FER3_LEPBY
ID FER3_LEPBY Reviewed; 96 AA.
AC P46036;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ferredoxin-3;
DE AltName: Full=Ferredoxin III;
DE Short=FdIII;
GN Name=fdxB;
OS Leptolyngbya boryana (Plectonema boryanum).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Leptolyngbyaceae; Leptolyngbya.
OX NCBI_TaxID=1184;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 18200 / UTEX 594 / PCC 73110;
RX PubMed=8106314; DOI=10.1128/jb.176.4.1037-1046.1994;
RA Schrautemeier B., Cassing A., Boehme H.;
RT "Characterization of the genome region encoding an fdxH-type ferredoxin and
RT a new 2[4Fe-4S] ferredoxin from the nonheterocystous, nitrogen-fixing
RT cyanobacterium Plectonema boryanum PCC 73110.";
RL J. Bacteriol. 176:1037-1046(1994).
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; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; X71865; CAA50700.1; -; Genomic_DNA.
DR PIR; D49890; D49890.
DR AlphaFoldDB; P46036; -.
DR SMR; P46036; -.
DR PRIDE; P46036; -.
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:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR014283; FdIII_4_nif.
DR TIGRFAMs; TIGR02936; fdxN_nitrog; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Repeat; Transport.
FT CHAIN 1..96
FT /note="Ferredoxin-3"
FT /id="PRO_0000159187"
FT DOMAIN 18..47
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 65..95
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 27
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 96 AA; 10694 MW; 2970C67DF4B438B5 CRC64;
MATLTNVTFG GTAWIPQFVQ SINQTKCIGC GRCFKACGRD VLALKALNDE GEWVEDEDDE
EIERKVMTIA NRDKCIGCEA CSRVCPKNCY THESLN