ID   ADXH1_DROME             Reviewed;         172 AA.
AC   P37193; Q8MYT2; Q9VSW8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 3.
DT   02-SEP-2026, entry version 180.
DE   RecName: Full=Adrenodoxin-like protein 1, mitochondrial {ECO:0000305};
DE   AltName: Full=Ferredoxin-1 {ECO:0000312|FlyBase:FBgn0011769};
DE   Flags: Precursor;
GN   Name=Fdx1 {ECO:0000312|FlyBase:FBgn0011769};
GN   Synonyms=Fdxh {ECO:0000303|PubMed:25628335,
GN   ECO:0000312|FlyBase:FBgn0011769};
GN   ORFNames=CG4205 {ECO:0000312|FlyBase:FBgn0011769};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3123699; DOI=10.1016/0022-2836(87)90309-3;
RA   Pauli D., Tonka C.H.;
RT   "A Drosophila heat shock gene from locus 67B is expressed during
RT   embryogenesis and pupation.";
RL   J. Mol. Biol. 198:235-240(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   IDENTIFICATION.
RA   Rudd K.E.;
RL   Unpublished observations (JUL-1994).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25628335; DOI=10.1093/hmg/ddv024;
RA   Palandri A., L'hote D., Cohen-Tannoudji J., Tricoire H., Monnier V.;
RT   "Frataxin inactivation leads to steroid deficiency in flies and human
RT   ovarian cells.";
RL   Hum. Mol. Genet. 24:2615-2626(2015).
CC   -!- FUNCTION: Required for ecdysteroidogenesis in the prothoracic gland
CC       which is necessary for larval to pupal transition.
CC       {ECO:0000269|PubMed:25628335}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the whole body or in
CC       the prothoracic gland results in delayed or absent pupariation.
CC       {ECO:0000269|PubMed:25628335}.
CC   -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB55551.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X06542; CAB55551.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE014296; AAF50293.2; -; Genomic_DNA.
DR   EMBL; AY113620; AAM29625.1; -; mRNA.
DR   RefSeq; NP_001189075.1; NM_001202146.1.
DR   RefSeq; NP_523993.1; NM_079269.3.
DR   AlphaFoldDB; P37193; -.
DR   SMR; P37193; -.
DR   FunCoup; P37193; 584.
DR   STRING; 7227.FBpp0292527; -.
DR   PaxDb; 7227-FBpp0292527; -.
DR   PeptideAtlas; P37193; -.
DR   EnsemblMetazoa; FBtr0076498; FBpp0076226; FBgn0011769.
DR   EnsemblMetazoa; FBtr0303475; FBpp0292527; FBgn0011769.
DR   GeneID; 39070; -.
DR   KEGG; dme:Dmel_CG4205; -.
DR   UCSC; CG4205-RA; d. melanogaster.
DR   AGR; FB:FBgn0011769; -.
DR   CTD; 2230; -.
DR   FlyBase; FBgn0011769; Fdx1.
DR   VEuPathDB; VectorBase:FBgn0011769; -.
DR   eggNOG; KOG3309; Eukaryota.
DR   HOGENOM; CLU_082632_0_2_1; -.
DR   InParanoid; P37193; -.
DR   OMA; TLGWGWR; -.
DR   OrthoDB; 268593at2759; -.
DR   PhylomeDB; P37193; -.
DR   Reactome; R-DME-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR   Reactome; R-DME-2395516; Electron transport from NADPH to Ferredoxin.
DR   BioGRID-ORCS; 39070; 1 hit in 3 CRISPR screens.
DR   GenomeRNAi; 39070; -.
DR   PRO; PR:P37193; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0011769; Expressed in adult middle midgut class II enteroendocrine cell in adult midgut (Drosophila) and 86 other cell types or tissues.
DR   ExpressionAtlas; P37193; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:FlyBase.
DR   GO; GO:0005739; C:mitochondrion; ISS:FlyBase.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:FlyBase.
DR   GO; GO:0009055; F:electron transfer activity; ISS:FlyBase.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; NAS:FlyBase.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; NAS:FlyBase.
DR   GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR   GO; GO:0045998; P:positive regulation of ecdysteroid biosynthetic process; IMP:FlyBase.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:FlyBase.
DR   CDD; cd00207; fer2; 1.
DR   FunFam; 3.10.20.30:FF:000013; Adrenodoxin, mitochondrial; 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-like.
DR   InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   PANTHER; PTHR23426:SF65; FERREDOXIN-2, 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   2: Evidence at transcript level;
KW   2Fe-2S; Electron transport; Iron; Iron-sulfur; Lipid metabolism;
KW   Metal-binding; Mitochondrion; Reference proteome; Steroid metabolism;
KW   Steroidogenesis; Transit peptide; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..172
FT                   /note="Adrenodoxin-like protein 1, mitochondrial"
FT                   /id="PRO_0000000993"
FT   DOMAIN          57..159
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         94
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         100
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         103
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         140
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   CONFLICT        161
FT                   /note="N -> D (in Ref. 4; AAM29625)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   172 AA;  19734 MW;  9D70F51572562E2F CRC64;
     MFCLLLRRSA VHNSCKLISK QIAKPAFYTP HNALHTTIPR RHGEFEWQDP KSTDEIVNIT
     YVDKDGKRTK VQGKVGDNVL YLAHRHGIEM EGACEASLAC TTCHVYVQHD YLQKLKEAEE
     QEDDLLDMAP FLRENSRLGC QILLDKSMEG MELELPKATR NFYVDGHKPK PH
//