ID E9H3I4_DAPPU Unreviewed; 471 AA.
AC E9H3I4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 69.
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=DAPPUDRAFT_307619 {ECO:0000313|EMBL:EFX73780.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX73780.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX73780.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
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; GL732588; EFX73780.1; -; Genomic_DNA.
DR AlphaFoldDB; E9H3I4; -.
DR STRING; 6669.E9H3I4; -.
DR EnsemblMetazoa; EFX73780; EFX73780; DAPPUDRAFT_307619.
DR KEGG; dpx:DAPPUDRAFT_307619; -.
DR eggNOG; KOG1800; Eukaryota.
DR HOGENOM; CLU_024722_3_1_1; -.
DR InParanoid; E9H3I4; -.
DR OMA; RFNFIGN; -.
DR PhylomeDB; E9H3I4; -.
DR UniPathway; UPA00296; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
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:UP000000305};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..471
FT /note="NADPH:adrenodoxin oxidoreductase, mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003240784"
FT DOMAIN 20..176
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 29
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 165..168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 209..210
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 381..383
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 381
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ SEQUENCE 471 AA; 52264 MW; 26335F751017C709 CRC64;
MLIFVFFLHI TIRILLTVAQ LCIVGSGPAG FYTAQHLLKN CPTLEIDMIE KLPVPFGLVR
YGVAPDHPDV KNVINTFTAI AKSGRLQFVG NVTVGKDVTL NDLRNAYDVV VLAYGAAQDR
WLGISGENLC NVVSARKFVG WYNGLPEESH LKFDLDAETV VIIGQGNVAL DIARILLTPI
DMLKKTDIAQ HALEALSQSK IKNVKIVGRR GPLQVAFTIK ELREMIKLPG NSYRIHLENP
EYIDACLPKT SRPRKRLTEL MLQSSSMKRS EEDSSKQWEL IFHRTPIKIV GDSNANKVNG
LVVGINHLTG DDWENPQVED TGLRETIPCG MILKSIGYKS LPLSDELPFD HAKGIIRQTE
GRVEGMQGVF CSGWVASGPV GVIASTMQSG HDVGKRIIED LKNGIVGTGT RKPGRDAILS
QLEARNVEPV TFVEWEALDN EERERGKYQK KPREKIVDVR EMIDIAKKGQ S
//
