(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 108.
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 Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   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 Saccharomyces
RT   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 dehydrogenase
CC       (SDH) that is involved in complex II of the mitochondrial electron
CC       transport chain and is responsible for transferring electrons from
CC       succinate to ubiquinone (coenzyme Q). {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; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC       iron-sulfur protein family. {ECO:0000305}.
DR   EMBL; AE016816; AAS51163.1; -; Genomic_DNA.
DR   RefSeq; NP_983339.1; NM_208692.1.
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   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;
DR   PRODOM; Q75CI4.
DR   SWISS-2DPAGE; Q75CI4.
KW   2Fe-2S; 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..261
FT                   /note="Succinate dehydrogenase [ubiquinone] iron-sulfur
FT                   subunit, mitochondrial"
FT                   /id="PRO_0000010347"
FT   DOMAIN          31..122
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          164..194
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   METAL           82
FT                   /note="Iron-sulfur 1 (2Fe-2S)"
FT                   /evidence="ECO:0000250"
FT   METAL           87
FT                   /note="Iron-sulfur 1 (2Fe-2S)"
FT                   /evidence="ECO:0000250"
FT   METAL           90
FT                   /note="Iron-sulfur 1 (2Fe-2S)"
FT                   /evidence="ECO:0000250"
FT   METAL           102
FT                   /note="Iron-sulfur 1 (2Fe-2S)"
FT                   /evidence="ECO:0000250"
FT   METAL           174
FT                   /note="Iron-sulfur 2 (4Fe-4S)"
FT                   /evidence="ECO:0000250"
FT   METAL           177
FT                   /note="Iron-sulfur 2 (4Fe-4S)"
FT                   /evidence="ECO:0000250"
FT   METAL           180
FT                   /note="Iron-sulfur 2 (4Fe-4S)"
FT                   /evidence="ECO:0000250"
FT   METAL           184
FT                   /note="Iron-sulfur 3 (3Fe-4S)"
FT                   /evidence="ECO:0000250"
FT   METAL           231
FT                   /note="Iron-sulfur 3 (3Fe-4S)"
FT                   /evidence="ECO:0000250"
FT   METAL           237
FT                   /note="Iron-sulfur 3 (3Fe-4S)"
FT                   /evidence="ECO:0000250"
FT   METAL           241
FT                   /note="Iron-sulfur 2 (4Fe-4S)"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /note="Ubiquinone; shared with DHSD"
FT                   /evidence="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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