FDX2_DANRE
ID FDX2_DANRE Reviewed; 195 AA.
AC Q08C57;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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; ORFNames=zgc:153554;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) 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; BC124384; AAI24385.1; -; mRNA.
DR RefSeq; NP_001070132.1; NM_001076664.2.
DR AlphaFoldDB; Q08C57; -.
DR SMR; Q08C57; -.
DR STRING; 7955.ENSDARP00000088240; -.
DR PaxDb; Q08C57; -.
DR PRIDE; Q08C57; -.
DR GeneID; 767726; -.
DR KEGG; dre:767726; -.
DR CTD; 112812; -.
DR ZFIN; ZDB-GENE-060929-1046; fdx2.
DR eggNOG; KOG3309; Eukaryota.
DR InParanoid; Q08C57; -.
DR OrthoDB; 1380051at2759; -.
DR PhylomeDB; Q08C57; -.
DR Reactome; R-DRE-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR Reactome; R-DRE-196108; Pregnenolone biosynthesis.
DR Reactome; R-DRE-211976; Endogenous sterols.
DR Reactome; R-DRE-2395516; Electron transport from NADPH to Ferredoxin.
DR PRO; PR:Q08C57; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
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:0051353; P:positive regulation of oxidoreductase activity; IBA:GO_Central.
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..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 62..195
FT /note="Ferredoxin-2, mitochondrial"
FT /id="PRO_0000325954"
FT DOMAIN 81..182
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 117
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 123
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 126
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 163
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 195 AA; 21468 MW; B4EE7717920597D6 CRC64;
MAAAAAVRAG VNFTQRLNRI SPVCRVCPLL RLNRCTGAAV RRAVDGFSAP SRRLRTSIGV
CQSEDSSAPE EDAHAQEHIV NVVYIDRSGR RIPVQARVGD NVLYLAHKHG IDLEGACEAS
LACSTCHVYV SSGHYDRLPE PEEREDDMLD MAPLLQENSR LGCQIILTPE LDGMELTLPK
VTRNFYVDGH VPKPH