FER3_TRIV2
ID FER3_TRIV2 Reviewed; 98 AA.
AC P46050; Q3M578;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ferredoxin-3;
DE AltName: Full=Ferredoxin III;
DE Short=FdIII;
GN Name=fdxB; OrderedLocusNames=Ava_4259;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8709854; DOI=10.1111/j.1365-2958.1995.mmi_18020357.x;
RA Schrautemeier B., Neveling U., Schmitz S.;
RT "Distinct and differently regulated Mo-dependent nitrogen-fixing systems
RT evolved for heterocysts and vegetative cells of Anabaena variabilis ATCC
RT 29413: characterization of the fdxH1/2 gene regions as part of the nif1/2
RT gene clusters.";
RL Mol. Microbiol. 18:357-369(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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; Z46890; CAA86992.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA23858.1; -; Genomic_DNA.
DR PIR; S70250; S70250.
DR AlphaFoldDB; P46050; -.
DR SMR; P46050; -.
DR STRING; 240292.Ava_4259; -.
DR EnsemblBacteria; ABA23858; ABA23858; Ava_4259.
DR KEGG; ava:Ava_4259; -.
DR eggNOG; COG1145; Bacteria.
DR HOGENOM; CLU_155272_0_0_3; -.
DR OMA; EYCIGCQ; -.
DR Proteomes; UP000002533; Chromosome.
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 Pfam; PF12838; Fer4_7; 1.
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..98
FT /note="Ferredoxin-3"
FT /id="PRO_0000159186"
FT DOMAIN 18..47
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 66..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 98 AA; 10866 MW; 268AF7E0CD735AA9 CRC64;
MATLTGLTFG GQVWTPQFVE AVNQDKCIGC GRCFKACGRN VLILQALNEN GEFVEDEEGE
EIERKVMSII HPEYCIGCQA CARACPKNCY THSPLEHN