(data stored in ACNUC1104 zone)

SWISSPROT: B1K389_BURCC

ID   B1K389_BURCC            Unreviewed;       233 AA.
AC   B1K389;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Succinate dehydrogenase iron-sulfur subunit {ECO:0000256|RuleBase:RU361237};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237};
GN   OrderedLocusNames=Bcenmc03_3591 {ECO:0000313|EMBL:ACA92743.1};
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92743.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|RuleBase:RU361237};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU361237};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237};
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family.
CC       {ECO:0000256|RuleBase:RU361237}.
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DR   EMBL; CP000959; ACA92743.1; -; Genomic_DNA.
DR   RefSeq; WP_006479352.1; NC_010515.1.
DR   EnsemblBacteria; ACA92743; ACA92743; Bcenmc03_3591.
DR   GeneID; 29784306; -.
DR   KEGG; bcm:Bcenmc03_3591; -.
DR   HOGENOM; HOG000160590; -.
DR   KO; K00240; -.
DR   OMA; DGQYFGP; -.
DR   BioCyc; BCEN406425:G1GBC-3813-MONOMER; -.
DR   Proteomes; UP000002169; Chromosome 2.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.10.1060.10; -; 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; 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; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR   InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR   Pfam; PF13085; Fer2_3; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR00384; dhsB; 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;
DR   PRODOM; B1K389.
DR   SWISS-2DPAGE; B1K389.
KW   2Fe-2S {ECO:0000256|RuleBase:RU361237};
KW   3Fe-4S {ECO:0000256|RuleBase:RU361237};
KW   4Fe-4S {ECO:0000256|RuleBase:RU361237};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002169};
KW   Iron {ECO:0000256|RuleBase:RU361237};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU361237};
KW   Metal-binding {ECO:0000256|RuleBase:RU361237};
KW   Oxidoreductase {ECO:0000313|EMBL:ACA92743.1}.
FT   DOMAIN        6     93       2Fe-2S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51085}.
FT   DOMAIN      134    164       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
SQ   SEQUENCE   233 AA;  26596 MW;  92E9BE206B167196 CRC64;
     MAKRIFEVYR YDPDKDAAPR MQTYELEIQH ERMLLDALVK LKALDETLSF RRSCREGVCG
     SDAMNINGKN GLACLTNLND LPQKIVLRPL PGLPVVRDLI VDMTHFFNQY HSIKPYLIND
     APPPEKERLQ SPEERDELDG VYECILCASC STSCPSFWWN PDKFVGPAGL LQAYRFIADS
     RDTATGERLD NLEDPYRLFR CHTIMNCVDV CPKGLNPTKA IGKIKELMVR RAV
//

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