ID A0A3Q4MSY0_NEOBR Unreviewed; 454 AA.
AC A0A3Q4MSY0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=NADPH:adrenodoxin oxidoreductase, mitochondrial {ECO:0000256|ARBA:ARBA00016287, ECO:0000256|PIRNR:PIRNR000362};
DE EC=1.18.1.6 {ECO:0000256|ARBA:ARBA00013219, ECO:0000256|PIRNR:PIRNR000362};
GN Name=FDXR {ECO:0000313|Ensembl:ENSNBRP00000018609.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000018609.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000018609.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003133}.
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:0000256|ARBA:ARBA00000384,
CC ECO:0000256|PIRNR:PIRNR000362};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRNR:PIRNR000362, ECO:0000256|PIRSR:PIRSR000362-1};
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC {ECO:0000256|ARBA:ARBA00004731}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|PIRNR:PIRNR000362}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008312, ECO:0000256|PIRNR:PIRNR000362}.
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DR AlphaFoldDB; A0A3Q4MSY0; -.
DR STRING; 32507.ENSNBRP00000018609; -.
DR Ensembl; ENSNBRT00000019100.1; ENSNBRP00000018609.1; ENSNBRG00000014334.1.
DR GeneTree; ENSGT00390000013574; -.
DR OMA; RFNFIGN; -.
DR UniPathway; UPA00296; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000014334; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF91; NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000362; FNR; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000362};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000362};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR000362};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000362};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000362};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580}.
FT DOMAIN 7..157
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 31
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 75
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 146..149
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 190..191
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 360
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 367..369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 367
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ SEQUENCE 454 AA; 49384 MW; 7C202E9CC72EBC34 CRC64;
MSSCSPKVCI VGSGPAGFYT AQHLIKVDIY ERLPVPFGLV RFGVAPDHPE VKNVINTFTQ
TAKHSRCSFY GNVNVGKNVS ITELQQAYHA VVLSYGAEGN RSMGVPGEDL AGVYSAKDFV
GWYNGLPSCR ELSPDLSCET AVILGQGNVA LDVARILLAP IDILKKTDIT QPTLEALAES
QVRRVLIVGR RGPIQIACTI KELREMVNLP DTRPDMVAAD FDGVKEALKD LPRPRKRLTE
LMLKTALEVP GEKEQERRSK ASRTWGFRFF RSPVEVLAEP GHSRIAGIRL AINKLEGSGD
GAQAVLTGEV EDVSCGLVVS SIGYKSLPID PSVPFDSRKA IVPNTMGRVK QAAGLYCSGW
LKTGPTGVIA TTMNNSFDTA RSIVEDMESG TLDMSAAKPG SQSISALLEK RGVKPVTFSD
WEKIDNVEMK RGESRGKPRE KLLTVEEMLH VAWT
//
