ID   FDX2_XENLA              Reviewed;         193 AA.
AC   Q5FWQ0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Ferredoxin-2, mitochondrial;
DE   AltName: Full=Adrenodoxin-like protein;
DE   AltName: Full=Ferredoxin-1-like protein;
DE   Flags: Precursor;
GN   Name=fdx2; Synonyms=fdx1l;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for heme A and Fe/S protein biosynthesis.
CC       {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC       {ECO:0000305}.
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DR   EMBL; BC089254; AAH89254.1; -; mRNA.
DR   RefSeq; NP_001089982.1; NM_001096513.1.
DR   AlphaFoldDB; Q5FWQ0; -.
DR   SMR; Q5FWQ0; -.
DR   DNASU; 735053; -.
DR   GeneID; 735053; -.
DR   KEGG; xla:735053; -.
DR   CTD; 735053; -.
DR   Xenbase; XB-GENE-5933715; fdx2.L.
DR   OrthoDB; 1380051at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 735053; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0140647; P:P450-containing electron transport chain; IEA:InterPro.
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; Metal-binding;
KW   Mitochondrion; Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..193
FT                   /note="Ferredoxin-2, mitochondrial"
FT                   /id="PRO_0000325955"
FT   DOMAIN          78..180
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   REGION          38..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         115
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         121
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         124
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         161
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   193 AA;  21361 MW;  CB4612854BAAD791 CRC64;
     MAVFLLKRGV WASLMIGGFG PRAVLFSKLG QNHARLSQAT PEKLETSNEE EGSSSAQITA
     GVESDAENQR AELSEETVEV VFLDRSGQRI PVKGKVGESV LCLAHRYNIE LEGACESSLA
     CSTCHVYVNT EYFHKLPEPD EREDDMLDMA PLLQENSRLG CQIILTKQLN GAEFTLPKIT
     RNFYVDGHVP KPH