SDH3_SCHPO
ID SDH3_SCHPO Reviewed; 180 AA.
AC O74882;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Succinate dehydrogenase cytochrome B subunit, mitochondrial;
DE Flags: Precursor;
GN Name=sdh3; ORFNames=SPCC330.12c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=The heme is bound between the two transmembrane subunits.
CC {ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC -!- SUBUNIT: Forms part of complex II containing four subunits: a 70 kDa
CC flavoprotein (FP), a 27 kDa iron-sulfur protein (IP), a cytochrome B
CC and a membrane-anchoring protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA20917.1; -; Genomic_DNA.
DR PIR; T41322; T41322.
DR RefSeq; NP_587712.1; NM_001022707.2.
DR AlphaFoldDB; O74882; -.
DR SMR; O74882; -.
DR BioGRID; 275672; 35.
DR ComplexPortal; CPX-566; Mitochondrial respiratory chain complex II.
DR STRING; 4896.SPCC330.12c.1; -.
DR SwissPalm; O74882; -.
DR PaxDb; O74882; -.
DR EnsemblFungi; SPCC330.12c.1; SPCC330.12c.1:pep; SPCC330.12c.
DR GeneID; 2539100; -.
DR KEGG; spo:SPCC330.12c; -.
DR PomBase; SPCC330.12c; sdh3.
DR VEuPathDB; FungiDB:SPCC330.12c; -.
DR eggNOG; KOG0449; Eukaryota.
DR HOGENOM; CLU_094691_0_0_1; -.
DR InParanoid; O74882; -.
DR OMA; IPGGIPC; -.
DR PhylomeDB; O74882; -.
DR Reactome; R-SPO-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; -.
DR PRO; PR:O74882; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
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; ISS:PomBase.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:PomBase.
DR GO; GO:0006105; P:succinate metabolic process; IC:PomBase.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR PANTHER; PTHR10978; PTHR10978; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
DR TIGRFAMs; TIGR02970; succ_dehyd_cytB; 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 CHAIN ?..180
FT /note="Succinate dehydrogenase cytochrome B subunit,
FT mitochondrial"
FT /id="PRO_0000041773"
FT TOPO_DOM 1..82
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..122
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..159
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 138
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with second transmembrane
FT subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 180 AA; 20136 MW; F9A0B370306B79B6 CRC64;
MFATRSFCLS SSLFRPAAQL LRPAGRSTLR NVWRRSIATE HLTQTEANSR LASQRVHRPN
SPHLTIYEPQ LTWYLSSLHR ITGCVVAGTL YAFAMGYLVA PLAGYSLDTA TISGLIQQVP
TWIKVPAKFV ISYPLTFHIF NGIRHLIWDT TKELSLKGVY RTGYAVLALS VLTSGYFAMI
