ID F4WRN3_ACREC Unreviewed; 473 AA.
AC F4WRN3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
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 ORFNames=G5I_08486 {ECO:0000313|EMBL:EGI63040.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI63040.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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: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 EMBL; GL888292; EGI63040.1; -; Genomic_DNA.
DR RefSeq; XP_011058426.1; XM_011060124.1.
DR AlphaFoldDB; F4WRN3; -.
DR STRING; 103372.F4WRN3; -.
DR EnsemblMetazoa; XM_011060124.1; XP_011058426.1; LOC105148416.
DR GeneID; 105148416; -.
DR KEGG; aec:105148416; -.
DR eggNOG; KOG1800; Eukaryota.
DR InParanoid; F4WRN3; -.
DR OrthoDB; 5764at2759; -.
DR UniPathway; UPA00296; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
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; SSF51971; Nucleotide-binding domain; 1.
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:UP000007755}.
FT DOMAIN 23..217
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 32
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 168..171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 212..213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 224
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 385..387
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 385
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ SEQUENCE 473 AA; 53663 MW; 2CC8D4B13292D4C8 CRC64;
MRYNIFKNCT RLLCTVTQQS VPQVCIVGAG PAGFYAAQQL LRDSSNAIIT ILDKQPVPFG
LIRYGVAPDH QDVKNVLNTF HKIATNPRVE FLGNVRLGIN IDVNYLRNVY DAVLLAYGAQ
EDRFLNIPGE HLNNVISARH FVGWYNGLPD DKDLKINLDV EEAVIIGQGN VAIDVARILL
TPVDKLKNTD ITSYALEALS RSKVRKVTMV GRRGPLQAAF TTAELREILR LQDCKTFWRE
QDFENIQTII PTLDRPRKRL TELMLKSLEE SKNDLVHAKE LHQIFLRSPI EFHGSKELQS
IKFAINQLRG ETIQNQVAQT IGKFEEIPCS LALRSIGYKT EQIYKDIPCN AKMGCLENIN
GKIEERNGER APLYVAGWAG TGPTGIILTT MRNAFQVARL IYNDLPSNLK GGNARRELCY
ELCNKNSVQI VSYEDWLKID RVEQQRGRQL GKVREKIVNV HEMLRIAENC IHR
//
