Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q00711 (SDHA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit of complex II
Short name=FP
Gene names
Name:SDH1
Synonyms:SDHA
Ordered Locus Names:YKL148C
ORF Names:YKL602
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length640 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Cofactor

FAD.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.

Subunit structure

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. Ref.12

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Ref.8.

Miscellaneous

Present with 10400 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SDH2P218012EBI-5851,EBI-5856

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Ref.1 Ref.7
Chain29 – 640612Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
PRO_0000010342

Regions

Nucleotide binding59 – 646FAD By similarity
Nucleotide binding82 – 9716FAD By similarity
Nucleotide binding449 – 4502FAD By similarity

Sites

Active site3311Proton acceptor By similarity
Binding site2661FAD By similarity
Binding site2871Substrate By similarity
Binding site2991Substrate By similarity
Binding site3981Substrate By similarity
Binding site4331FAD By similarity
Binding site4441Substrate By similarity

Amino acid modifications

Modified residue901Tele-8alpha-FAD histidine By similarity

Experimental info

Mutagenesis901H → S: Abolishes covalent attachment of FAD. No effect on complex assembly. Abolishes succinate-dehydrogenase activity but no effect on fumarate reductase activity. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q00711 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: A657E440B8ED58E2

FASTA64070,229
        10         20         30         40         50         60 
MLSLKKSALS KLTLLRNTRT FTSSALVRQT QGSVNGSASR SADGKYHIID HEYDCVVIGA 

        70         80         90        100        110        120 
GGAGLRAAFG LAEAGYKTAC ISKLFPTRSH TVAAQGGINA ALGNMHKDNW KWHMYDTVKG 

       130        140        150        160        170        180 
SDWLGDQDSI HYMTREAPKS IIELEHYGVP FSRTENGKIY QRAFGGQTKE YGKGAQAYRT 

       190        200        210        220        230        240 
CAVADRTGHA LLHTLYGQAL RHDTHFFIEY FALDLLTHNG EVVGVIAYNQ EDGTIHRFRA 

       250        260        270        280        290        300 
HKTIIATGGY GRAYFSCTSA HTCTGDGNAM VSRAGFPLQD LEFVQFHPSG IYGSGCLITE 

       310        320        330        340        350        360 
GARGEGGFLV NSEGERFMER YAPTAKDLAC RDVVSRAITM EIREGRGVGK KKDHMYLQLS 

       370        380        390        400        410        420 
HLPPEVLKER LPGISETAAI FAGVDVTKEP IPIIPTVHYN MGGIPTKWNG EALTIDEETG 

       430        440        450        460        470        480 
EDKVIPGLMA CGEAACVSVH GANRLGANSL LDLVVFGRAV AHTVADTLQP GLPHKPLPSD 

       490        500        510        520        530        540 
LGKESIANLD KLRNANGSRS TAEIRMNMKQ TMQKDVSVFR TQSSLDEGVR NITAVEKTFD 

       550        560        570        580        590        600 
DVKTTDRSMI WNSDLVETLE LQNLLTCASQ TAVSAANRKE SRGAHAREDY PNRDDEHWMK 

       610        620        630        640 
HTLSWQKDVA APVTLKYRRV IDHTLDEKEC PSVPPTVRAY 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure, import, and assembly of the yeast homolog of succinate dehydrogenase flavoprotein."
Schuelke N., Blobel G., Pain D.
Proc. Natl. Acad. Sci. U.S.A. 89:8011-8015(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-53; 114-136 AND 429-448.
[2]"SDH1, the gene encoding the succinate dehydrogenase flavoprotein subunit from Saccharomyces cerevisiae."
Chapman K.B., Solomon S.D., Boeke J.D.
Gene 118:131-136(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Isolation and nucleotide sequence of the Saccharomyces cerevisiae gene for the succinate dehydrogenase flavoprotein subunit."
Robinson K.M., Lemire B.D.
J. Biol. Chem. 267:10101-10107(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci of chromosome XI of Saccharomyces cerevisiae."
Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.
Yeast 10:S35-S40(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Complete DNA sequence of yeast chromosome XI."
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. expand/collapse author list , 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.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"Isolation and characterization of the Saccharomyces cerevisiae SDH4 gene encoding a membrane anchor subunit of succinate dehydrogenase."
Bullis B.L., Lemire B.D.
J. Biol. Chem. 269:6543-6549(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-38.
Strain: S288c / GRF88.
[8]"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 607-615, SUBCELLULAR LOCATION.
Strain: ATCC 201238 / W303-1B.
[9]"The covalent attachment of FAD to the flavoprotein of Saccharomyces cerevisiae succinate dehydrogenase is not necessary for import and assembly into mitochondria."
Robinson K.M., Rothery R.A., Weiner J.H., Lemire B.D.
Eur. J. Biochem. 222:983-990(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-90.
[10]"The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase."
Lemire B.D., Oyedotun K.S.
Biochim. Biophys. Acta 1553:102-116(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON SUCCINATE DEHYDROGENASE.
[11]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]"SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma."
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.
Science 325:1139-1142(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EMI5.
[13]"The quaternary structure of the Saccharomyces cerevisiae succinate dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics simulation studies."
Oyedotun K.S., Lemire B.D.
J. Biol. Chem. 279:9424-9431(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 29-640.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M94874 Genomic DNA. Translation: AAA35024.1.
M86909 Genomic DNA. Translation: AAA35022.1.
M86746 Genomic DNA. Translation: AAA35026.1.
Z26877 Genomic DNA. Translation: CAA81506.1.
Z28148 Genomic DNA. Translation: CAA81989.1.
BK006944 Genomic DNA. Translation: DAA09015.1.
PIRS34793.
RefSeqNP_012774.1. NM_001179714.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ORZmodel-A29-640[»]
1PB4model-A29-640[»]
ProteinModelPortalQ00711.
SMRQ00711. Positions 45-640.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33989. 57 interactions.
DIPDIP-5853N.
IntActQ00711. 6 interactions.
MINTMINT-4817456.
STRING4932.YKL148C.

Proteomic databases

PaxDbQ00711.
PeptideAtlasQ00711.
PRIDEQ00711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL148C; YKL148C; YKL148C.
GeneID853709.
KEGGsce:YKL148C.

Organism-specific databases

CYGDYKL148c.
SGDS000001631. SDH1.

Phylogenomic databases

eggNOGCOG1053.
GeneTreeENSGT00750000117848.
HOGENOMHOG000160475.
KOK00234.
OMARACFAKD.
OrthoDBEOG7V76G3.

Enzyme and pathway databases

BioCycMetaCyc:YKL148C-MONOMER.
YEAST:YKL148C-MONOMER.
UniPathwayUPA00223; UER01006.

Gene expression databases

GenevestigatorQ00711.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974713.

Entry information

Entry nameSDHA_YEAST
AccessionPrimary (citable) accession number: Q00711
Secondary accession number(s): D6VX49
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways