ID C4KF47_SULIK Unreviewed; 104 AA.
AC C4KF47;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Zinc-containing ferredoxin {ECO:0000256|PIRNR:PIRNR000068};
GN OrderedLocusNames=M164_2718 {ECO:0000313|EMBL:ACR43310.1};
OS Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR43310.1, ECO:0000313|Proteomes:UP000001479};
RN [1] {ECO:0000313|EMBL:ACR43310.1, ECO:0000313|Proteomes:UP000001479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC {ECO:0000256|PIRNR:PIRNR000068}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR000068,
CC ECO:0000256|PIRSR:PIRSR000068-1};
CC Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR000068,
CC ECO:0000256|PIRSR:PIRSR000068-1};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|PIRNR:PIRNR000068,
CC ECO:0000256|PIRSR:PIRSR000068-1};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|PIRNR:PIRNR000068,
CC ECO:0000256|PIRSR:PIRSR000068-1};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRNR:PIRNR000068,
CC ECO:0000256|PIRSR:PIRSR000068-1};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|PIRNR:PIRNR000068,
CC ECO:0000256|PIRSR:PIRSR000068-1};
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DR EMBL; CP001402; ACR43310.1; -; Genomic_DNA.
DR RefSeq; WP_012712645.1; NC_012726.1.
DR AlphaFoldDB; C4KF47; -.
DR GeneID; 8762896; -.
DR KEGG; sid:M164_2718; -.
DR HOGENOM; CLU_178207_0_0_2; -.
DR Proteomes; UP000001479; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009157; Fd_Zn-bd.
DR PANTHER; PTHR43687; ADENYLYLSULFATE REDUCTASE, BETA SUBUNIT; 1.
DR PANTHER; PTHR43687:SF1; L-ASPARTATE SEMIALDEHYDE SULFURTRANSFERASE IRON-SULFUR SUBUNIT; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR PIRSF; PIRSF000068; Zn_Fdx_Sulfol; 1.
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|PIRNR:PIRNR000068, ECO:0000256|PIRSR:PIRSR000068-1};
KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR000068, ECO:0000256|PIRSR:PIRSR000068-1};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000068};
KW Iron {ECO:0000256|PIRNR:PIRNR000068, ECO:0000256|PIRSR:PIRSR000068-1};
KW Iron-sulfur {ECO:0000256|PIRNR:PIRNR000068, ECO:0000256|PIRSR:PIRSR000068-
KW 1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000068,
KW ECO:0000256|PIRSR:PIRSR000068-1}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000068};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR000068}.
FT DOMAIN 36..66
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 75..104
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
FT BINDING 46
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
FT BINDING 52
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
FT BINDING 84
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
FT BINDING 90
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
FT BINDING 94
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000068-1"
SQ SEQUENCE 104 AA; 11072 MW; B61E7C5833B3B651 CRC64;
MGIDPNYRTN FPVSGEHSGH KIYGTVEPPA KLGIHGTIVG VDFDLCIADG SCINACPVNV
FQWYDTPGHP ASEKKADPVN EQACIFCMAC VNVCPVAAID VKPP
//