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Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (FP)

 SDHA_YEAST              Reviewed;         640 AA.
Q00711; D6VX49;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
23-MAY-2018, entry version 189.
RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
AltName: Full=Flavoprotein subunit of complex II;
Short=FP;
Flags: Precursor;
Name=SDH1; Synonyms=SDHA; OrderedLocusNames=YKL148C; ORFNames=YKL602;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-53;
114-136 AND 429-448.
PubMed=1518827; DOI=10.1073/pnas.89.17.8011;
Schuelke N., Blobel G., Pain D.;
"Primary structure, import, and assembly of the yeast homolog of
succinate dehydrogenase flavoprotein.";
Proc. Natl. Acad. Sci. U.S.A. 89:8011-8015(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1511876; DOI=10.1016/0378-1119(92)90260-V;
Chapman K.B., Solomon S.D., Boeke J.D.;
"SDH1, the gene encoding the succinate dehydrogenase flavoprotein
subunit from Saccharomyces cerevisiae.";
Gene 118:131-136(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1577780;
Robinson K.M., Lemire B.D.;
"Isolation and nucleotide sequence of the Saccharomyces cerevisiae
gene for the succinate dehydrogenase flavoprotein subunit.";
J. Biol. Chem. 267:10101-10107(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091859; DOI=10.1002/yea.320100005;
Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
"DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP
loci of chromosome XI of Saccharomyces cerevisiae.";
Yeast 10:S35-S40(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[6]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[7]
PROTEIN SEQUENCE OF 29-38.
STRAIN=S288c / GRF88;
PubMed=8120006;
Bullis B.L., Lemire B.D.;
"Isolation and characterization of the Saccharomyces cerevisiae SDH4
gene encoding a membrane anchor subunit of succinate dehydrogenase.";
J. Biol. Chem. 269:6543-6549(1994).
[8]
PROTEIN SEQUENCE OF 607-615, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 201238 / W303-1B;
PubMed=11502169; DOI=10.1021/bi010277r;
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N.,
Manon S., Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular
complex.";
Biochemistry 40:9758-9769(2001).
[9]
MUTAGENESIS OF HIS-90.
PubMed=8026509; DOI=10.1111/j.1432-1033.1994.tb18949.x;
Robinson K.M., Rothery R.A., Weiner J.H., Lemire B.D.;
"The covalent attachment of FAD to the flavoprotein of Saccharomyces
cerevisiae succinate dehydrogenase is not necessary for import and
assembly into mitochondria.";
Eur. J. Biochem. 222:983-990(1994).
[10]
REVIEW ON SUCCINATE DEHYDROGENASE.
PubMed=11803020; DOI=10.1016/S0005-2728(01)00229-8;
Lemire B.D., Oyedotun K.S.;
"The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone
oxidoreductase.";
Biochim. Biophys. Acta 1553:102-116(2002).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
INTERACTION WITH EMI5.
PubMed=19628817; DOI=10.1126/science.1175689;
Hao H.-X., Khalimonchuk O., Schraders M., Dephoure N., Bayley J.-P.,
Kunst H., Devilee P., Cremers C.W.R.J., Schiffman J.D., Bentz B.G.,
Gygi S.P., Winge D.R., Kremer H., Rutter J.;
"SDH5, a gene required for flavination of succinate dehydrogenase, is
mutated in paraganglioma.";
Science 325:1139-1142(2009).
[13]
3D-STRUCTURE MODELING OF 29-640.
PubMed=14672929; DOI=10.1074/jbc.M311876200;
Oyedotun K.S., Lemire B.D.;
"The quaternary structure of the Saccharomyces cerevisiae succinate
dehydrogenase. Homology modeling, cofactor docking, and molecular
dynamics simulation studies.";
J. Biol. Chem. 279:9424-9431(2004).
-!- FUNCTION: Catalytic subunit of succinate dehydrogenase (SDH) that
is involved in complex II of the mitochondrial electron transport
chain and is responsible for transferring electrons from succinate
to ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic
dimer. Electrons flow from succinate to the FAD bound to SDH1, and
sequentially through the iron-sulfur clusters bound to SDH2 and
enter the membrane dimer formed by SDH3 and SDH4.
-!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
{ECO:0000250|UniProtKB:P31040}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:Q0QF01};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
fumarate from succinate (eukaryal route): step 1/1.
{ECO:0000250|UniProtKB:P31040}.
-!- SUBUNIT: Component of complex II composed of four subunits: a
flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
composed of a large and a small subunit. Interacts with EMI5/SDH5;
interaction is required for FAD attachment.
{ECO:0000269|PubMed:19628817}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:11502169}; Peripheral membrane protein
{ECO:0000269|PubMed:11502169}; Matrix side
{ECO:0000269|PubMed:11502169}.
-!- MISCELLANEOUS: Present with 10400 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
FRD/SDH subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M94874; AAA35024.1; -; Genomic_DNA.
EMBL; M86909; AAA35022.1; -; Genomic_DNA.
EMBL; M86746; AAA35026.1; -; Genomic_DNA.
EMBL; Z26877; CAA81506.1; -; Genomic_DNA.
EMBL; Z28148; CAA81989.1; -; Genomic_DNA.
EMBL; BK006944; DAA09015.1; -; Genomic_DNA.
PIR; S34793; S34793.
RefSeq; NP_012774.1; NM_001179714.1.
PDB; 1ORZ; Model; -; A=29-640.
PDB; 1PB4; Model; -; A=29-640.
PDBsum; 1ORZ; -.
PDBsum; 1PB4; -.
ProteinModelPortal; Q00711; -.
SMR; Q00711; -.
BioGrid; 33989; 105.
DIP; DIP-5853N; -.
IntAct; Q00711; 7.
MINT; Q00711; -.
STRING; 4932.YKL148C; -.
MaxQB; Q00711; -.
PaxDb; Q00711; -.
PRIDE; Q00711; -.
EnsemblFungi; YKL148C; YKL148C; YKL148C.
GeneID; 853709; -.
KEGG; sce:YKL148C; -.
EuPathDB; FungiDB:YKL148C; -.
SGD; S000001631; SDH1.
GeneTree; ENSGT00910000145155; -.
HOGENOM; HOG000160475; -.
InParanoid; Q00711; -.
KO; K00234; -.
OMA; GDSPWEH; -.
OrthoDB; EOG092C17LB; -.
BioCyc; MetaCyc:YKL148C-MONOMER; -.
BioCyc; YEAST:YKL148C-MONOMER; -.
UniPathway; UPA00223; UER01006.
PRO; PR:Q00711; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0031966; C:mitochondrial membrane; IDA:SGD.
GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:SGD.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:SGD.
GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IDA:SGD.
GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
GO; GO:0045333; P:cellular respiration; IMP:SGD.
GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IDA:SGD.
GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
Gene3D; 3.50.50.60; -; 2.
Gene3D; 3.90.700.10; -; 1.
InterPro; IPR003953; FAD-binding_2.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR003952; FRD_SDH_FAD_BS.
InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
InterPro; IPR011281; Succ_DH_flav_su_fwd.
InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
Pfam; PF00890; FAD_binding_2; 1.
Pfam; PF02910; Succ_DH_flav_C; 1.
SUPFAM; SSF46977; SSF46977; 1.
SUPFAM; SSF51905; SSF51905; 2.
SUPFAM; SSF56425; SSF56425; 1.
TIGRFAMs; TIGR01816; sdhA_forward; 1.
TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
Transit peptide; Transport; Tricarboxylic acid cycle.
TRANSIT 1 28 Mitochondrion.
{ECO:0000269|PubMed:1518827,
ECO:0000269|PubMed:8120006}.
CHAIN 29 640 Succinate dehydrogenase [ubiquinone]
flavoprotein subunit, mitochondrial.
/FTId=PRO_0000010342.
NP_BIND 59 64 FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
NP_BIND 82 97 FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
NP_BIND 449 450 FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
ACT_SITE 331 331 Proton acceptor.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 266 266 FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 287 287 Substrate.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 299 299 Substrate.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 398 398 Substrate.
{ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 433 433 FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
BINDING 444 444 Substrate.
{ECO:0000250|UniProtKB:Q9YHT1}.
MOD_RES 90 90 Tele-8alpha-FAD histidine.
{ECO:0000250|UniProtKB:Q9YHT1}.
MUTAGEN 90 90 H->S: Abolishes covalent attachment of
FAD. No effect on complex assembly.
Abolishes succinate-dehydrogenase
activity but no effect on fumarate
reductase activity.
{ECO:0000269|PubMed:8026509}.
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


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