ID A0A2G5CKF7_AQUCA Unreviewed; 154 AA.
AC A0A2G5CKF7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ferredoxin {ECO:0000256|RuleBase:RU364001};
GN ORFNames=AQUCO_04900211v1 {ECO:0000313|EMBL:PIA31764.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA31764.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA31764.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC {ECO:0000256|RuleBase:RU364001}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|RuleBase:RU364001};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|RuleBase:RU364001};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229, ECO:0000256|RuleBase:RU364001}.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000256|ARBA:ARBA00007874, ECO:0000256|RuleBase:RU364001}.
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DR EMBL; KZ305066; PIA31764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5CKF7; -.
DR STRING; 218851.A0A2G5CKF7; -.
DR InParanoid; A0A2G5CKF7; -.
DR OrthoDB; 312286at2759; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR010241; Fd_pln.
DR NCBIfam; TIGR02008; fdx_plant; 1.
DR PANTHER; PTHR43112; FERREDOXIN; 1.
DR PANTHER; PTHR43112:SF9; FERREDOXIN C 1, CHLOROPLASTIC; 1.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|RuleBase:RU364001};
KW Chloroplast {ECO:0000256|RuleBase:RU364001};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU364001};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364001};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364001};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364001}; Plastid {ECO:0000256|RuleBase:RU364001};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364001}.
FT DOMAIN 53..142
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 154 AA; 17216 MW; A3D93CE451971ED3 CRC64;
MPFLFLNKPV MATLHFCTSP PFTIYKQRQV NKHSAFYPKP SKLSSRRSLI RAYKVVIEHE
GKNTILEVDP DESILERALD NGLSVPHDCK LGVCMTCPAR LISGSVDQSD GMLSDDVVEK
GYTLLCVAYP RSDCQVKIIP EEELLSLQLA TSDD
//
