ID   ADRX_ENCCU              Reviewed;         128 AA.
AC   Q8SV19;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Adrenodoxin homolog;
DE   AltName: Full=Ferredoxin;
GN   OrderedLocusNames=ECU07_0600;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18318866; DOI=10.1111/j.1550-7408.2008.00315.x;
RA   Williams B.A.P., Cali A., Takvorian P.M., Keeling P.J.;
RT   "Distinct localization patterns of two putative mitochondrial proteins in
RT   the microsporidian Encephalitozoon cuniculi.";
RL   J. Eukaryot. Microbiol. 55:131-133(2008).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions. {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: Mitosome {ECO:0000269|PubMed:18318866}.
CC   -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC       {ECO:0000305}.
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DR   EMBL; AL590447; CAD25592.1; -; Genomic_DNA.
DR   RefSeq; NP_585988.1; NM_001041610.1.
DR   PDB; 5UJ5; NMR; -; A=1-128.
DR   PDBsum; 5UJ5; -.
DR   AlphaFoldDB; Q8SV19; -.
DR   BMRB; Q8SV19; -.
DR   SMR; Q8SV19; -.
DR   STRING; 284813.Q8SV19; -.
DR   GeneID; 859417; -.
DR   KEGG; ecu:ECU07_0600; -.
DR   VEuPathDB; MicrosporidiaDB:ECU07_0600; -.
DR   HOGENOM; CLU_082632_5_0_1; -.
DR   InParanoid; Q8SV19; -.
DR   OMA; SACGGVC; -.
DR   OrthoDB; 1380051at2759; -.
DR   Proteomes; UP000000819; Chromosome VII.
DR   GO; GO:0032047; C:mitosome; 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; 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.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Mitosome; Reference proteome; Transport.
FT   CHAIN           1..128
FT                   /note="Adrenodoxin homolog"
FT                   /id="PRO_0000382938"
FT   DOMAIN          12..115
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         50
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         56
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         59
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         96
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   STRAND          14..22
FT                   /evidence="ECO:0007829|PDB:5UJ5"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:5UJ5"
FT   HELIX           35..42
FT                   /evidence="ECO:0007829|PDB:5UJ5"
FT   HELIX           65..71
FT                   /evidence="ECO:0007829|PDB:5UJ5"
FT   HELIX           76..83
FT                   /evidence="ECO:0007829|PDB:5UJ5"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:5UJ5"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:5UJ5"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:5UJ5"
SQ   SEQUENCE   128 AA;  14060 MW;  D22B4EEE19BAD3CF CRC64;
     MDMFSAPDRI PEQIRIFFKT MKQVVPAKAV CGSTVLDVAH KNGVDLEGAC EGNLACSTCH
     VILEEPLYRK LGEPSDKEYD LIDQAFGATG TSRLGCQLRV DKSFENAVFT VPRATKNMAV
     DGFKPKPH