FER_SYNY3
ID FER_SYNY3 Reviewed; 97 AA.
AC P27320;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ferredoxin-1;
DE AltName: Full=Ferredoxin I;
GN Name=petF; Synonyms=fed; OrderedLocusNames=ssl0020;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nakamoto H., Suzuki T.;
RT "Cloning, characterization and transcriptional studies of ferredoxin genes
RT from the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and the
RT thermophilic cyanobacterium Synechococcus vulcanus.";
RL Physiol. Plantarum 101:199-205(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9305771; DOI=10.1016/s0378-1119(97)00165-0;
RA Cassier-Chauvat C., Poncelet M., Chauvat F.;
RT "Three insertion sequences from the cyanobacterium Synechocystis PCC6803
RT support the occurrence of horizontal DNA transfer among bacteria.";
RL Gene 195:257-266(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [5]
RP PROTEIN SEQUENCE OF 2-97.
RX PubMed=1633177; DOI=10.1016/0167-4838(92)90465-p;
RA Bottin H., Lagoutte B.;
RT "Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp PCC
RT 6803.";
RL Biochim. Biophys. Acta 1101:48-56(1992).
RN [6]
RP PROTEIN SEQUENCE OF 2-15.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=7578051; DOI=10.1021/bi00044a024;
RA Lelong C., Setif P., Bottin H., Andre F., Neumann J.-M.;
RT "1H and 15N NMR sequential assignment, secondary structure, and tertiary
RT fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC 6803.";
RL Biochemistry 34:14462-14473(1995).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-97 IN COMPLEXES WITH FTRC; FTRV
RP AND TRX-F, AND SUBUNIT.
RX PubMed=17611542; DOI=10.1038/nature05937;
RA Dai S., Friemann R., Glauser D.A., Bourquin F., Manieri W., Schurmann P.,
RA Eklund H.;
RT "Structural snapshots along the reaction pathway of ferredoxin-thioredoxin
RT reductase.";
RL Nature 448:92-96(2007).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -412 mV.;
CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC reductase (FTR) and thioredoxin. {ECO:0000269|PubMed:17611542}.
CC -!- INTERACTION:
CC P27320; Q55389: ftrC; NbExp=4; IntAct=EBI-863421, EBI-863211;
CC P27320; Q55781: ftrV; NbExp=4; IntAct=EBI-863421, EBI-863219;
CC P27320; P19569: psaD; NbExp=3; IntAct=EBI-863421, EBI-595298;
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; D85607; BAA24020.1; -; Genomic_DNA.
DR EMBL; U38802; AAB72025.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10197.1; -; Genomic_DNA.
DR PIR; S76345; FEYB6.
DR PDB; 1DOX; NMR; -; A=2-97.
DR PDB; 1DOY; NMR; -; A=2-97.
DR PDB; 1OFF; X-ray; 1.80 A; A=2-97.
DR PDB; 2KAJ; NMR; -; A=2-97.
DR PDB; 2PVG; X-ray; 2.40 A; C=2-97.
DR PDB; 2PVO; X-ray; 3.40 A; D=2-97.
DR PDB; 5AUK; X-ray; 1.62 A; A=2-97.
DR PDBsum; 1DOX; -.
DR PDBsum; 1DOY; -.
DR PDBsum; 1OFF; -.
DR PDBsum; 2KAJ; -.
DR PDBsum; 2PVG; -.
DR PDBsum; 2PVO; -.
DR PDBsum; 5AUK; -.
DR AlphaFoldDB; P27320; -.
DR BMRB; P27320; -.
DR SMR; P27320; -.
DR DIP; DIP-35027N; -.
DR IntAct; P27320; 7.
DR MINT; P27320; -.
DR STRING; 1148.1001570; -.
DR PaxDb; P27320; -.
DR EnsemblBacteria; BAA10197; BAA10197; BAA10197.
DR KEGG; syn:ssl0020; -.
DR eggNOG; COG1018; Bacteria.
DR InParanoid; P27320; -.
DR OMA; CAARMIS; -.
DR PhylomeDB; P27320; -.
DR EvolutionaryTrace; P27320; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
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; Disulfide bond;
KW Electron transport; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1633177,
FT ECO:0000269|PubMed:9298645"
FT CHAIN 2..97
FT /note="Ferredoxin-1"
FT /id="PRO_0000189381"
FT DOMAIN 4..94
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:7578051"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:7578051"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:7578051"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:7578051"
FT DISULFID 19..86
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="S -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:5AUK"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:5AUK"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:5AUK"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:5AUK"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:5AUK"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1DOX"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:5AUK"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5AUK"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:5AUK"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:5AUK"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5AUK"
SQ SEQUENCE 97 AA; 10363 MW; 137FFD4F87A66DA1 CRC64;
MASYTVKLIT PDGESSIECS DDTYILDAAE EAGLDLPYSC RAGACSTCAG KITAGSVDQS
DQSFLDDDQI EAGYVLTCVA YPTSDCTIET HKEEDLY
