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ADX_CHICK
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   03-AUG-2022, entry version 143.
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; P13216; -.
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   OrthoDB; 1380051at2759; -.
DR   PhylomeDB; P13216; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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: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; PTHR23426; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00355; ADRENODOXIN.
DR   SUPFAM; SSF54292; SSF54292; 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
 
 
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