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Database: UniProt/SWISS-PROT
Entry: SDHB_ASHGO
LinkDB: SDHB_ASHGO
Original site: SDHB_ASHGO 
ID   SDHB_ASHGO              Reviewed;         261 AA.
AC   Q75CI4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   05-DEC-2018, entry version 105.
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=SDH2; OrderedLocusNames=ACL065C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient
RT   Saccharomyces cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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: a
CC       flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
CC       composed of a large and a small subunit. {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; AE016816; AAS51163.1; -; Genomic_DNA.
DR   RefSeq; NP_983339.1; NM_208692.1.
DR   ProteinModelPortal; Q75CI4; -.
DR   SMR; Q75CI4; -.
DR   STRING; 33169.AAS51163; -.
DR   EnsemblFungi; AAS51163; AAS51163; AGOS_ACL065C.
DR   GeneID; 4619459; -.
DR   KEGG; ago:AGOS_ACL065C; -.
DR   HOGENOM; HOG000160590; -.
DR   InParanoid; Q75CI4; -.
DR   KO; K00235; -.
DR   OMA; DGQYFGP; -.
DR   OrthoDB; EOG092C401C; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
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: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.
FT   CHAIN         ?    261       Succinate dehydrogenase [ubiquinone]
FT                                iron-sulfur subunit, mitochondrial.
FT                                /FTId=PRO_0000010347.
FT   DOMAIN       31    122       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      164    194       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        82     82       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        87     87       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        90     90       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       102    102       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       174    174       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       177    177       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       180    180       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       184    184       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       231    231       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       237    237       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       241    241       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   BINDING     189    189       Ubiquinone; shared with DHSD.
FT                                {ECO:0000250}.
SQ   SEQUENCE   261 AA;  29436 MW;  7F11084887FC7F5A CRC64;
     MVFRAGIGRI GLIRGLATQA AEVSATRYKS FKIYRWNPDT PAEKPRMQEY KVDLNKCGPM
     VLDALIKIKN EQDPTLTFRR SCREGICGSC AMNIGGRNTL ACLCKIDQAE NKDVKIYPLP
     HMYVVKDLVP DLTNFYKQYK SIQPYLQKAS KPADGREHLQ SIADRKKLDG LYECILCACC
     STACPSYWWN NEQYLGPAVL MQAYRWMVDS RDGAGAGRRE QLQNAMSVYR CHTIMNCTRT
     CPKGLNPGKA IAEIKKALAF A
//
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