ID ADX_CHICK Reviewed; 143 AA.
AC P13216;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 08-NOV-2023, entry version 148.
DE RecName: Full=Adrenodoxin, mitochondrial;
DE AltName: Full=Adrenal ferredoxin;
DE Flags: Precursor; Fragment;
GN Name=FDX1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=3415692; DOI=10.1016/s0006-291x(88)81096-9;
RA Kagimoto K., McCarthy J.L., Waterman M.R., Kagimoto M.;
RT "Deduced amino acid sequence of mature chicken testis ferredoxin.";
RL Biochem. Biophys. Res. Commun. 155:379-383(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-143.
RC TISSUE=Kidney;
RA Blanchard R.K., Henry H.L.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=1909889; DOI=10.1021/bi00101a024;
RA Skjeldal L., Markley J.L., Coghlan V.M., Vickery L.E.;
RT "1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances
RT suggest different electron delocalization patterns from plant
RT ferredoxins.";
RL Biochemistry 30:9078-9083(1991).
CC -!- FUNCTION: Essential for the synthesis of various steroid hormones.
CC Participates in the reduction of mitochondrial cytochrome P450 for
CC steroidogenesis. Transfers electrons from adrenodoxin reductase to
CC CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain
CC cleavage. Does not form a ternary complex with adrenodoxin reductase
CC and CYP11A1 but shuttles between the two enzymes to transfer electrons.
CC {ECO:0000250|UniProtKB:P00257}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P10109}.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; M21275; AAA48576.1; -; mRNA.
DR EMBL; U25823; AAA82597.1; -; mRNA.
DR PIR; A31574; A31574.
DR RefSeq; NP_001185597.1; NM_001198668.1.
DR AlphaFoldDB; P13216; -.
DR SMR; P13216; -.
DR STRING; 9031.ENSGALP00000040794; -.
DR PaxDb; 9031-ENSGALP00000040794; -.
DR GeneID; 373947; -.
DR KEGG; gga:373947; -.
DR CTD; 2230; -.
DR VEuPathDB; HostDB:geneid_373947; -.
DR eggNOG; KOG3309; Eukaryota.
DR HOGENOM; CLU_082632_2_1_1; -.
DR InParanoid; P13216; -.
DR PhylomeDB; P13216; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426:SF26; ADRENODOXIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR23426; FERREDOXIN/ADRENODOXIN; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cholesterol metabolism; Electron transport; Iron; Iron-sulfur;
KW Lipid metabolism; Metal-binding; Mitochondrion; Reference proteome;
KW Steroid metabolism; Steroidogenesis; Sterol metabolism; Transit peptide;
KW Transport.
FT TRANSIT <1..19
FT /note="Mitochondrion"
FT CHAIN 20..143
FT /note="Adrenodoxin, mitochondrial"
FT /id="PRO_0000000992"
FT DOMAIN 26..130
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 65
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 71
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 74
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 111
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT CONFLICT 4
FT /note="V -> P (in Ref. 2; AAA82597)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="A -> S (in Ref. 2; AAA82597)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 143 AA; 15483 MW; 15BC3DA3067914B7 CRC64;
CSAVAVRTLR PLSLSARAAC SSEDKITVHF INRDGDKLTA KGKPGDSLLD VVVENNLDID
GFGACEGTLA CSTCHLIFED HIFEKLDAIT DEEMDMLDLA YGLTETSRLG CQICLKKSMD
NMTVRVPEAV ADARQSVDLS KNS
//
