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Database: UniProt/SWISS-PROT
Entry: SDHB_XENTR
LinkDB: SDHB_XENTR
Original site: SDHB_XENTR 
ID   SDHB_XENTR              Reviewed;         284 AA.
AC   B0BM36;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   16-JAN-2019, entry version 74.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial;
DE            EC=1.3.5.1;
DE   AltName: Full=Iron-sulfur subunit of complex II;
DE            Short=Ip;
DE   Flags: Precursor;
GN   Name=sdhb;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
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: the
CC       flavoprotein (FP) sdha, iron-sulfur protein (IP) sdhb, and a
CC       cytochrome b composed of sdhc and sdhd. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Matrix side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family. {ECO:0000305}.
DR   EMBL; BC158270; AAI58271.1; -; mRNA.
DR   RefSeq; NP_001120000.1; NM_001126528.1.
DR   UniGene; Str.51669; -.
DR   ProteinModelPortal; B0BM36; -.
DR   SMR; B0BM36; -.
DR   STRING; 8364.ENSXETP00000029442; -.
DR   PaxDb; B0BM36; -.
DR   Ensembl; ENSXETT00000029442; ENSXETP00000029442; ENSXETG00000013435.
DR   GeneID; 100144957; -.
DR   KEGG; xtr:100144957; -.
DR   CTD; 6390; -.
DR   Xenbase; XB-GENE-970193; sdhb.
DR   eggNOG; KOG3049; Eukaryota.
DR   eggNOG; COG0479; LUCA.
DR   GeneTree; ENSGT00390000013558; -.
DR   HOGENOM; HOG000160590; -.
DR   HOVERGEN; HBG005483; -.
DR   InParanoid; B0BM36; -.
DR   KO; K00235; -.
DR   OMA; CTHCYRC; -.
DR   OrthoDB; 1264157at2759; -.
DR   TreeFam; TF300754; -.
DR   Reactome; R-XTR-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   Bgee; ENSXETG00000013435; Expressed in 18 organ(s), highest expression level in skeletal muscle tissue.
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   2: Evidence at transcript level;
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     26       Mitochondrion. {ECO:0000250}.
FT   CHAIN        27    284       Succinate dehydrogenase [ubiquinone]
FT                                iron-sulfur subunit, mitochondrial.
FT                                /FTId=PRO_0000343803.
FT   DOMAIN       44    137       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      180    210       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        97     97       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       102    102       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       105    105       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       117    117       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       190    190       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       193    193       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       196    196       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       200    200       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       247    247       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       253    253       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       257    257       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   BINDING     205    205       Ubiquinone; shared with dhsd.
FT                                {ECO:0000250}.
SQ   SEQUENCE   284 AA;  32087 MW;  88CCE71B1DCB3D6C CRC64;
     MAAVVFSLRR SGPVFRLPGV LQVCRGAQTA AAAAPASQAE ARIKKFAIYR WDPDKPGDKP
     RMQTYEVDLN ECGSMVLDAL IKIKNEMDPT LTFRRSCREG ICGSCAMNIN GGNTLACTVR
     IDTNLSKVSK IYPLPHMYVV KDLVPDLSNF YAQYKSIEPY LKKKDESQEG KEQYLQSIED
     RDKLDGLYEC ILCACCSTSC PSYWWNADKY LGPAVLMQAY RWMIDSRDDY TEERLAKLQD
     PFSLYRCHTI MNCTRTCPKG LNPGKAIAEI KKMMATYKER AASV
//
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