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Database: UniProt
Entry: A0A399CVM2_9BACT
LinkDB: A0A399CVM2_9BACT
Original site: A0A399CVM2_9BACT 
ID   A0A399CVM2_9BACT        Unreviewed;        56 AA.
AC   A0A399CVM2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU365098};
GN   ORFNames=D1164_19515 {ECO:0000313|EMBL:RIH63467.1};
OS   Mariniphaga sediminis.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Mariniphaga.
OX   NCBI_TaxID=1628158 {ECO:0000313|EMBL:RIH63467.1, ECO:0000313|Proteomes:UP000266441};
RN   [1] {ECO:0000313|EMBL:RIH63467.1, ECO:0000313|Proteomes:UP000266441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY21 {ECO:0000313|EMBL:RIH63467.1,
RC   ECO:0000313|Proteomes:UP000266441};
RX   PubMed=26012581; DOI=10.1099/ijs.0.000354;
RA   Wang F.Q., Shen Q.Y., Chen G.J., Du Z.J.;
RT   "Mariniphaga sediminis sp. nov., isolated from coastal sediment.";
RL   Int. J. Syst. Evol. Microbiol. 65:2908-2912(2015).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions.
CC       {ECO:0000256|RuleBase:RU365098}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU365098};
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:RIH63467.1}.
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DR   EMBL; QWET01000020; RIH63467.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A399CVM2; -.
DR   OrthoDB; 9803397at2; -.
DR   Proteomes; UP000266441; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR43687; ADENYLYLSULFATE REDUCTASE, BETA SUBUNIT; 1.
DR   PANTHER; PTHR43687:SF1; L-ASPARTATE SEMIALDEHYDE SULFURTRANSFERASE IRON-SULFUR SUBUNIT; 1.
DR   Pfam; PF00037; Fer4; 2.
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   4Fe-4S {ECO:0000256|RuleBase:RU365098};
KW   Electron transport {ECO:0000256|RuleBase:RU365098};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365098};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266441};
KW   Transport {ECO:0000256|RuleBase:RU365098}.
FT   DOMAIN          1..25
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          28..56
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   56 AA;  5882 MW;  CE51F1AA80281FDA CRC64;
     MAYKISDECI ACGTCIDECP VDAISEGDIY VIDADLCTDC GSCAEVCPVE AISVEE
//
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