FER_METTL
ID FER_METTL Reviewed; 60 AA.
AC P21305;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Ferredoxin;
OS Methanothermococcus thermolithotrophicus (Methanococcus
OS thermolithotrophicus).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanothermococcus.
OX NCBI_TaxID=2186;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1986796; DOI=10.1016/0167-4838(91)90222-l;
RA Bruschi M., Bonicel J., Hatchikian E.C., Fardeau M.L., Belaich J.-P.,
RA Frey M.;
RT "Amino acid sequence and molecular modelling of a thermostable two (4Fe-4S)
RT ferredoxin from the archaebacterium Methanococcus thermolithotrophicus.";
RL Biochim. Biophys. Acta 1076:79-85(1991).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC probably in the CO-dehydrogenase complex.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 2 [4Fe-4S] clusters.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable.;
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DR PIR; S13476; S13476.
DR AlphaFoldDB; P21305; -.
DR SMR; P21305; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF13187; Fer4_9; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Repeat; Transport.
FT CHAIN 1..60
FT /note="Ferredoxin"
FT /id="PRO_0000159154"
FT DOMAIN 2..30
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 31..60
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 9
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 60 AA; 6539 MW; 3092B3AF9D2C5CE2 CRC64;
SVTIDYDKCK GPECAECVNA CPMEVFEIQG DKVVVAKEDD CTFCMVCVDV CPTDAITVKE