ADXH1_DROME
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 03-AUG-2022, entry version 166.
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; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; 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 STRING; 7227.FBpp0292527; -.
DR PaxDb; 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 CTD; 2230; -.
DR FlyBase; FBgn0011769; Fdx1.
DR VEuPathDB; VectorBase:FBgn0011769; -.
DR eggNOG; KOG3309; Eukaryota.
DR GeneTree; ENSGT00940000161143; -.
DR HOGENOM; CLU_082632_0_2_1; -.
DR InParanoid; P37193; -.
DR OMA; WQDPKSP; -.
DR OrthoDB; 1380051at2759; -.
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 ChiTaRS; Fdx1; fly.
DR GenomeRNAi; 39070; -.
DR PRO; PR:P37193; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011769; Expressed in adult hindgut (Drosophila) and 23 other tissues.
DR ExpressionAtlas; P37193; baseline and differential.
DR Genevisible; P37193; DM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; 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:0045998; P:positive regulation of ecdysteroid biosynthetic process; IMP:FlyBase.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IBA:GO_Central.
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 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
