FER1_NOSS1
ID FER1_NOSS1 Reviewed; 99 AA.
AC P0A3C7; P06543;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Ferredoxin-1;
DE AltName: Full=Ferredoxin I;
GN Name=petF; Synonyms=fdxV; OrderedLocusNames=all4148;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2430949; DOI=10.1128/jb.168.3.1265-1271.1986;
RA Alam J., Whitaker R.A., Krogmann D.W., Curtis S.E.;
RT "Isolation and sequence of the gene for ferredoxin I from the
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL J. Bacteriol. 168:1265-1271(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP PROTEIN SEQUENCE OF 6-16, AND MASS SPECTROMETRY.
RA Singh H., Rajaram H., Apte S.K.;
RL Submitted (DEC-2008) to UniProtKB.
RN [4]
RP MUTAGENESIS.
RX PubMed=8369305; DOI=10.1021/bi00087a013;
RA Hurley J.K., Salamon Z., Meyer T.E., Fitch J.C., Cusanovich M.A.,
RA Markley J.L., Cheng H., Xia B., Chae Y.K., Medina M., Gomez-Moreno C.,
RA Tollin G.;
RT "Amino acid residues in Anabaena ferredoxin crucial to interaction with
RT ferredoxin-NADP+ reductase: site-directed mutagenesis and laser flash
RT photolysis.";
RL Biochemistry 32:9346-9354(1993).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=2354171; DOI=10.1021/bi00468a029;
RA Oh B.-H., Markley J.L.;
RT "Multinuclear magnetic resonance studies of the 2Fe.2S* ferredoxin from
RT Anabaena species strain PCC 7120. 1. Sequence-specific hydrogen-1 resonance
RT assignments and secondary structure in solution of the oxidized form.";
RL Biochemistry 29:3993-4004(1990).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=2354172; DOI=10.1021/bi00468a030;
RA Oh B.-H., Mooberry E.S., Markley J.L.;
RT "Multinuclear magnetic resonance studies of the 2Fe.2S* ferredoxin from
RT Anabaena species strain PCC 7120. 2. Sequence-specific carbon-13 and
RT nitrogen-15 resonance assignments of the oxidized form.";
RL Biochemistry 29:4004-4011(1990).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND IRON-SULFUR CLUSTER-BINDING
RP SITES CYS-42; CYS-47; CYS-50 AND CYS-80.
RX PubMed=1902376; DOI=10.1021/bi00231a003;
RA Rypniewski W.R., Breiter D.R., Benning M.M., Wesenberg G., Oh B.-H.,
RA Markley J.L., Rayment I., Holden H.M.;
RT "Crystallization and structure determination to 2.5-A resolution of the
RT oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120.";
RL Biochemistry 30:4126-4131(1991).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9287153; DOI=10.1021/bi9709001;
RA Hurley J.K., Weber-Main A.M., Stankovich M.T., Benning M.M., Thoden J.B.,
RA Vanhooke J.L., Holden H.M., Chae Y.K., Xia B., Cheng H., Markley J.L.,
RA Martinez-Julvez M., Gomez-Moreno C., Schmeits J.L., Tollin G.;
RT "Structure-function relationships in Anabaena ferredoxin: correlations
RT between X-ray crystal structures, reduction potentials, and rate constants
RT of electron transfer to ferredoxin:NADP+ reductase for site-specific
RT ferredoxin mutants.";
RL Biochemistry 36:11100-11117(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 -!- MASS SPECTROMETRY: Mass=10921; Method=MALDI;
CC Evidence={ECO:0000269|Ref.3};
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; M14737; AAA22021.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB75847.1; -; Genomic_DNA.
DR PIR; AE2324; AE2324.
DR PIR; S25233; S25233.
DR RefSeq; WP_010998287.1; NZ_RSCN01000010.1.
DR PDB; 1FXA; X-ray; 2.50 A; A/B=2-99.
DR PDB; 1J7A; X-ray; 1.80 A; A=2-99.
DR PDB; 1J7B; X-ray; 1.80 A; A=2-99.
DR PDB; 1J7C; X-ray; 1.80 A; A=2-99.
DR PDB; 1QOA; X-ray; 1.70 A; A/B=2-99.
DR PDB; 1QOB; X-ray; 1.80 A; A/B=2-99.
DR PDB; 1QOF; X-ray; 1.80 A; A/B=2-99.
DR PDB; 1QOG; X-ray; 1.80 A; A/B=2-99.
DR PDBsum; 1FXA; -.
DR PDBsum; 1J7A; -.
DR PDBsum; 1J7B; -.
DR PDBsum; 1J7C; -.
DR PDBsum; 1QOA; -.
DR PDBsum; 1QOB; -.
DR PDBsum; 1QOF; -.
DR PDBsum; 1QOG; -.
DR AlphaFoldDB; P0A3C7; -.
DR BMRB; P0A3C7; -.
DR SMR; P0A3C7; -.
DR STRING; 103690.17133283; -.
DR EnsemblBacteria; BAB75847; BAB75847; BAB75847.
DR KEGG; ana:all4148; -.
DR eggNOG; COG0633; Bacteria.
DR OMA; CAARMIS; -.
DR OrthoDB; 1885467at2; -.
DR EvolutionaryTrace; P0A3C7; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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:0000250"
FT CHAIN 2..99
FT /note="Ferredoxin-1"
FT /id="PRO_0000189300"
FT DOMAIN 4..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 80
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT MUTAGEN 43
FT /note="R->A,E,H: No effect on electron transfer."
FT /evidence="ECO:0000269|PubMed:8369305"
FT MUTAGEN 49
FT /note="T->A: No effect on electron transfer."
FT /evidence="ECO:0000269|PubMed:8369305"
FT MUTAGEN 66
FT /note="F->A,I: 1000-fold decrease in electron transfer."
FT /evidence="ECO:0000269|PubMed:8369305"
FT MUTAGEN 69
FT /note="D->K: Small effect on electron transfer."
FT /evidence="ECO:0000269|PubMed:8369305"
FT MUTAGEN 70
FT /note="D->K: Small effect on electron transfer."
FT /evidence="ECO:0000269|PubMed:8369305"
FT MUTAGEN 95
FT /note="E->K: 20000-fold decrease in electron transfer."
FT /evidence="ECO:0000269|PubMed:8369305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1QOA"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:1QOA"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1QOA"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:1QOA"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1QOA"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1QOA"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1QOA"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1QOA"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1QOA"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1QOA"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1QOA"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1QOA"
SQ SEQUENCE 99 AA; 10830 MW; 874FD6365346BFFF CRC64;
MATFKVTLIN EAEGTKHEIE VPDDEYILDA AEEQGYDLPF SCRAGACSTC AGKLVSGTVD
QSDQSFLDDD QIEAGYVLTC VAYPTSDVVI QTHKEEDLY
