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Database: UniProt
Entry: A0A2I2KSU0_9ACTN
LinkDB: A0A2I2KSU0_9ACTN
Original site: A0A2I2KSU0_9ACTN 
ID   A0A2I2KSU0_9ACTN        Unreviewed;       510 AA.
AC   A0A2I2KSU0;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Ferredoxin {ECO:0000256|ARBA:ARBA00013529};
GN   ORFNames=FRACA_2750003 {ECO:0000313|EMBL:SNQ48751.1};
OS   Frankia canadensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=1836972 {ECO:0000313|EMBL:SNQ48751.1, ECO:0000313|Proteomes:UP000234331};
RN   [1] {ECO:0000313|EMBL:SNQ48751.1, ECO:0000313|Proteomes:UP000234331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRACA_ARgP5 {ECO:0000313|EMBL:SNQ48751.1};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-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|ARBA:ARBA00003532}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; FZMO01000196; SNQ48751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2KSU0; -.
DR   Proteomes; UP000234331; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 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   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR000813; 7Fe_ferredoxin.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PRINTS; PR00354; 7FE8SFRDOXIN.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234331}.
FT   DOMAIN          33..62
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   510 AA;  52837 MW;  01B39E59A7DB532A CRC64;
     MIMVYIITAA CLDVMDRSCV DECPVDCVYE GRRKLYIHPE ECIDCGACAR VCPVDAISWD
     RDADADPTAT DLTATDEIHA HLAAPLAAVD ADLTARHPAA SADADAHSDA RRSQPVHTCY
     LPADQMSPDI VPVWAARATT LLAAHGSDPA TLAAATGGDP HPATAAAVHA HVTRVLATEP
     IQDLRVDLED GYGPRPDAVE DADTERAAAA LRAASAAGTL PARYGLRPKS LDPTVRARGL
     RSLDLFLSAL VADAAPPPPG LVLTLPKVGD PRQLTVFVAV LTELERRLGL APIGVEVQVE
     TPAAVLALPE LVTAGLALGP GRLVGLHVGT YDYSASLGIG AADQASDHPA VEHATTMMQL
     AAAGTGIEVA DGSSNLLPKD EQPSDERTVH RAWRRHAGLV RRAWHRGLYQ GWDLHPGQLV
     SRHAAVGGCL LAGLDAALAR LGAYVSGIEG AGIEGAGTVS GAIADEPATG RALAGHVRRA
     LDAGLLDDAG LAAAGLHRTV VDRLATASPS
//
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