ID A0A133VA51_9EURY Unreviewed; 67 AA.
AC A0A133VA51;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU368020};
GN ORFNames=AKJ45_01880 {ECO:0000313|EMBL:KXB03316.1};
OS candidate division MSBL1 archaeon SCGC-AAA261F19.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698275 {ECO:0000313|EMBL:KXB03316.1, ECO:0000313|Proteomes:UP000070565};
RN [1] {ECO:0000313|EMBL:KXB03316.1, ECO:0000313|Proteomes:UP000070565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA261F19 {ECO:0000313|EMBL:KXB03316.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC {ECO:0000256|RuleBase:RU368020}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KXB03316.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LHXZ01000019; KXB03316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133VA51; -.
DR Proteomes; UP000070565; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR001080; 3Fe4S_ferredoxin.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; PR00352; 3FE4SFRDOXIN.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:UP000070565};
KW Transport {ECO:0000256|RuleBase:RU368020}.
FT DOMAIN 12..41
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 49..67
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 67 AA; 7266 MW; 9289FDE13F31957F CRC64;
MLLVSLRFLE DLKMKVDRDK CISCGACSSV CPSDAIEVPS RGVRVLGVCT NCRLCIKACP
MGAMEIE
//