Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial precursor

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q00711 (DHSA_YEAST)

Last modified June 16, 2009. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

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 names

Name:	SDH1
Synonyms:	SDHA
Ordered Locus Names:	YKL148C
ORF Names:	YKL602

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Hide | Top

Protein attributes

Sequence length	640 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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 + ubiquinone = fumarate + ubiquinol.
Cofactor	FAD.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
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.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. Ref.7
Miscellaneous	Present with 10400 molecules/cell in log phase SD medium. Ref.10
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Hide | Top

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	mitochondrial electron transport, succinate to ubiquinone Inferred from direct assay. Source: SGD transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred by curator. Source: SGD
Cellular component	mitochondrial respiratory chain complex II Inferred from direct assay. Source: SGD
Molecular function	FAD binding Inferred from direct assay. Source: SGD electron carrier activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct succinate dehydrogenase (ubiquinone) activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SDH2	P21801	1	EBI-5851,EBI-5856

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 28

Mitochondrion Ref.6 Ref.1

Chain

29 – 640

612

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

PRO_0000010342

Regions

Nucleotide binding

82 – 97

FAD By similarity

Sites

Active site

331

Proton acceptor By similarity

Binding site

287

Substrate By similarity

Binding site

299

Substrate By similarity

Binding site

398

Substrate By similarity

Binding site

444

Substrate By similarity

Amino acid modifications

Modified residue

Tele-8alpha-FAD histidine By similarity

Experimental info

Mutagenesis

H → S: Abolishes covalent attachment of FAD. No effect on complex assembly. Abolishes succinate-dehydrogenase activity but no effect on fumarate reductase activity. Ref.8

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q00711-1 [UniParc].

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

FASTA

640

70,229

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 1518827] [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: 1511876] [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: 1577780] [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: 8091859] [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. Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"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: 8120006] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-38. Strain: S288c / GRF88.
[7]	"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: 11502169] [Abstract] Cited for: PROTEIN SEQUENCE OF 607-615, SUBCELLULAR LOCATION. Strain: ATCC 201238 / W303-1B.
[8]	"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: 8026509] [Abstract] Cited for: MUTAGENESIS OF HIS-90.
[9]	"The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase." Lemire B.D., Oyedotun K.S. Biochim. Biophys. Acta 1553:102-116(2002) [PubMed: 11803020] [Abstract] Cited for: REVIEW ON SUCCINATE DEHYDROGENASE.
[10]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"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: 14672929] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 29-640.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

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.

PIR

S34793.

RefSeq

NP_012774.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ORZ	model	-	A	29-640	[»]
1PB4	model	-	A	29-640	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5853N.

IntAct

Q00711. 6 interactions.

Proteomic databases

PeptideAtlas

Q00711.

Genome annotation databases

Ensembl

YKL148C. Saccharomyces cerevisiae. [Contig view]

GeneID

853709.

GenomeReviews

Gene locus YKL148C in contig Y13137_GR.

KEGG

sce:YKL148C.

NMPDR

fig|4932.3.peg.3753.

Organism-specific databases

CYGD

YKL148c.

SGD

S000001631. SDH1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q00711.

OMA

Q00711. HEIASAG.

Enzyme and pathway databases

BRENDA

1.3.5.1. 250.

Gene expression databases

ArrayExpress

Q00711.

GermOnline

YKL148C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR003953. FAD_bind2_N.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR003952. FRD_SDH_FAD_BS.
IPR004112. Fum_Rdtase/Succ_DH_flav_C.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_frdA_Gneg.
[Graphical view]

Pfam

PF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

TIGRFAMs

TIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.

PROSITE

PS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

974713.

Hide | Top

Entry information

Entry name

DHSA_YEAST

Accession

Primary (citable) accession number: Q00711

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	June 16, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XI

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents