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Database: UniProt
Entry: P00254
LinkDB: P00254
Original site: P00254 
ID   FER1_TRIV2              Reviewed;          99 AA.
AC   P00254; Q3MF56;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Ferredoxin-1;
DE   AltName: Full=Ferredoxin I;
GN   Name=petF1; OrderedLocusNames=Ava_0756;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3095790; DOI=10.1093/nar/14.19.7803;
RA   van der Plas J., Groot R.P., Weisbeek P.J., van Arkel G.A.;
RT   "Coding sequence of a ferredoxin gene from Anabaena variabilis ATCC
RT   29413.";
RL   Nucleic Acids Res. 14:7803-7803(1986).
RN   [2]
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   [3]
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).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-99.
RA   Chan T.-M., Hermodson M.A., Ulrich E.L., Markley J.L.;
RT   "Nuclear magnetic resonance studies of two-iron-two-sulfur ferredoxins. 2.
RT   Determination of the sequence of Anabaena variabilis ferredoxin II,
RT   assignment of aromatic resonances in proton spectra, and effects of
RT   chemical modification.";
RL   Biochemistry 22:5988-5995(1983).
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; X06210; CAA29563.1; -; Genomic_DNA.
DR   EMBL; X14343; CAA32528.1; -; Genomic_DNA.
DR   EMBL; CP000117; ABA20380.1; -; Genomic_DNA.
DR   PIR; A25761; FEAI.
DR   AlphaFoldDB; P00254; -.
DR   SMR; P00254; -.
DR   STRING; 240292.Ava_0756; -.
DR   KEGG; ava:Ava_0756; -.
DR   eggNOG; COG0633; Bacteria.
DR   HOGENOM; CLU_082632_7_3_3; -.
DR   Proteomes; UP000002533; 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   NCBIfam; TIGR02008; fdx_plant; 1.
DR   PANTHER; PTHR43112; FERREDOXIN; 1.
DR   PANTHER; PTHR43112:SF3; FERREDOXIN-2, CHLOROPLASTIC; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 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|Ref.4"
FT   CHAIN           2..99
FT                   /note="Ferredoxin-1"
FT                   /id="PRO_0000189302"
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;  10726 MW;  5260D1B6108EEF0A CRC64;
     MATFKVTLIN EAEGTSNTID VPDDEYILDA AEEQGYDLPF SCRAGACSTC AGKLVSGTVD
     QSDQSFLDDD QIEAGYVLTC VAYPTSDVTI QTHKEEDLY
//
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