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YEAST:NCPR

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) NCP1 (ECO:0000255 with HAMAP-Rule:MF_03212) (synonyms: CPR1, NCPR1, PRD1)
Protein Name(s) NADPH--cytochrome P450 reductase (ECO:0000255 with HAMAP-Rule:MF_03212)

CPR (ECO:0000255 with HAMAP-Rule:MF_03212) P450R (ECO:0000255 with HAMAP-Rule:MF_03212)

External Links
UniProt P16603
EMBL D13788
U00062
AY693091
BK006934
PIR S46735
RefSeq NP_011908.1
PDB 2BF4
2BN4
2BPO
3FJO
PDBsum 2BF4
2BN4
2BPO
3FJO
ProteinModelPortal P16603
SMR P16603
BioGrid 36474
DIP DIP-8294N
IntAct P16603
MINT MINT-2782506
iPTMnet P16603
MaxQB P16603
PeptideAtlas P16603
EnsemblFungi [example_ID YHR042W]
GeneID 856438
KEGG sce:YHR042W
EuPathDB FungiDB:YHR042W
SGD S000001084
GeneTree ENSGT00620000087711
HOGENOM HOG000282027
InParanoid P16603
KO K00327
OMA VPIYVRK
OrthoDB EOG744TKC
BioCyc YEAST:YHR042W-MONOMER
BRENDA 1.6.2.4
Reactome R-SCE-1474151
R-SCE-203615
R-SCE-5218920
R-SCE-5578775
EvolutionaryTrace P16603
NextBio 982042
PRO PR:P16603
Proteomes UP000002311
GO GO:0005789
GO:0016021
GO:0005741
GO:0005886
GO:0009055
GO:0010181
GO:0005506
GO:0003958
GO:0006696
Gene3D 1.20.990.10
3.40.50.360
HAMAP MF_03212
InterPro IPR003097
IPR017927
IPR001094
IPR008254
IPR001709
IPR029039
IPR023173
IPR001433
IPR023208
IPR017938
Pfam PF00667
PF00258
PF00175
PIRSF PIRSF000208
PRINTS PR00369
PR00371
SUPFAM SSF52218
SSF63380
PROSITE PS51384
PS50902

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009055

electron carrier activity

other:GO_REF:0000100

ECO:0000247

PMID:2334437[1]


F

The transfer annotation HHpred hits had an E-value of 2.1E-24, a similarity of 99.9%, and a query coverage of 75.25% which serves as the evidence.

complete
CACAO 12061

GO:0003959

NADPH dehydrogenase activity

PMID:27694803[2]

ECO:0000314

F

The author cloned and overexpressed Ncp1 and monitored the reduction of Dph3 by Dph3's absorbance at 488nm. The author found that Ncp1 reduced Dph3 after the addition of NADPH to the reaction tube (Supplementary figure 5C).

complete
CACAO 12191

part_of

GO:0005741

mitochondrial outer membrane

PMID:16407407[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:16823961[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:24769239[5]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:14576278[6]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0009055

electron transfer activity

PMID:11485306[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006696

ergosterol biosynthetic process

PMID:9468503[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003958

NADPH-hemoprotein reductase activity

PMID:9087488[9]

ECO:0000314

direct assay evidence used in manual assertion

F

has_direct_input:(UniProtKB:P10614)

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10191
MGI:MGI:97361
PANTHER:PTN000453956
RGD:3184
RGD:68335
UniProtKB:O08336
UniProtKB:O08394
UniProtKB:Q9UBK8
UniProtKB:Q9UHB4

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:97744
PANTHER:PTN000453956
UniProtKB:Q9UHB4

F

Seeded From UniProt

complete

enables

GO:0010181

FMN binding

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10191
MGI:MGI:97361
PANTHER:PTN000453956
RGD:3184
RGD:68335
UniProtKB:O08336
UniProtKB:O08394
UniProtKB:Q9UBK8
UniProtKB:Q9UHB4

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000453956
RGD:3184
RGD:3185
RGD:3186
UniProtKB:P35228
UniProtKB:Q9SB48
UniProtKB:Q9UHB4

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000453765
RGD:3184
RGD:3185
RGD:3186
UniProtKB:P35228

C

Seeded From UniProt

complete

enables

GO:0003958

NADPH-hemoprotein reductase activity

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000453763
PomBase:SPBC29A10.01
RGD:68335
SGD:S000001084
TAIR:locus:2128951
UniProtKB:A0A1D8PLR7
UniProtKB:O08336
UniProtKB:O08394
UniProtKB:P16435
UniProtKB:Q9UBK8

F

Seeded From UniProt

complete

involved_in

GO:0022900

electron transport chain

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0009055

P

Seeded From UniProt

complete

enables

GO:0003958

NADPH-hemoprotein reductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023208

F

Seeded From UniProt

complete

enables

GO:0010181

FMN binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001094
InterPro:IPR008254

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001433
InterPro:IPR001709
InterPro:IPR003097
InterPro:IPR017927
InterPro:IPR023173

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001094
InterPro:IPR001433
InterPro:IPR001709
InterPro:IPR003097
InterPro:IPR017927
InterPro:IPR023173
InterPro:IPR023208

P

Seeded From UniProt

complete

enables

GO:0003958

NADPH-hemoprotein reductase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.6.2.4

F

Seeded From UniProt

complete

enables

GO:0050660

flavin adenine dinucleotide binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000239476

F

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000239476

F

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000239476

C

Seeded From UniProt

complete

part_of

GO:0005789

endoplasmic reticulum membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000239476

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000239476

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000239476

C

Seeded From UniProt

complete

involved_in

GO:0006696

ergosterol biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000239476

P

Seeded From UniProt

complete

enables

GO:0003958

NADPH-hemoprotein reductase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000239476

F

Seeded From UniProt

complete

enables

GO:0010181

FMN binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000239476

F

Seeded From UniProt

complete

part_of

GO:0005741

mitochondrial outer membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1000
UniProtKB-SubCell:SL-0172

C

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0256

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

involved_in

GO:0006629

lipid metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0443

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

Seeded From UniProt

complete

involved_in

GO:0008202

steroid metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0753

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

involved_in

GO:0016126

sterol biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0756

P

Seeded From UniProt

complete

involved_in

GO:0006694

steroid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0752

P

Seeded From UniProt

complete

part_of

GO:0005789

endoplasmic reticulum membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0097

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Helms, LR et al. (1990) Identification, sequence determination, and expression of the flavodoxin gene from Desulfovibrio salexigens. Biochem. Biophys. Res. Commun. 168 809-17 PubMed GONUTS page
  2. Lin, Z et al. (2016) Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification. Nat. Chem. Biol. PubMed GONUTS page
  3. Zahedi, RP et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol. Biol. Cell 17 1436-50 PubMed GONUTS page
  4. Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
  5. Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page
  6. Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
  7. Lamb, DC et al. (2001) Activities and kinetic mechanisms of native and soluble NADPH-cytochrome P450 reductase. Biochem. Biophys. Res. Commun. 286 48-54 PubMed GONUTS page
  8. Venkateswarlu, K et al. (1998) The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity. J. Biol. Chem. 273 4492-6 PubMed GONUTS page
  9. Venkateswarlu, K et al. (1997) Characterization of Saccharomyces cerevisiae CYP51 and a CYP51 fusion protein with NADPH cytochrome P-450 oxidoreductase expressed in Escherichia coli. Antimicrob. Agents Chemother. 41 776-80 PubMed GONUTS page
  10. 10.0 10.1 10.2 10.3 10.4 10.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page