ADRO_YEAST
ID ADRO_YEAST Reviewed; 493 AA.
AC P48360; D6VT08; P32840;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Probable NADPH:adrenodoxin oxidoreductase, mitochondrial {ECO:0000303|PubMed:9818721};
DE Short=AR {ECO:0000303|PubMed:9818721};
DE Short=Adrenodoxin reductase {ECO:0000303|PubMed:9818721};
DE EC=1.18.1.6 {ECO:0000269|PubMed:9727014};
DE AltName: Full=Ferredoxin--NADP(+) reductase {ECO:0000303|PubMed:9727014};
DE Short=Ferredoxin reductase {ECO:0000303|PubMed:9727014};
DE Flags: Precursor;
GN Name=ARH1 {ECO:0000303|PubMed:9818721}; OrderedLocusNames=YDR376W;
GN ORFNames=D9481.5;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9818721;
RX DOI=10.1002/(sici)1097-0061(19980630)14:9<839::aid-yea283>3.0.co;2-a;
RA Manzella L., Barros M.H., Nobrega F.G.;
RT "ARH1 of Saccharomyces cerevisiae: a new essential gene that codes for a
RT protein homologous to the human adrenodoxin reductase.";
RL Yeast 14:839-846(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FL200;
RX PubMed=8890749; DOI=10.1016/0378-1119(96)00041-8;
RA Lacour T., Dumas B.L.;
RT "A gene encoding a yeast equivalent of mammalian NADPH-adrenodoxin
RT oxidoreductases.";
RL Gene 174:289-292(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RX PubMed=1327750; DOI=10.1002/j.1460-2075.1992.tb05474.x;
RA Nobrega F.G., Nobrega M.P., Tzagoloff A.;
RT "BCS1, a novel gene required for the expression of functional Rieske iron-
RT sulfur protein in Saccharomyces cerevisiae.";
RL EMBO J. 11:3821-3829(1992).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=9727014; DOI=10.1074/jbc.273.37.23984;
RA Lacour T., Achstetter T., Dumas B.;
RT "Characterization of recombinant adrenodoxin reductase homologue (Arh1p)
RT from yeast. Implication in in vitro cytochrome p45011beta monooxygenase
RT system.";
RL J. Biol. Chem. 273:23984-23992(1998).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Adrenodoxin reductase transfers electrons from NADPH to
CC adrenodoxin, which subsequently donates them to the cytochrome P450
CC forms. {ECO:0000269|PubMed:9727014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized
CC [adrenodoxin]; Xref=Rhea:RHEA:42312, Rhea:RHEA-COMP:9998, Rhea:RHEA-
CC COMP:9999, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.6;
CC Evidence={ECO:0000269|PubMed:9727014};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P08165};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for NADPH {ECO:0000269|PubMed:9727014};
CC KM=0.6 uM for NADH {ECO:0000269|PubMed:9727014};
CC KM=0.1 uM for bovine adrenodoxin {ECO:0000269|PubMed:9727014};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:9727014}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Lethality in aerobic growth conditions and also
CC during fermentation. {ECO:0000269|PubMed:9727014}.
CC -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; U28038; AAA69523.1; -; Genomic_DNA.
DR EMBL; U38689; AAC49500.1; -; Genomic_DNA.
DR EMBL; U28373; AAB64812.1; -; Genomic_DNA.
DR EMBL; S47189; AAC09006.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12218.1; -; Genomic_DNA.
DR PIR; S61171; S61171.
DR RefSeq; NP_010664.3; NM_001180684.3.
DR AlphaFoldDB; P48360; -.
DR SMR; P48360; -.
DR BioGRID; 32435; 52.
DR DIP; DIP-1201N; -.
DR IntAct; P48360; 2.
DR MINT; P48360; -.
DR STRING; 4932.YDR376W; -.
DR MaxQB; P48360; -.
DR PaxDb; P48360; -.
DR PRIDE; P48360; -.
DR EnsemblFungi; YDR376W_mRNA; YDR376W; YDR376W.
DR GeneID; 851982; -.
DR KEGG; sce:YDR376W; -.
DR SGD; S000002784; ARH1.
DR VEuPathDB; FungiDB:YDR376W; -.
DR eggNOG; KOG1800; Eukaryota.
DR GeneTree; ENSGT00390000013574; -.
DR HOGENOM; CLU_024722_3_1_1; -.
DR InParanoid; P48360; -.
DR OMA; RFNFIGN; -.
DR BioCyc; MetaCyc:YDR376W-MON; -.
DR BioCyc; YEAST:YDR376W-MON; -.
DR Reactome; R-SCE-2395516; Electron transport from NADPH to Ferredoxin.
DR PRO; PR:P48360; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P48360; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; IDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:SGD.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR PIRSF; PIRSF000362; FNR; 1.
PE 1: Evidence at protein level;
KW Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NADP; Oxidoreductase; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..493
FT /note="Probable NADPH:adrenodoxin oxidoreductase,
FT mitochondrial"
FT /id="PRO_0000019425"
FT BINDING 26
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 100
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 177..180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 223..224
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 235
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 407
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 414..416
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 414
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT CONFLICT 33
FT /note="H -> Y (in Ref. 2; AAC49500)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="G -> S (in Ref. 1; AAA69523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 56237 MW; 9B0600BEA5A18CF3 CRC64;
MSFVQIRHIS SQINRKTVSI VGSGPSGFYT AYHLLKKSPI PLNVTIWEKL PVPFGLSRYG
VAPDHPEVKN CEETFTTCAE EFSSPTNQKH KFSFVGGITI GKEILLKELL DNQDAVILSY
GCTGDRKLNI PGELGTKGVF SSREFVNWYN GHPDFAKDKR FTDFDWSKVS KVGIIGNGNV
ALDITRVLIS NQIDEIWENT DISSLALNLL RRAPVKDVKL IARRDFVHSK FTNKELRELW
ELEKYGIRGR IDPKFFQKEM FDPSKYDRAF NRRVEMCSEY LKPFNERSKK NYKKAPPPSS
GYDKFWELDY LKTPLKINRD DFGAINSLSL CNNRLNEDNS LQPLKDVNNI MTYKVDLLIT
SLGYAGVPMP EFSKLSIGFD KDHIANKQGR VLTSSGEIFP HLYASGWIRK GSQGVIASTM
QDAFEVGDRV IQDLVVSGAL SLENSIDLSN IKHTTWKDWE RINKKELLRG KKEHKTRSKF
LTFEELWNGV EGI
