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P21801 (SDHB_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. 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] iron-sulfur subunit, mitochondrial

EC=1.3.5.1
Alternative name(s):
Iron-sulfur subunit of complex II
Short name=Ip
Gene names
Name:SDH2
Synonyms:SDH, SDHB
Ordered Locus Names:YLL041C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Binds 1 2Fe-2S cluster By similarity.

Binds 1 3Fe-4S cluster By similarity.

Binds 1 4Fe-4S cluster By similarity.

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 By similarity.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.

Miscellaneous

Present with 9540 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 4Fe-4S ferredoxin-type domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SDH1Q007112EBI-5856,EBI-5851

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?2020Mitochondrion
Chain?21 – 266246Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
PRO_0000010353

Regions

Domain36 – 127922Fe-2S ferredoxin-type
Domain169 – 199314Fe-4S ferredoxin-type

Sites

Metal binding871Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding921Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding951Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1071Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1791Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1821Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1851Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1891Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2361Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2421Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2461Iron-sulfur 2 (4Fe-4S) By similarity
Binding site1941Ubiquinone; shared with DHSD By similarity

Experimental info

Mutagenesis260 – 2667Missing: Abolishes SDH activity and complex assembly. Ref.7
Mutagenesis2601K → T: Abolishes SDH activity. No effect on complex assembly and stability; when associated with T-261. Ref.7
Mutagenesis2611K → T: Abolishes SDH activity. No effect on complex assembly and stability; when associated with T-260. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P21801 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: C14170F3670F6930

FASTA26630,231
        10         20         30         40         50         60 
MLNVLLRRKA FCLVTKKGMA TATTAAATHT PRLKTFKVYR WNPDEPSAKP HLQSYQVDLN 

        70         80         90        100        110        120 
DCGPMVLDAL LKIKDEQDST LTFRRSCREG ICGSCAMNIG GRNTLACICK IDQNESKQLK 

       130        140        150        160        170        180 
IYPLPHMFIV KDLVPDLTNF YQQYKSIQPY LQRSSFPKDG TEVLQSIEDR KKLDGLYECI 

       190        200        210        220        230        240 
LCACCSTSCP SYWWNQEQYL GPAVLMQAYR WLIDSRDQAT KTRKAMLNNS MSLYRCHTIM 

       250        260 
NCTRTCPKGL NPGLAIAEIK KSLAFA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the iron-sulfur subunit gene of succinate dehydrogenase from Saccharomyces cerevisiae."
Lombardo A., Carine K., Scheffler I.E.
J. Biol. Chem. 265:10419-10423(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species."
Gould S.J., Subramani S., Scheffler I.E.
Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-242.
[6]Erratum
Gould S.J., Subramani S., Scheffler I.E.
Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)
[7]"The C-terminus of the succinate dehydrogenase IP peptide of Saccharomyces cerevisiae is significant for assembly of complex II."
Schmidt D.M., Saghbini M., Scheffler I.E.
Biochemistry 31:8442-8448(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-260; LYS-261 AND 260-LYS--ALA-266.
[8]"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.
[9]"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].
[10]"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 21-266.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05487 Genomic DNA. Translation: AAA35021.1.
Z73146 Genomic DNA. Translation: CAA97492.1.
AY558189 Genomic DNA. Translation: AAS56515.1.
BK006945 Genomic DNA. Translation: DAA09281.1.
PIRRDBYIS. A35435.
RefSeqNP_013059.1. NM_001181861.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ORZmodel-B21-266[»]
1PB4model-B21-266[»]
ProteinModelPortalP21801.
SMRP21801. Positions 30-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31272. 50 interactions.
DIPDIP-5856N.
IntActP21801. 4 interactions.
MINTMINT-695166.
STRING4932.YLL041C.

Proteomic databases

PaxDbP21801.
PeptideAtlasP21801.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLL041C; YLL041C; YLL041C.
GeneID850685.
KEGGsce:YLL041C.

Organism-specific databases

CYGDYLL041c.
SGDS000003964. SDH2.

Phylogenomic databases

eggNOGCOG0479.
GeneTreeENSGT00390000013558.
HOGENOMHOG000160590.
KOK00235.
OMADSHERML.
OrthoDBEOG7X9GJ0.

Enzyme and pathway databases

BioCycMetaCyc:YLL041C-MONOMER.
YEAST:YLL041C-MONOMER.
UniPathwayUPA00223; UER01006.

Gene expression databases

GenevestigatorP21801.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR00384. dhsB. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966692.
PROP21801.

Entry information

Entry nameSDHB_YEAST
AccessionPrimary (citable) accession number: P21801
Secondary accession number(s): D6VXW5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 146 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 XII

Yeast (Saccharomyces cerevisiae) chromosome XII: 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