FDX2_BOVIN
ID FDX2_BOVIN Reviewed; 186 AA.
AC Q05B51;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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; BC122825; AAI22826.1; -; mRNA.
DR RefSeq; NP_001073695.1; NM_001080226.2.
DR AlphaFoldDB; Q05B51; -.
DR SMR; Q05B51; -.
DR STRING; 9913.ENSBTAP00000013630; -.
DR PaxDb; Q05B51; -.
DR Ensembl; ENSBTAT00000013630; ENSBTAP00000013630; ENSBTAG00000010318.
DR GeneID; 505159; -.
DR KEGG; bta:505159; -.
DR CTD; 112812; -.
DR VEuPathDB; HostDB:ENSBTAG00000010318; -.
DR VGNC; VGNC:55209; FDX2.
DR eggNOG; KOG3309; Eukaryota.
DR GeneTree; ENSGT00940000161143; -.
DR HOGENOM; CLU_082632_0_2_1; -.
DR InParanoid; Q05B51; -.
DR OMA; WQDPKSP; -.
DR OrthoDB; 1380051at2759; -.
DR TreeFam; TF354319; -.
DR Reactome; R-BTA-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000010318; Expressed in oocyte and 106 other tissues.
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..55
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 56..186
FT /note="Ferredoxin-2, mitochondrial"
FT /id="PRO_0000325951"
FT DOMAIN 71..173
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 114
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
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 154
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 186 AA; 19947 MW; 108F58EE6061B4FA CRC64;
MPVMAASVAW GGVNAGFLLR AARGAWWSRP GGFWGSGEAA APAIARKFRA TGSRPAGEEE
AGGPERPGDV VNVVFVDRSG QRIPVSGRVG DNVLHLAQRH GLDLEGACEA SLACSTCHVY
VSEDHLDLLP PPDEREDDML DMAPLLQENS RLGCQIVLTP ELEGAEFTLP KITRNFYVDG
HVPKPH