ID F9S8V2_9VIBR Unreviewed; 107 AA.
AC F9S8V2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU364098};
GN ORFNames=VII00023_09264 {ECO:0000313|EMBL:EGU29589.1};
OS Vibrio ichthyoenteri ATCC 700023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=870968 {ECO:0000313|EMBL:EGU29589.1, ECO:0000313|Proteomes:UP000004605};
RN [1] {ECO:0000313|EMBL:EGU29589.1, ECO:0000313|Proteomes:UP000004605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700023 {ECO:0000313|EMBL:EGU29589.1,
RC ECO:0000313|Proteomes:UP000004605};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU29589.1}.
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DR EMBL; AFWF01000320; EGU29589.1; -; Genomic_DNA.
DR RefSeq; WP_006714874.1; NZ_AFWF01000320.1.
DR AlphaFoldDB; F9S8V2; -.
DR OrthoDB; 9803397at2; -.
DR Proteomes; UP000004605; Unassembled WGS sequence.
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; 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; PF13187; Fer4_9; 1.
DR PRINTS; PR00354; 7FE8SFRDOXIN.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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|RuleBase:RU364098};
KW Iron-sulfur {ECO:0000256|RuleBase:RU364098};
KW Metal-binding {ECO:0000256|RuleBase:RU364098};
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"
SQ SEQUENCE 107 AA; 11971 MW; B8F55B6C23204F7A CRC64;
MAFVVTDNCI QCKYTDCVAV CPADAFHEGP NFMVINPIEC IDCGLCVDEC AAQAIFQEDE
LSDDQQVFIE LNAELAEIWP VQTEVKPAMD DAEQWNGVPN KLDKLER
//
