ADRO_SCHPO
ID ADRO_SCHPO Reviewed; 469 AA.
AC O59710;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable NADPH:adrenodoxin oxidoreductase, mitochondrial;
DE Short=AR;
DE Short=Adrenodoxin reductase;
DE EC=1.18.1.6;
DE AltName: Full=Ferredoxin--NADP(+) reductase;
DE Short=Ferredoxin reductase;
DE Flags: Precursor;
GN Name=arh1; ORFNames=SPBC3B8.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Serves as the first electron transfer protein in all the
CC mitochondrial P450 systems. {ECO:0000250}.
CC -!- FUNCTION: Acts as an electron transfer protein. Essential for
CC viability. {ECO:0000250|UniProtKB:P48360}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P08165};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA18290.1; -; Genomic_DNA.
DR PIR; T40339; T40339.
DR RefSeq; NP_596413.1; NM_001022332.2.
DR AlphaFoldDB; O59710; -.
DR SMR; O59710; -.
DR STRING; 4896.SPBC3B8.01c.1; -.
DR SwissPalm; O59710; -.
DR MaxQB; O59710; -.
DR PaxDb; O59710; -.
DR EnsemblFungi; SPBC3B8.01c.1; SPBC3B8.01c.1:pep; SPBC3B8.01c.
DR GeneID; 2541049; -.
DR KEGG; spo:SPBC3B8.01c; -.
DR PomBase; SPBC3B8.01c; arh1.
DR VEuPathDB; FungiDB:SPBC3B8.01c; -.
DR eggNOG; KOG1800; Eukaryota.
DR HOGENOM; CLU_024722_3_1_1; -.
DR InParanoid; O59710; -.
DR OMA; MRPYHVA; -.
DR PhylomeDB; O59710; -.
DR Reactome; R-SPO-2395516; Electron transport from NADPH to Ferredoxin.
DR PRO; PR:O59710; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0071949; F:FAD binding; IDA:PomBase.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IDA:PomBase.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IDA:PomBase.
DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IC:PomBase.
DR GO; GO:0022904; P:respiratory electron transport chain; IC:PomBase.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; ISO:PomBase.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000362; FNR; 1.
PE 3: Inferred from homology;
KW Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NADP; Oxidoreductase; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 39..469
FT /note="Probable NADPH:adrenodoxin oxidoreductase,
FT mitochondrial"
FT /id="PRO_0000337259"
FT BINDING 27
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 92
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 164..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 208..209
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 375
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 382..384
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 382
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
SQ SEQUENCE 469 AA; 52716 MW; 2AFBDBCF86C57291 CRC64;
MLSRFIKRTY STQTSSPVVG IIGSGPAAFY TAHRLLRNDP NVKIDMFESR PVPFGLVRYG
VAPDHPEVKH VEHKFSEIAE STQFRFLGNV NVGTDVSLRD LTKNYDCLVL AYGAAGDKRL
GIPGEDLSGV YSAREVVGWY NSDPRNQNLE LDLSQVEDAV VIGHGNVSLD VARILLSNPA
QLSPTDINPL FLKSLERSNL KRLHIVGRRN IFSVSFTIKE LRELFALSSA VFFAPSFNYS
TKWMNETDAS GLDRPRKRLL KLLVSEIQKA VSEKRVAPYS KDKKCWNLEF GLTPVEILGH
KGNVENVRFQ ITDSIRTDAE SKFTTIPAQL FIRSIGYKSM PLPGMKDVGV PFDDAKGIVK
NVNGFVRPGI YTSGWVKHGP IGVIATTMMD AFATADTITK DWKSKKEFLK NSKLGWDGLK
KNIKTPVIHW KDWKVIRNAE IERGLRHESL SEKFRSNEDM IKLIYPGKK
