FER_THEVB
ID FER_THEVB Reviewed; 98 AA.
AC P0A3C9; P00256; P95742;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ferredoxin-1;
DE AltName: Full=Ferredoxin I;
GN Name=petF1; Synonyms=petF; OrderedLocusNames=tsl1009;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP PROTEIN SEQUENCE OF 2-98.
RA Hase T., Matsubara H., Koike H., Katoh S.;
RT "Amino acid sequence of ferredoxin from a thermophilic blue-green alga,
RT Synechococcus sp.";
RL Biochim. Biophys. Acta 744:46-52(1983).
RN [3]
RP STRUCTURE BY NMR, AND MASS SPECTROMETRY.
RX PubMed=8841126; DOI=10.1021/bi961144m;
RA Baumann B., Sticht H., Schaerpf M., Sutter M., Haehnel W., Roesch P.;
RT "Structure of Synechococcus elongatus [Fe2S2] ferredoxin in solution.";
RL Biochemistry 35:12831-12841(1996).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=9180381; DOI=10.1006/jmbi.1997.1001;
RA Hatanaka H., Tanimura R., Katoh S., Inagaki F.;
RT "Solution structure of ferredoxin from the thermophilic cyanobacterium
RT Synechococcus elongatus and its thermostability.";
RL J. Mol. Biol. 268:922-933(1997).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC reductase (FTR) and thioredoxin. {ECO:0000250}.
CC -!- INTERACTION:
CC P0A3C9; Q8DLW1: ho1; NbExp=2; IntAct=EBI-766786, EBI-6947306;
CC P0A3C9; Q8DK70: ispG; NbExp=3; IntAct=EBI-766786, EBI-766800;
CC -!- MASS SPECTROMETRY: Mass=10715.7; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8841126};
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; BA000039; BAC08561.1; -; Genomic_DNA.
DR PIR; A00259; FEYCT.
DR RefSeq; NP_681799.1; NC_004113.1.
DR RefSeq; WP_011056851.1; NC_004113.1.
DR PDB; 1ROE; NMR; -; A=2-98.
DR PDB; 2CJN; NMR; -; A=2-98.
DR PDB; 2CJO; NMR; -; A=2-98.
DR PDB; 5AUI; X-ray; 1.50 A; A=2-98.
DR PDB; 5ZF0; X-ray; 4.20 A; P1/P2/P3/P4/P5/P6=2-98.
DR PDB; 6JO2; X-ray; 1.55 A; A=2-98.
DR PDB; 6KHI; EM; 3.00 A; 1=1-98.
DR PDB; 6L7O; EM; 3.20 A; R=1-98.
DR PDBsum; 1ROE; -.
DR PDBsum; 2CJN; -.
DR PDBsum; 2CJO; -.
DR PDBsum; 5AUI; -.
DR PDBsum; 5ZF0; -.
DR PDBsum; 6JO2; -.
DR PDBsum; 6KHI; -.
DR PDBsum; 6L7O; -.
DR AlphaFoldDB; P0A3C9; -.
DR SMR; P0A3C9; -.
DR IntAct; P0A3C9; 4.
DR MINT; P0A3C9; -.
DR STRING; 197221.22294732; -.
DR EnsemblBacteria; BAC08561; BAC08561; BAC08561.
DR KEGG; tel:tsl1009; -.
DR PATRIC; fig|197221.4.peg.1059; -.
DR eggNOG; COG1018; Bacteria.
DR OMA; CAARMIS; -.
DR OrthoDB; 1885467at2; -.
DR EvolutionaryTrace; P0A3C9; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR010241; Fd_pln.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR02008; fdx_plant; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..98
FT /note="Ferredoxin-1"
FT /id="PRO_0000189372"
FT DOMAIN 4..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 41
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 79
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:5AUI"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1ROE"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:5AUI"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:5AUI"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:5AUI"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:5AUI"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2CJN"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:5AUI"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5AUI"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5AUI"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:5AUI"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:5AUI"
SQ SEQUENCE 98 AA; 10847 MW; DE8198FFB127C7AF CRC64;
MATYKVTLVR PDGSETTIDV PEDEYILDVA EEQGLDLPFS CRAGACSTCA GKLLEGEVDQ
SDQSFLDDDQ IEKGFVLTCV AYPRSDCKIL TNQEEELY
