADUniRule annotation | 4 | |
Nucleotide bindingi | 613 – 614 | NADPUniRule annotation | 2 | |
Nucleotide bindingi | 619 – 623 | NADPUniRule annotation | 5 |
GO - Molecular functioni
- electron transfer activity Source: UniProtKB
- flavin adenine dinucleotide binding Source: UniProtKB-UniRule
- FMN binding Source: UniProtKB-UniRule
- NADP binding Source: UniProtKB-UniRule
- NADPH-hemoprotein reductase activity Source: UniProtKB-UniRule
- oxidoreductase activity Source: UniProtKB
GO - Biological processi
- ergosterol biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism |
Ligand | FAD, Flavoprotein, FMN, NADP |
Names & Taxonomyi
Protein namesi | Recommended name: NADPH--cytochrome P450 reductaseUniRule annotation (EC:1.6.2.4UniRule annotation)Short name: CPRUniRule annotation Short name: P450RUniRule annotation |
Gene namesi | Name:cprAUniRule annotation |
Organismi | Aspergillus nigerImported |
Taxonomic identifieri | 5061 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Circumdati |
Subcellular locationi
Plasma membrane
- Cell membrane UniRule annotation; Single-pass membrane protein UniRule annotation; Cytoplasmic side UniRule annotation
Endoplasmic reticulum
- Endoplasmic reticulum membrane UniRule annotation; Single-pass membrane protein UniRule annotation; Cytoplasmic side UniRule annotation
Mitochondrion
- Mitochondrion outer membrane UniRule annotation; Single-pass membrane protein UniRule annotation; Cytoplasmic side UniRule annotation
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
Mitochondrion
- mitochondrial outer membrane Source: UniProtKB-SubCell
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- integral component of membrane Source: UniProtKB-KW
- intracellular membrane-bounded organelle Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 8 | LumenalUniRule annotation | 8 | |
Transmembranei | 9 – 31 | HelicalUniRule annotationAdd BLAST | 23 | |
Topological domaini | 32 – 694 | CytoplasmicUniRule annotationAdd BLAST | 663 |
Keywords - Cellular componenti
Cell membrane, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000167604 | 1 – 694 | NADPH--cytochrome P450 reductaseAdd BLAST | 694 |
Expressioni
Inductioni
By benzoic acid (BA).1 Publication
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 66 – 220 | Flavodoxin-likeUniRule annotationAdd BLAST | 155 | |
Domaini | 276 – 537 | FAD-binding FR-typeUniRule annotationAdd BLAST | 262 |
Sequence similaritiesi
Belongs to the NADPH--cytochrome P450 reductase family.UniRule annotation
In the N-terminal section; belongs to the flavodoxin family.UniRule annotation
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1158, Eukaryota |
Family and domain databases
Gene3Di | 1.20.990.10, 1 hit 3.40.50.360, 1 hit 3.40.50.80, 1 hit |
HAMAPi | MF_03212, NCPR, 1 hit |
InterProi | View protein in InterPro IPR003097, CysJ-like_FAD-binding IPR017927, FAD-bd_FR_type IPR001094, Flavdoxin-like IPR008254, Flavodoxin/NO_synth IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase IPR029039, Flavoprotein-like_sf IPR039261, FNR_nucleotide-bd IPR023173, NADPH_Cyt_P450_Rdtase_alpha IPR001433, OxRdtase_FAD/NAD-bd IPR023208, P450R IPR017938, Riboflavin_synthase-like_b-brl |
Pfami | View protein in Pfam PF00667, FAD_binding_1, 1 hit PF00258, Flavodoxin_1, 1 hit PF00175, NAD_binding_1, 1 hit |
PIRSFi | PIRSF000208, P450R, 1 hit |
PRINTSi | PR00369, FLAVODOXIN PR00371, FPNCR |
SUPFAMi | SSF52218, SSF52218, 1 hit SSF52343, SSF52343, 1 hit SSF63380, SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS51384, FAD_FR, 1 hit PS50902, FLAVODOXIN_LIKE, 1 hit |
i Sequence
Sequence statusi: Complete.
Q00141-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAQLDTLDLV VLAVLLVGSV AYFTKGTYWA VAKDPYASTG PAMNGAAKAG
60 70 80 90 100
KTRNIIEKME ETGKNCVIFY GSQTGTAEDY ASRLAKEGSQ RFGLKTMVAD
110 120 130 140 150
LEEYDYENLD QFPEDKVAFF VLATYGEGEP TDNAVEFYQF FTGDDVAFES
160 170 180 190 200
ASADEKPLSK LKYVAFGLGN NTYEHYNAMV RQVDAAFQKL GPQRIGSAGE
210 220 230 240 250
GDDGAGTMEE DFLAWKEPMW AALSESMDLE EREAVYEPVF CVTENESLSP
260 270 280 290 300
EDETVYLGEP TQSHLQGTPK GPYSAHNPFI APIAESRELF TVKDRNCLHM
310 320 330 340 350
EISIAGSNLS YQTGDHIAVW PTNAGAEVDR FLQVFGLEGK RDSVINIKGI
360 370 380 390 400
DVTAKVPIPT PTTYDAAVRY YMEVCAPVSR QFVATLAAFA PDEESKAEIV
410 420 430 440 450
RLGSHKDYFH EKVTNQCFNM AQALQSITSK PFSAVPFSLL IEGITKLQPR
460 470 480 490 500
YYSISSSSLV QKDKISITAV VESVRLPGAS HMVKGVTTNY LLALKQKQNG
510 520 530 540 550
DPSPDPHGLT YSITGPRNKY DGIHVPVHVR HSNFKLPSDP SRPIIMVGPG
560 570 580 590 600
TGVAPFRGFI QERAALAAKG EKVGPTVLFF GCRKSDEDFL YKDEWKTYQD
610 620 630 640 650
QLGDNLKIIT AFSREGPQKV YVQHRLREHS ELVSDLLKQK ATFYVCGDAA
660 670 680 690
NMAREVNLVL GQIIAAQRGL PAEKGEEMVK HMRRRGRYQE DVWS
Sequence cautioni
The sequence CAA81550 differs from that shown. Reason: Frameshift.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z26938 Genomic DNA Translation: CAA81550.1 Frameshift. |
PIRi | S38427 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z26938 Genomic DNA Translation: CAA81550.1 Frameshift. |
PIRi | S38427 |
3D structure databases
SMRi | Q00141 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 5061.CADANGAP00006979 |
Phylogenomic databases
eggNOGi | KOG1158, Eukaryota |
Family and domain databases
Gene3Di | 1.20.990.10, 1 hit 3.40.50.360, 1 hit 3.40.50.80, 1 hit |
HAMAPi | MF_03212, NCPR, 1 hit |
InterProi | View protein in InterPro IPR003097, CysJ-like_FAD-binding IPR017927, FAD-bd_FR_type IPR001094, Flavdoxin-like IPR008254, Flavodoxin/NO_synth IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase IPR029039, Flavoprotein-like_sf IPR039261, FNR_nucleotide-bd IPR023173, NADPH_Cyt_P450_Rdtase_alpha IPR001433, OxRdtase_FAD/NAD-bd IPR023208, P450R IPR017938, Riboflavin_synthase-like_b-brl |
Pfami | View protein in Pfam PF00667, FAD_binding_1, 1 hit PF00258, Flavodoxin_1, 1 hit PF00175, NAD_binding_1, 1 hit |
PIRSFi | PIRSF000208, P450R, 1 hit |
PRINTSi | PR00369, FLAVODOXIN PR00371, FPNCR |
SUPFAMi | SSF52218, SSF52218, 1 hit SSF52343, SSF52343, 1 hit SSF63380, SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS51384, FAD_FR, 1 hit PS50902, FLAVODOXIN_LIKE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NCPR_ASPNG | |
Accessioni | Q00141Primary (citable) accession number: Q00141 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 2002 |
Last sequence update: | February 8, 2011 | |
Last modified: | April 7, 2021 | |
This is version 129 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |