FER_THEMA
ID FER_THEMA Reviewed; 60 AA.
AC P46797;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ferredoxin;
GN Name=fdx; OrderedLocusNames=TM_0927;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=8168477; DOI=10.1002/j.1460-2075.1994.tb06445.x;
RA Darimont B., Sterner R.;
RT "Sequence, assembly and evolution of a primordial ferredoxin from
RT Thermotoga maritima.";
RL EMBO J. 13:1772-1781(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RX PubMed=8939753; DOI=10.1016/s0969-2126(96)00137-2;
RA Macedo-Ribeiro S., Darimont B., Sterner R., Huber R.;
RT "Small structural changes account for the high thermostability of 1[4Fe-4S]
RT ferredoxin from the hyperthermophilic bacterium Thermotoga maritima.";
RL Structure 4:1291-1301(1996).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=8647119; DOI=10.1111/j.1432-1033.1996.0726p.x;
RA Sticht H., Wildegger G., Bentrop D., Darimont B., Sterner R., Roesch P.;
RT "An NMR-derived model for the solution structure of oxidized Thermotoga
RT maritima 1[Fe4-S4] ferredoxin.";
RL Eur. J. Biochem. 237:726-735(1996).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster.;
CC -!- SUBUNIT: Monomer.
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DR EMBL; X82178; CAA57669.1; -; Genomic_DNA.
DR EMBL; U24145; AAA65437.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36008.1; -; Genomic_DNA.
DR PIR; S44350; S44350.
DR RefSeq; NP_228735.1; NC_000853.1.
DR RefSeq; WP_004080635.1; NZ_CP011107.1.
DR PDB; 1ROF; NMR; -; A=1-60.
DR PDB; 1VJW; X-ray; 1.75 A; A=1-60.
DR PDBsum; 1ROF; -.
DR PDBsum; 1VJW; -.
DR AlphaFoldDB; P46797; -.
DR SMR; P46797; -.
DR STRING; 243274.THEMA_09715; -.
DR EnsemblBacteria; AAD36008; AAD36008; TM_0927.
DR KEGG; tma:TM0927; -.
DR eggNOG; COG1141; Bacteria.
DR InParanoid; P46797; -.
DR OMA; DVFEMND; -.
DR OrthoDB; 1873445at2; -.
DR EvolutionaryTrace; P46797; -.
DR Proteomes; UP000008183; Chromosome.
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:0005506; F:iron ion binding; IEA:InterPro.
DR InterPro; IPR001080; 3Fe4S_ferredoxin.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR PRINTS; PR00352; 3FE4SFRDOXIN.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Disulfide bond;
KW Electron transport; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..60
FT /note="Ferredoxin"
FT /id="PRO_0000159203"
FT DOMAIN 2..29
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 30..60
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 10
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:8939753"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:8939753"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:8939753"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:8939753"
FT DISULFID 20..43
FT /evidence="ECO:0000269|PubMed:8939753"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1ROF"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1VJW"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:1VJW"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1VJW"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1VJW"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1VJW"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:1VJW"
SQ SEQUENCE 60 AA; 6213 MW; A00A03A13FDF1690 CRC64;
MKVRVDADAC IGCGVCENLC PDVFQLGDDG KAKVLQPETD LPCAKDAADS CPTGAISVEE
