ID   FER_SACER               Reviewed;         106 AA.
AC   P24496;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Ferredoxin;
GN   Name=fdxA;
OS   Saccharopolyspora erythraea (Streptomyces erythraeus).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=1836;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WHM22;
RX   PubMed=2055472; DOI=10.1016/0378-1119(91)90372-i;
RA   Donadio S., Hutchinson C.R.;
RT   "Cloning and characterization of the Saccharopolyspora erythraea fdxA gene
RT   encoding ferredoxin.";
RL   Gene 100:231-235(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=CA340;
RX   PubMed=3127376; DOI=10.1128/jb.170.4.1548-1553.1988;
RA   Shafiee A., Hutchinson C.R.;
RT   "Purification and reconstitution of the electron transport components for
RT   6-deoxyerythronolide B hydroxylase, a cytochrome P-450 enzyme of macrolide
RT   antibiotic (erythromycin) biosynthesis.";
RL   J. Bacteriol. 170:1548-1553(1988).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster.;
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC       Note=Binds 1 [3Fe-4S] cluster.;
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DR   EMBL; M61119; AAA92023.1; -; Genomic_DNA.
DR   PIR; JH0239; JH0239.
DR   RefSeq; WP_009949328.1; NZ_CP069353.1.
DR   AlphaFoldDB; P24496; -.
DR   SMR; P24496; -.
DR   PRIDE; P24496; -.
DR   OMA; DRMLYIH; -.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR000813; 7Fe_ferredoxin.
DR   Pfam; PF00037; Fer4; 1.
DR   PRINTS; PR00354; 7FE8SFRDOXIN.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   3Fe-4S; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Repeat; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3127376"
FT   CHAIN           2..106
FT                   /note="Ferredoxin"
FT                   /id="PRO_0000159103"
FT   DOMAIN          31..60
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   REGION          84..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         9
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   106 AA;  11538 MW;  1647105FF97C9516 CRC64;
     MTYVIAEPCV DVLDKACIEE CPVDCIYEGG RMLYIHPDEC VDCGACEPVC PVEAIYYEDD
     VPDEWAAYTK ANVDFFDELG SPGGAAKVGK VDRDVEPVSS LPPQGE