DHSD_ASHGO
ID DHSD_ASHGO Reviewed; 171 AA.
AC Q750S6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE Short=CybS;
DE AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit;
DE Flags: Precursor;
GN Name=SDH4; OrderedLocusNames=AGL137W;
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: Membrane-anchoring subunit of succinate dehydrogenase (SDH)
CC that is involved in complex II of the mitochondrial electron transport
CC chain and is responsible for transferring electrons from succinate to
CC ubiquinone (coenzyme Q). {ECO:0000250}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC -!- SUBUNIT: Forms part of complex II containing 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 Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CybS family. {ECO:0000305}.
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DR EMBL; AE016820; AAS54354.1; -; Genomic_DNA.
DR RefSeq; NP_986530.1; NM_211592.1.
DR AlphaFoldDB; Q750S6; -.
DR SMR; Q750S6; -.
DR STRING; 33169.AAS54354; -.
DR EnsemblFungi; AAS54354; AAS54354; AGOS_AGL137W.
DR GeneID; 4622829; -.
DR KEGG; ago:AGOS_AGL137W; -.
DR eggNOG; KOG4097; Eukaryota.
DR HOGENOM; CLU_096618_0_0_1; -.
DR InParanoid; Q750S6; -.
DR OMA; CGTILMH; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd03496; SQR_TypeC_CybS; 1.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR007992; CybS.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR PANTHER; PTHR13337; PTHR13337; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..171
FT /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT small subunit, mitochondrial"
FT /id="PRO_0000006493"
FT TOPO_DOM 1..61
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..91
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..121
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..171
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 103
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with large subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with IP"
FT /evidence="ECO:0000250"
SQ SEQUENCE 171 AA; 18143 MW; CC3983D0670824F1 CRC64;
MQGIKMASPV IRAACKRSLH QSAVRAITIP FLPTLPQNPG GVKGDVNEAN PVPPANKMHG
SLHWNIERAF AVAAVPLVGL PLVAGSGVST LMDSLLASVM LGHCYIGFQA CIIDYIPQRV
YGKFHQYAMY LLAFGSLLSG VGIYKMESEG YGICGAVAAV WSGKAAREEK A
