ADRO_SALFO
ID ADRO_SALFO Reviewed; 498 AA.
AC P82861;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=NADPH:adrenodoxin oxidoreductase, mitochondrial;
DE Short=AR;
DE Short=Adrenodoxin reductase;
DE EC=1.18.1.6 {ECO:0000250|UniProtKB:P08165};
DE AltName: Full=Ferredoxin--NADP(+) reductase;
DE Short=Ferredoxin reductase;
DE Flags: Precursor;
GN Name=fdxr;
OS Salvelinus fontinalis (Brook trout) (Salmo fontinalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salvelinus.
OX NCBI_TaxID=8038;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Bobe J., Goetz F.W., Langenau D.;
RT "Molecular cloning of adrenodoxin reductase from brook trout.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serves as the first electron transfer protein in all the
CC mitochondrial P450 systems including cholesterol side chain cleavage in
CC all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal
CC cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-
CC 27 hydroxylation in the liver. {ECO:0000250|UniProtKB:P08165}.
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:0000250|UniProtKB:P08165};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P08165};
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC {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; AF283287; AAG13948.1; -; mRNA.
DR AlphaFoldDB; P82861; -.
DR SMR; P82861; -.
DR UniPathway; UPA00296; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Cholesterol metabolism; Electron transport; FAD; Flavoprotein;
KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NADP; Oxidoreductase; Steroid metabolism; Sterol metabolism;
KW Transit peptide; Transport.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT CHAIN 38..498
FT /note="NADPH:adrenodoxin oxidoreductase, mitochondrial"
FT /id="PRO_0000019423"
FT REGION 469..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 75
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 190..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 234..235
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 246
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 404
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 411..413
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 411
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
SQ SEQUENCE 498 AA; 54342 MW; B472004DF7BC4AA7 CRC64;
MSTHKAALCK VQILKLFLIS ARCVRITRFY GVCGLSTSTP ASSPKVCIVG GGPAGFYTAQ
HLVKTRTDVQ VDIYERLPVP FGLVRFGVAP DHPEVKNVIN TFTQTARHAR CSFHGNVRVG
KDVTVEELQE AYHAVVLSYG AEGNRTMGVP GEDLAGVYSA KDFVGWYNGL PRNRELRPDL
SCETAVILGQ GNVALDVARM LLSPVDILKK TDITQHALDA LAESSVRRVL IVGRRGPLQV
ACTIKELREM VNLPGTRPEM EASEFEGIAE TLKSLARPRK RLTELLLKAA IETPGEEELE
KRNKAERAWG FRFLRRPLEV LPSTDLIRAA GIRLAVNRLE GDGEGVRAVA TGEVEDVECG
LVISSIGYKS LPIDPAVPFD GRKAIIPNTM GRVQQTAGLY CSGWVKRGPT GVIATTMNDS
FDTARTLLQD IGKGTLDVSS VKPGSQGVSA LLEKRGVKPV SFSDWEKIDS EETRRGETRG
KPREKMLDVG EMLQVARA
