FER1_SYNP6
ID FER1_SYNP6 Reviewed; 99 AA.
AC P0A3D3; P06517;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ferredoxin-1;
DE AltName: Full=Ferredoxin I;
GN Name=petF1; OrderedLocusNames=syc2484_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA van der Plas J., de Groot R.P., Woortman M.R., Cremers F., Borrias M.,
RA van Arkel G.A., Weisbeek P.J.;
RT "Genes encoding ferredoxins from Anabaena sp. PCC 7937 and Synechococcus
RT sp. PCC 7942: structure and regulation.";
RL Photosyn. Res. 18:179-204(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
RN [3]
RP PROTEIN SEQUENCE OF 2-99.
RX PubMed=3137930; DOI=10.1042/bj2520571;
RA Wada K., Masui R., Matsubara H., Rogers L.J.;
RT "Properties and structure of the soluble ferredoxin from Synechococcus 6301
RT (Anacystis nidulans). Relationship to gene sequences.";
RL Biochem. J. 252:571-575(1988).
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 -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; M35127; AAA22054.1; -; Genomic_DNA.
DR EMBL; AP008231; BAD80674.1; -; Genomic_DNA.
DR RefSeq; WP_011244794.1; NC_006576.1.
DR AlphaFoldDB; P0A3D3; -.
DR SMR; P0A3D3; -.
DR STRING; 269084.syc2484_c; -.
DR EnsemblBacteria; BAD80674; BAD80674; syc2484_c.
DR KEGG; syc:syc2484_c; -.
DR eggNOG; COG0633; Bacteria.
DR OMA; CAARMIS; -.
DR Proteomes; UP000001175; 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; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3137930"
FT CHAIN 2..99
FT /note="Ferredoxin-1"
FT /id="PRO_0000189378"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 80
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 99 AA; 10521 MW; 2358EDC9E128F406 CRC64;
MATYKVTLVN AAEGLNTTID VADDTYILDA AEEQGIDLPY SCRAGACSTC AGKVVSGTVD
QSDQSFLDDD QIAAGFVLTC VAYPTSDVTI ETHKEEDLY