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Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene

SDH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Pathway:itricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes fumarate from succinate (eukaryal route).
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial (YJL045W), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SDH2), Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (SDH1)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes fumarate from succinate (eukaryal route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei266 – 2661FADBy similarity
Binding sitei287 – 2871SubstrateBy similarity
Binding sitei299 – 2991SubstrateBy similarity
Active sitei331 – 3311Proton acceptorBy similarity
Binding sitei398 – 3981SubstrateBy similarity
Binding sitei433 – 4331FADBy similarity
Binding sitei444 – 4441SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi59 – 646FADBy similarity
Nucleotide bindingi82 – 9716FADBy similarityAdd
BLAST
Nucleotide bindingi449 – 4502FADBy similarity

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: SGD
  • succinate dehydrogenase (ubiquinone) activity Source: SGD

GO - Biological processi

  • cellular respiration Source: SGD
  • mitochondrial electron transport, succinate to ubiquinone Source: SGD
  • tricarboxylic acid cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:YKL148C-MONOMER.
YEAST:YKL148C-MONOMER.
ReactomeiREACT_278278. Citric acid cycle (TCA cycle).
REACT_346640. Respiratory electron transport.
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC:1.3.5.1)
Alternative name(s):
Flavoprotein subunit of complex II
Short name:
FP
Gene namesi
Name:SDH1
Synonyms:SDHA
Ordered Locus Names:YKL148C
ORF Names:YKL602
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XI

Organism-specific databases

CYGDiYKL148c.
EuPathDBiFungiDB:YKL148C.
SGDiS000001631. SDH1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial membrane Source: SGD
  • mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901H → S: Abolishes covalent attachment of FAD. No effect on complex assembly. Abolishes succinate-dehydrogenase activity but no effect on fumarate reductase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828Mitochondrion2 PublicationsAdd
BLAST
Chaini29 – 640612Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialPRO_0000010342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901Tele-8alpha-FAD histidineBy similarity

Proteomic databases

MaxQBiQ00711.
PaxDbiQ00711.
PeptideAtlasiQ00711.
PRIDEiQ00711.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi33989. 56 interactions.
DIPiDIP-5853N.
IntActiQ00711. 5 interactions.
MINTiMINT-4817456.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ORZmodel-A29-640[»]
1PB4model-A29-640[»]
ProteinModelPortaliQ00711.
SMRiQ00711. Positions 45-640.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1053.
GeneTreeiENSGT00390000010046.
HOGENOMiHOG000160475.
InParanoidiQ00711.
KOiK00234.
OMAiETMELEN.
OrthoDBiEOG7V76G3.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProiIPR003953. 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]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLKKSALS KLTLLRNTRT FTSSALVRQT QGSVNGSASR SADGKYHIID
60 70 80 90 100
HEYDCVVIGA GGAGLRAAFG LAEAGYKTAC ISKLFPTRSH TVAAQGGINA
110 120 130 140 150
ALGNMHKDNW KWHMYDTVKG SDWLGDQDSI HYMTREAPKS IIELEHYGVP
160 170 180 190 200
FSRTENGKIY QRAFGGQTKE YGKGAQAYRT CAVADRTGHA LLHTLYGQAL
210 220 230 240 250
RHDTHFFIEY FALDLLTHNG EVVGVIAYNQ EDGTIHRFRA HKTIIATGGY
260 270 280 290 300
GRAYFSCTSA HTCTGDGNAM VSRAGFPLQD LEFVQFHPSG IYGSGCLITE
310 320 330 340 350
GARGEGGFLV NSEGERFMER YAPTAKDLAC RDVVSRAITM EIREGRGVGK
360 370 380 390 400
KKDHMYLQLS HLPPEVLKER LPGISETAAI FAGVDVTKEP IPIIPTVHYN
410 420 430 440 450
MGGIPTKWNG EALTIDEETG EDKVIPGLMA CGEAACVSVH GANRLGANSL
460 470 480 490 500
LDLVVFGRAV AHTVADTLQP GLPHKPLPSD LGKESIANLD KLRNANGSRS
510 520 530 540 550
TAEIRMNMKQ TMQKDVSVFR TQSSLDEGVR NITAVEKTFD DVKTTDRSMI
560 570 580 590 600
WNSDLVETLE LQNLLTCASQ TAVSAANRKE SRGAHAREDY PNRDDEHWMK
610 620 630 640
HTLSWQKDVA APVTLKYRRV IDHTLDEKEC PSVPPTVRAY
Length:640
Mass (Da):70,229
Last modified:April 1, 1993 - v1
Checksum:iA657E440B8ED58E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS34793.
RefSeqiNP_012774.1. NM_001179714.1.

Genome annotation databases

EnsemblFungiiYKL148C; YKL148C; YKL148C.
GeneIDi853709.
KEGGisce:YKL148C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS34793.
RefSeqiNP_012774.1. NM_001179714.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ORZmodel-A29-640[»]
1PB4model-A29-640[»]
ProteinModelPortaliQ00711.
SMRiQ00711. Positions 45-640.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33989. 56 interactions.
DIPiDIP-5853N.
IntActiQ00711. 5 interactions.
MINTiMINT-4817456.

Proteomic databases

MaxQBiQ00711.
PaxDbiQ00711.
PeptideAtlasiQ00711.
PRIDEiQ00711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL148C; YKL148C; YKL148C.
GeneIDi853709.
KEGGisce:YKL148C.

Organism-specific databases

CYGDiYKL148c.
EuPathDBiFungiDB:YKL148C.
SGDiS000001631. SDH1.

Phylogenomic databases

eggNOGiCOG1053.
GeneTreeiENSGT00390000010046.
HOGENOMiHOG000160475.
InParanoidiQ00711.
KOiK00234.
OMAiETMELEN.
OrthoDBiEOG7V76G3.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.
BioCyciMetaCyc:YKL148C-MONOMER.
YEAST:YKL148C-MONOMER.
ReactomeiREACT_278278. Citric acid cycle (TCA cycle).
REACT_346640. Respiratory electron transport.

Miscellaneous databases

NextBioi974713.
PROiQ00711.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProiIPR003953. 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]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. 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.

Entry informationi

Entry nameiSDHA_YEAST
AccessioniPrimary (citable) accession number: Q00711
Secondary accession number(s): D6VX49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 22, 2015
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 10400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.