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Database: UniProt
Entry: K9ZM89_ANACC
LinkDB: K9ZM89_ANACC
Original site: K9ZM89_ANACC 
ID   K9ZM89_ANACC            Unreviewed;       105 AA.
AC   K9ZM89;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Ferredoxin (2Fe-2S) {ECO:0000313|EMBL:AFZ59662.1};
GN   OrderedLocusNames=Anacy_4298 {ECO:0000313|EMBL:AFZ59662.1};
OS   Anabaena cylindrica (strain ATCC 27899 / PCC 7122).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=272123 {ECO:0000313|EMBL:AFZ59662.1, ECO:0000313|Proteomes:UP000010474};
RN   [1] {ECO:0000313|Proteomes:UP000010474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27899 / PCC 7122 {ECO:0000313|Proteomes:UP000010474};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC       {ECO:0000256|ARBA:ARBA00007874}.
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DR   EMBL; CP003659; AFZ59662.1; -; Genomic_DNA.
DR   RefSeq; WP_015216279.1; NZ_AP018166.1.
DR   AlphaFoldDB; K9ZM89; -.
DR   STRING; 272123.Anacy_4298; -.
DR   KEGG; acy:Anacy_4298; -.
DR   PATRIC; fig|272123.3.peg.4683; -.
DR   eggNOG; COG1018; Bacteria.
DR   HOGENOM; CLU_082632_7_3_3; -.
DR   OrthoDB; 462043at2; -.
DR   Proteomes; UP000010474; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
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:SF10; FERREDOXIN C 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   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022714};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010474};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          5..95
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   105 AA;  11270 MW;  DDCCAD96B8022925 CRC64;
     MSKTYTVEIN HQGKIHALQV PENETILSVA QDAGLDLPTS CGAGVCTTCA GQITEGKVDQ
     ADGMGVSLEL QKQGYVLLCV AKPLSDLKID TEKEDIVYQK QFGKD
//
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