SDHA_YEAST
ID SDHA_YEAST Reviewed; 640 AA.
AC Q00711; D6VX49;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE AltName: Full=Flavoprotein subunit of complex II;
DE Short=FP;
DE Flags: Precursor;
GN Name=SDH1; Synonyms=SDHA; OrderedLocusNames=YKL148C; ORFNames=YKL602;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-53; 114-136
RP AND 429-448.
RX PubMed=1518827; DOI=10.1073/pnas.89.17.8011;
RA Schuelke N., Blobel G., Pain D.;
RT "Primary structure, import, and assembly of the yeast homolog of succinate
RT dehydrogenase flavoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8011-8015(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1511876; DOI=10.1016/0378-1119(92)90260-v;
RA Chapman K.B., Solomon S.D., Boeke J.D.;
RT "SDH1, the gene encoding the succinate dehydrogenase flavoprotein subunit
RT from Saccharomyces cerevisiae.";
RL Gene 118:131-136(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1577780; DOI=10.1016/s0021-9258(19)50205-8;
RA Robinson K.M., Lemire B.D.;
RT "Isolation and nucleotide sequence of the Saccharomyces cerevisiae gene for
RT the succinate dehydrogenase flavoprotein subunit.";
RL J. Biol. Chem. 267:10101-10107(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091859; DOI=10.1002/yea.320100005;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT of chromosome XI of Saccharomyces cerevisiae.";
RL Yeast 10:S35-S40(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP PROTEIN SEQUENCE OF 29-38.
RC STRAIN=S288c / GRF88;
RX PubMed=8120006; DOI=10.1016/s0021-9258(17)37406-9;
RA Bullis B.L., Lemire B.D.;
RT "Isolation and characterization of the Saccharomyces cerevisiae SDH4 gene
RT encoding a membrane anchor subunit of succinate dehydrogenase.";
RL J. Biol. Chem. 269:6543-6549(1994).
RN [8]
RP PROTEIN SEQUENCE OF 607-615, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 201238 / W303-1B;
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [9]
RP MUTAGENESIS OF HIS-90.
RX PubMed=8026509; DOI=10.1111/j.1432-1033.1994.tb18949.x;
RA Robinson K.M., Rothery R.A., Weiner J.H., Lemire B.D.;
RT "The covalent attachment of FAD to the flavoprotein of Saccharomyces
RT cerevisiae succinate dehydrogenase is not necessary for import and assembly
RT into mitochondria.";
RL Eur. J. Biochem. 222:983-990(1994).
RN [10]
RP REVIEW ON SUCCINATE DEHYDROGENASE.
RX PubMed=11803020; DOI=10.1016/s0005-2728(01)00229-8;
RA Lemire B.D., Oyedotun K.S.;
RT "The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone
RT oxidoreductase.";
RL Biochim. Biophys. Acta 1553:102-116(2002).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP INTERACTION WITH EMI5.
RX PubMed=19628817; DOI=10.1126/science.1175689;
RA Hao H.-X., Khalimonchuk O., Schraders M., Dephoure N., Bayley J.-P.,
RA Kunst H., Devilee P., Cremers C.W.R.J., Schiffman J.D., Bentz B.G.,
RA Gygi S.P., Winge D.R., Kremer H., Rutter J.;
RT "SDH5, a gene required for flavination of succinate dehydrogenase, is
RT mutated in paraganglioma.";
RL Science 325:1139-1142(2009).
RN [13]
RP 3D-STRUCTURE MODELING OF 29-640.
RX PubMed=14672929; DOI=10.1074/jbc.m311876200;
RA Oyedotun K.S., Lemire B.D.;
RT "The quaternary structure of the Saccharomyces cerevisiae succinate
RT dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics
RT simulation studies.";
RL J. Biol. Chem. 279:9424-9431(2004).
CC -!- FUNCTION: Catalytic subunit of succinate dehydrogenase (SDH) that is
CC involved in complex II of the mitochondrial electron transport chain
CC and is responsible for transferring electrons from succinate to
CC ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic dimer.
CC Electrons flow from succinate to the FAD bound to SDH1, and
CC sequentially through the iron-sulfur clusters bound to SDH2 and enter
CC the membrane dimer formed by SDH3 and SDH4.
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 Evidence={ECO:0000250|UniProtKB:P31040};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q0QF01};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (eukaryal route): step 1/1.
CC {ECO:0000250|UniProtKB:P31040}.
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. Interacts with EMI5/SDH5;
CC interaction is required for FAD attachment.
CC {ECO:0000269|PubMed:19628817}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11502169}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11502169}; Matrix side
CC {ECO:0000269|PubMed:11502169}.
CC -!- MISCELLANEOUS: Present with 10400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; M94874; AAA35024.1; -; Genomic_DNA.
DR EMBL; M86909; AAA35022.1; -; Genomic_DNA.
DR EMBL; M86746; AAA35026.1; -; Genomic_DNA.
DR EMBL; Z26877; CAA81506.1; -; Genomic_DNA.
DR EMBL; Z28148; CAA81989.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09015.1; -; Genomic_DNA.
DR PIR; S34793; S34793.
DR RefSeq; NP_012774.1; NM_001179714.1.
DR AlphaFoldDB; Q00711; -.
DR SMR; Q00711; -.
DR BioGRID; 33989; 119.
DR ComplexPortal; CPX-565; Mitochondrial respiratory chain complex II.
DR DIP; DIP-5853N; -.
DR IntAct; Q00711; 7.
DR MINT; Q00711; -.
DR STRING; 4932.YKL148C; -.
DR MaxQB; Q00711; -.
DR PaxDb; Q00711; -.
DR PRIDE; Q00711; -.
DR DNASU; 853709; -.
DR EnsemblFungi; YKL148C_mRNA; YKL148C; YKL148C.
DR GeneID; 853709; -.
DR KEGG; sce:YKL148C; -.
DR SGD; S000001631; SDH1.
DR VEuPathDB; FungiDB:YKL148C; -.
DR eggNOG; KOG2403; Eukaryota.
DR HOGENOM; CLU_014312_6_1_1; -.
DR InParanoid; Q00711; -.
DR OMA; DPIPIQP; -.
DR BioCyc; MetaCyc:YKL148C-MON; -.
DR BioCyc; YEAST:YKL148C-MON; -.
DR Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER01006.
DR PRO; PR:Q00711; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q00711; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:SGD.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:SGD.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IDA:SGD.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0045333; P:cellular respiration; IMP:SGD.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IDA:SGD.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:ComplexPortal.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:ComplexPortal.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR003952; FRD_SDH_FAD_BS.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Reference proteome; Transit peptide; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1518827,
FT ECO:0000269|PubMed:8120006"
FT CHAIN 29..640
FT /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT subunit, mitochondrial"
FT /id="PRO_0000010342"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 59..64
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 82..97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 433
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 449..450
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT MOD_RES 90
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT MUTAGEN 90
FT /note="H->S: Abolishes covalent attachment of FAD. No
FT effect on complex assembly. Abolishes succinate-
FT dehydrogenase activity but no effect on fumarate reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:8026509"
SQ SEQUENCE 640 AA; 70229 MW; A657E440B8ED58E2 CRC64;
MLSLKKSALS KLTLLRNTRT FTSSALVRQT QGSVNGSASR SADGKYHIID HEYDCVVIGA
GGAGLRAAFG LAEAGYKTAC ISKLFPTRSH TVAAQGGINA ALGNMHKDNW KWHMYDTVKG
SDWLGDQDSI HYMTREAPKS IIELEHYGVP FSRTENGKIY QRAFGGQTKE YGKGAQAYRT
CAVADRTGHA LLHTLYGQAL RHDTHFFIEY FALDLLTHNG EVVGVIAYNQ EDGTIHRFRA
HKTIIATGGY GRAYFSCTSA HTCTGDGNAM VSRAGFPLQD LEFVQFHPSG IYGSGCLITE
GARGEGGFLV NSEGERFMER YAPTAKDLAC RDVVSRAITM EIREGRGVGK KKDHMYLQLS
HLPPEVLKER LPGISETAAI FAGVDVTKEP IPIIPTVHYN MGGIPTKWNG EALTIDEETG
EDKVIPGLMA CGEAACVSVH GANRLGANSL LDLVVFGRAV AHTVADTLQP GLPHKPLPSD
LGKESIANLD KLRNANGSRS TAEIRMNMKQ TMQKDVSVFR TQSSLDEGVR NITAVEKTFD
DVKTTDRSMI WNSDLVETLE LQNLLTCASQ TAVSAANRKE SRGAHAREDY PNRDDEHWMK
HTLSWQKDVA APVTLKYRRV IDHTLDEKEC PSVPPTVRAY
