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Database: UniProt
Entry: A0A2K8K8Y5_9RHOB
LinkDB: A0A2K8K8Y5_9RHOB
Original site: A0A2K8K8Y5_9RHOB 
ID   A0A2K8K8Y5_9RHOB        Unreviewed;       112 AA.
AC   A0A2K8K8Y5;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU364098};
GN   ORFNames=BG454_08790 {ECO:0000313|EMBL:ATX65912.1};
OS   Rhodobaca barguzinensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobaca.
OX   NCBI_TaxID=441209 {ECO:0000313|EMBL:ATX65912.1, ECO:0000313|Proteomes:UP000228948};
RN   [1] {ECO:0000313|EMBL:ATX65912.1, ECO:0000313|Proteomes:UP000228948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=alga05 {ECO:0000313|Proteomes:UP000228948};
RA   Kopejtka K., Tomasch J.M., Bunk B., Koblizek M.;
RT   "Revised Sequence and Annotation of the Rhodobaca barguzinensis strain
RT   alga05 Genome.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions.
CC       {ECO:0000256|RuleBase:RU364098}.
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|ARBA:ARBA00001927,
CC         ECO:0000256|RuleBase:RU364098};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU364098};
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DR   EMBL; CP024899; ATX65912.1; -; Genomic_DNA.
DR   RefSeq; WP_071480451.1; NZ_SODJ01000003.1.
DR   AlphaFoldDB; A0A2K8K8Y5; -.
DR   STRING; 441209.GCA_001870665_01535; -.
DR   KEGG; rbg:BG454_08790; -.
DR   OrthoDB; 9803397at2; -.
DR   Proteomes; UP000228948; Chromosome.
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   Gene3D; 3.30.70.20; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR000813; 7Fe_ferredoxin.
DR   InterPro; IPR022569; Fd_C.
DR   PANTHER; PTHR42859:SF2; FERREDOXIN; 1.
DR   PANTHER; PTHR42859; OXIDOREDUCTASE; 1.
DR   Pfam; PF11953; DUF3470; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   PRINTS; PR00354; 7FE8SFRDOXIN.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|RuleBase:RU364098};
KW   4Fe-4S {ECO:0000256|RuleBase:RU364098};
KW   Electron transport {ECO:0000256|RuleBase:RU364098};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364098};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000228948};
KW   Repeat {ECO:0000256|RuleBase:RU364098};
KW   Transport {ECO:0000256|RuleBase:RU364098}.
FT   DOMAIN          1..30
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          31..60
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          84..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   112 AA;  12790 MW;  D5A845559AF65276 CRC64;
     MTYVVIDNCI ACKYTDCVEV CPVDCFYEGE NMLVIHPDEC IDCGVCEPEC PADAIRPDTE
     PEMEQWVEFN RKYSEKWPVI ITKKDPLPEA TERDGETDKL NKYFSENPGE GG
//
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