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Database: UniProt
Entry: P46050
LinkDB: P46050
Original site: P46050 
ID   FER3_ANAVT              Reviewed;          98 AA.
AC   P46050; Q3M578;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-JAN-2019, entry version 108.
DE   RecName: Full=Ferredoxin-3;
DE   AltName: Full=Ferredoxin III;
DE            Short=FdIII;
GN   Name=fdxB; OrderedLocusNames=Ava_4259;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
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
RT   systems evolved for heterocysts and vegetative cells of Anabaena
RT   variabilis ATCC 29413: characterization of the fdxH1/2 gene regions as
RT   part of the nif1/2 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.,
RA   Han C., 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
CC       electrons in a wide variety of metabolic reactions.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
DR   EMBL; Z46890; CAA86992.1; -; Genomic_DNA.
DR   EMBL; CP000117; ABA23858.1; -; Genomic_DNA.
DR   PIR; S70250; S70250.
DR   ProteinModelPortal; P46050; -.
DR   STRING; 240292.Ava_4259; -.
DR   EnsemblBacteria; ABA23858; ABA23858; Ava_4259.
DR   KEGG; ava:Ava_4259; -.
DR   eggNOG; ENOG4105WCA; Bacteria.
DR   eggNOG; COG1145; LUCA.
DR   HOGENOM; HOG000005481; -.
DR   BioCyc; AVAR240292:G7WH-9727-MONOMER; -.
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   GO; GO:0055114; P:oxidation-reduction process; 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; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Nitrogen fixation; Repeat; Transport.
FT   CHAIN         1     98       Ferredoxin-3.
FT                                /FTId=PRO_0000159186.
FT   DOMAIN       18     47       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       66     95       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        27     27       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        30     30       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        33     33       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        37     37       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        75     75       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        78     78       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        81     81       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        85     85       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   98 AA;  10866 MW;  268AF7E0CD735AA9 CRC64;
     MATLTGLTFG GQVWTPQFVE AVNQDKCIGC GRCFKACGRN VLILQALNEN GEFVEDEEGE
     EIERKVMSII HPEYCIGCQA CARACPKNCY THSPLEHN
//
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