Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q00711 (DHSA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 140. History...

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

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

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

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; 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.

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 Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial electron transport, succinate to ubiquinone Inferred from direct assay PubMed 2826438. Source: SGD tricarboxylic acid cycle Inferred by curator PubMed 13445213. Source: SGD
Cellular_component	mitochondrial respiratory chain complex II Inferred from direct assay PubMed 9822678. Source: SGD
Molecular_function	flavin adenine dinucleotide binding Inferred from direct assay PubMed 18279395. Source: SGD succinate dehydrogenase (ubiquinone) activity Inferred from direct assay PubMed 13445213. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SDH2	P21801	2	EBI-5851,EBI-5856

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 28

Mitochondrion Ref.1 Ref.7

Chain

29 – 640

612

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

PRO_0000010342

Regions

Nucleotide binding

59 – 64

FAD By similarity

Nucleotide binding

82 – 97

FAD By similarity

Nucleotide binding

449 – 450

FAD By similarity

Sites

Active site

331

Proton acceptor By similarity

Binding site

266

FAD By similarity

Binding site

287

Substrate By similarity

Binding site

299

Substrate By similarity

Binding site

398

Substrate By similarity

Binding site

433

FAD 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.9

Sequences

Sequence

Length

Mass (Da)

Tools

Q00711 [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

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] [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. 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.

PIR

S34793.

RefSeq

NP_012774.1. NM_001179714.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q00711.

SMR

Q00711. Positions 45-640.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5853N.

IntAct

Q00711. 5 interactions.

STRING

4932.YKL148C.

Proteomic databases

PaxDb

Q00711.

PeptideAtlas

Q00711.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YKL148C; YKL148C; YKL148C.

GeneID

853709.

KEGG

sce:YKL148C.

Organism-specific databases

CYGD

YKL148c.

SGD

S000001631. SDH1.

Phylogenomic databases

eggNOG

COG1053.

GeneTree

ENSGT00700000105263.

HOGENOM

HOG000160475.

K00234.

OMA

NIRTISF.

OrthoDB

EOG41G6C9.

Enzyme and pathway databases

UniPathway

UPA00223; UER01006.

Gene expression databases

Genevestigator

Q00711.

GermOnline

YKL148C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.20.58.100. 1 hit.

InterPro

IPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]

PANTHER

PTHR11632:SF5. PTHR11632:SF5. 1 hit.

Pfam

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

SUPFAM

SSF46977. Succ_DH_flav_C. 1 hit.

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

NextBio

974713.

Entry information

Entry name

DHSA_YEAST

Accession

Primary (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 3, 2013
This is version 140 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XI

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

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

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents