ID   ADX_SHEEP               Reviewed;         128 AA.
AC   P29330;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Adrenodoxin;
DE   AltName: Full=Adrenal ferredoxin;
DE   AltName: Full=Ferredoxin-1;
GN   Name=FDX1;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-127.
RC   TISSUE=Adrenal gland;
RX   PubMed=1733794; DOI=10.1016/0020-711x(92)90259-4;
RA   Shimizu C., Tomita S., Matsuo Y., Miyatake A., Ichikawa Y.;
RT   "Determination of the amino acid sequence of adreno-ferredoxin from sheep
RT   adrenocortical mitochondria.";
RL   Int. J. Biochem. 24:281-288(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-128.
RX   PubMed=1568470; DOI=10.1016/0014-5793(92)81232-b;
RA   Matsuo Y., Tsujita M., Mizoguchi K., Ichikawa Y.;
RT   "Expression cloning of a sheep adreno-ferredoxin using the polymerase chain
RT   reaction.";
RL   FEBS Lett. 301:132-136(1992).
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   -!- SUBUNIT: Interacts with CYP11A1. {ECO:0000250|UniProtKB:P10109}.
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   PIR; S21131; S21131.
DR   AlphaFoldDB; P29330; -.
DR   SMR; P29330; -.
DR   STRING; 9940.ENSOARP00000014331; -.
DR   eggNOG; KOG3309; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR   GO; GO:0042446; P:hormone biosynthetic process; ISS:UniProtKB.
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; Acetylation; Cholesterol metabolism; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Lipid metabolism; Metal-binding;
KW   Mitochondrion; Phosphoprotein; Reference proteome; Steroid metabolism;
KW   Steroidogenesis; Sterol metabolism; Transport.
FT   CHAIN           1..128
FT                   /note="Adrenodoxin"
FT                   /id="PRO_0000201161"
FT   DOMAIN          7..111
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         46
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         52
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         55
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         92
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46656"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P46656"
FT   MOD_RES         6
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P46656"
FT   MOD_RES         98
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P46656"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10109"
FT   CONFLICT        123
FT                   /note="N -> D (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   128 AA;  14014 MW;  46135A661315E463 CRC64;
     SSSEDKVTVN FINRDGETLT TKGKVGDSLL DVVVENNLDI DGFGACEGTL ACSTCHLIFE
     QHIYEKLEAI TDEENDMLDL AYGLTDRSRL GCQICLTKAM DNMTVRVPDA VSDARESIDM
     GMNSSKIE