ID A0A1M6AKI2_9FLAO Unreviewed; 76 AA.
AC A0A1M6AKI2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU368020};
GN ORFNames=IMZ16_05490 {ECO:0000313|EMBL:QOR73001.1},
GN SAMN05443429_101322 {ECO:0000313|EMBL:SHI36941.1};
OS Cruoricaptor ignavus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Cruoricaptor.
OX NCBI_TaxID=1118202 {ECO:0000313|EMBL:SHI36941.1, ECO:0000313|Proteomes:UP000184335};
RN [1] {ECO:0000313|EMBL:SHI36941.1, ECO:0000313|Proteomes:UP000184335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25479 {ECO:0000313|EMBL:SHI36941.1,
RC ECO:0000313|Proteomes:UP000184335};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QOR73001.1, ECO:0000313|Proteomes:UP000593605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1214 {ECO:0000313|EMBL:QOR73001.1,
RC ECO:0000313|Proteomes:UP000593605};
RA Guglielmino C.J.D.;
RT "Complete genome of Cruoricapor ignavus strain M1214 isolated from the
RT blood culture of a febrile patient.";
RL Submitted (OCT-2020) 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:RU368020}.
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DR EMBL; CP063145; QOR73001.1; -; Genomic_DNA.
DR EMBL; FQYI01000001; SHI36941.1; -; Genomic_DNA.
DR RefSeq; WP_073177666.1; NZ_FQYI01000001.1.
DR AlphaFoldDB; A0A1M6AKI2; -.
DR STRING; 1118202.SAMN05443429_101322; -.
DR KEGG; civ:IMZ16_05490; -.
DR OrthoDB; 1524937at2; -.
DR Proteomes; UP000184335; Unassembled WGS sequence.
DR Proteomes; UP000593605; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR001080; 3Fe4S_ferredoxin.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR PANTHER; PTHR36923; FERREDOXIN; 1.
DR PANTHER; PTHR36923:SF3; FERREDOXIN; 1.
DR Pfam; PF13370; Fer4_13; 1.
DR PRINTS; PR00352; 3FE4SFRDOXIN.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU368020};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU368020};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU368020};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368020};
KW Reference proteome {ECO:0000313|Proteomes:UP000184335};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368020}.
FT DOMAIN 2..30
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 76 AA; 8584 MW; BDEAE3D2CCED468D CRC64;
MVIVTLQREK CIGCNYCAEF APEFFRMSKK DGKSVLLKST EKKGFHTLKT PLHHAFEPCE
KAAKACPVNI ITVKEI
//