ADRO_DICDI
ID ADRO_DICDI Reviewed; 515 AA.
AC Q54KG7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=fdxr; ORFNames=DDB_G0287353;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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; AAFI02000100; EAL63744.1; -; Genomic_DNA.
DR RefSeq; XP_637256.1; XM_632164.1.
DR AlphaFoldDB; Q54KG7; -.
DR SMR; Q54KG7; -.
DR STRING; 44689.DDB0234047; -.
DR PaxDb; Q54KG7; -.
DR EnsemblProtists; EAL63744; EAL63744; DDB_G0287353.
DR GeneID; 8626086; -.
DR KEGG; ddi:DDB_G0287353; -.
DR dictyBase; DDB_G0287353; fdxr.
DR eggNOG; KOG1800; Eukaryota.
DR HOGENOM; CLU_024722_3_0_1; -.
DR InParanoid; Q54KG7; -.
DR OMA; RFNFIGN; -.
DR PhylomeDB; Q54KG7; -.
DR Reactome; R-DDI-2395516; Electron transport from NADPH to Ferredoxin.
DR PRO; PR:Q54KG7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:dictyBase.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; ISS:dictyBase.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0022900; P:electron transport chain; IC:dictyBase.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..515
FT /note="Probable NADPH:adrenodoxin oxidoreductase,
FT mitochondrial"
FT /id="PRO_0000331233"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 81
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 191..194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 236..237
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 419
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 426..428
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P08165"
FT BINDING 426
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P08165"
SQ SEQUENCE 515 AA; 57701 MW; 354F5110BB53F2D9 CRC64;
MINVLINKSS KLVNGVDSCI NNKTIRLFCS SSSTNQVNKT PFNLCIIGSG PAGLYTAAKV
HRQIPHANIT ILEKLPYPFG LVRSGISPDH QNEKKVKNTL EKVLLEHPHQ IQFIGNVDIE
KDIKFQYIKD NFHAVVLACG IEGDKKLGIP GELTLKNVYF AREFIGWLNG NLKDQHKQFD
LSNENLAIVG QGNVALDVAR LLLKKNSDEL KKTDITSTSF DKINKSNVKN IHIIGRRGPL
EVSFTNKEIR EILTLQNVNT FINDISTLDV SEEDVSKLER AKKRTFELFK QHLKPFDQEI
ANNGNMNLIF HFLRSPVELL DKYGSSSGSG DGMVLSKIKL EKNKLIIDEK TQQKKAIGSG
EFEIIECSSL FRSIGYTGTK QFPSVPFDFN SVSIPNKYGK VLEEPNSDKF INGLYVSGWL
KGGPSGSIPN ISANSEETAS IIHQDYESNQ FINNNNNNDG GHNSITSLLQ PNHKIINFND
YKKIESEEVK RGKEKGKLLE KIIVFDELKN IINNS
