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Database: UniProt
Entry: A8WPF0
LinkDB: A8WPF0
Original site: A8WPF0 
ID   SDHB_CAEBR              Reviewed;         282 AA.
AC   A8WPF0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   16-JAN-2019, entry version 63.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial {ECO:0000250|UniProtKB:Q9YHT2};
DE            EC=1.3.5.1;
DE   AltName: Full=Iron-sulfur subunit of complex II {ECO:0000250|UniProtKB:Q9YHT2};
DE            Short=Ip {ECO:0000250|UniProtKB:Q9YHT2};
DE   Flags: Precursor;
GN   Name=sdhb-1 {ECO:0000312|EMBL:CAP22357.2}; ORFNames=CBG00872;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP22357.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP22357.2};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A.,
RA   D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E.,
RA   Griffiths-Jones S., Harris T.W., Hillier L.W., Kamath R.,
RA   Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P.,
RA   Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M.,
RA   Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M.,
RA   Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for
RT   comparative genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Iron-sulfur protein (IP) subunit of succinate
CC       dehydrogenase (SDH) that is involved in complex II of the
CC       mitochondrial electron transport chain and is responsible for
CC       transferring electrons from succinate to ubiquinone (coenzyme Q).
CC       {ECO:0000250|UniProtKB:Q9YHT2}.
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   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000250|UniProtKB:Q9YHT2};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:Q9YHT2};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250|UniProtKB:Q9YHT2};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:Q9YHT2};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q9YHT2};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q9YHT2};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate from succinate (eukaryal route): step 1/1.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: a
CC       flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
CC       composed of a large and a small subunit.
CC       {ECO:0000250|UniProtKB:Q9YHT2}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9YHT2}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9YHT2}; Matrix side
CC       {ECO:0000250|UniProtKB:Q9YHT2}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family. {ECO:0000255}.
DR   EMBL; HE600951; CAP22357.2; -; Genomic_DNA.
DR   SMR; A8WPF0; -.
DR   STRING; 6238.CBG00872; -.
DR   EnsemblMetazoa; CBG00872; CBG00872; WBGene00024197.
DR   WormBase; CBG00872; CBP34424; WBGene00024197; Cbr-sdhb-1.
DR   eggNOG; KOG3049; Eukaryota.
DR   eggNOG; COG0479; LUCA.
DR   HOGENOM; HOG000160590; -.
DR   InParanoid; A8WPF0; -.
DR   OMA; DGQYFGP; -.
DR   OrthoDB; 1264157at2759; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000008549; Chromosome II.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
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:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd00207; fer2; 1.
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; 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; 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; 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   2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW   Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    282       Succinate dehydrogenase [ubiquinone]
FT                                iron-sulfur subunit, mitochondrial.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000367044.
FT   DOMAIN       43    131       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      174    204       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   COMPBIAS     25     28       Poly-Ala. {ECO:0000255}.
FT   METAL        91     91       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   METAL        96     96       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   METAL        99     99       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   METAL       111    111       Iron-sulfur 1 (2Fe-2S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   METAL       184    184       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   METAL       187    187       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   METAL       190    190       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   METAL       194    194       Iron-sulfur 3 (3Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   METAL       241    241       Iron-sulfur 3 (3Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   METAL       247    247       Iron-sulfur 3 (3Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   METAL       251    251       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
FT   BINDING     199    199       Ubiquinone; shared with DHSD.
FT                                {ECO:0000250|UniProtKB:Q9YHT2}.
SQ   SEQUENCE   282 AA;  31343 MW;  9A82F1BE0D05E8A1 CRC64;
     MLARSALFVH SAELAANAAR AASGAAAAQP KKTGNRIKTF EIYRFNPEAP GAKPTIQKFD
     VDLDQCGTMI LDALIKIKNE VDPTLTFRRS CREGICGSCA MNIGGENTLA CICKIDADTS
     KSTKIYPLPH MFVVKDLVPD MNLFYAQYAS IQPWIQKKTP LTLGEKQMHQ SVAERDRLDG
     LYECILCACC STSCPSYWWN ADKYLGPAVL MQAYRWVIDS RDDYAQERLH RMHDSFSAFK
     CHTIMNCTKT CPKHLNPAKA IGEIKSLLTG FKSKPAAEPS AF
//
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