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Database: UniProt
Entry: B3EIF0_CHLL2
LinkDB: B3EIF0_CHLL2
Original site: B3EIF0_CHLL2 
ID   B3EIF0_CHLL2            Unreviewed;       257 AA.
AC   B3EIF0;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=4Fe-4S ferredoxin iron-sulfur binding domain protein {ECO:0000313|EMBL:ACD91462.1};
GN   OrderedLocusNames=Clim_2441 {ECO:0000313|EMBL:ACD91462.1};
OS   Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290315 {ECO:0000313|EMBL:ACD91462.1, ECO:0000313|Proteomes:UP000008841};
RN   [1] {ECO:0000313|EMBL:ACD91462.1, ECO:0000313|Proteomes:UP000008841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 245 / NBRC 103803 / 6330
RC   {ECO:0000313|Proteomes:UP000008841};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium limicola DSM 245.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|ARBA:ARBA00001927};
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC       iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433}.
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DR   EMBL; CP001097; ACD91462.1; -; Genomic_DNA.
DR   RefSeq; WP_012467327.1; NC_010803.1.
DR   AlphaFoldDB; B3EIF0; -.
DR   STRING; 290315.Clim_2441; -.
DR   KEGG; cli:Clim_2441; -.
DR   eggNOG; COG0479; Bacteria.
DR   HOGENOM; CLU_044838_3_3_10; -.
DR   OrthoDB; 9804391at2; -.
DR   Proteomes; UP000008841; 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   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR   PANTHER; PTHR11921:SF41; 4FE-4S FERREDOXIN IRON-SULFUR BINDING DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
DR   Pfam; PF13085; Fer2_3; 1.
DR   Pfam; PF13237; Fer4_10; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          18..103
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          150..180
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   257 AA;  27939 MW;  956F39C51E1AEF84 CRC64;
     MNYTLKIWRQ KNAKARGEMV SYQVSGISAE ISFFEMLDML NQQLIAEGGD PVAFDHDCRE
     GICGTCSLYI NGRPHGPVRG VTTCQLHMRS FSDGEVIHIE PWRSKAFPVV RDLVVDRSAL
     DLIIQAGGYV SVNSGGIPDA NTIPVPKHHA DTAFDAAACI GCGACVAACP NAAAMLFVSA
     KVSHLSLLPQ GKAEAVKRVQ KMVARMDELG FGNCSNTYAC EVECPKLISV TNIARMNREF
     LSAKLFSEKD KIVRDSI
//
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