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P21801

- SDHB_YEAST

UniProt

P21801 - SDHB_YEAST

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Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

SDH2

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

Functioni

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

Binds 1 2Fe-2S cluster.By similarity
Binds 1 3Fe-4S cluster.By similarity
Binds 1 4Fe-4S cluster.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi92 – 921Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi95 – 951Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi107 – 1071Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi179 – 1791Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi182 – 1821Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi185 – 1851Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi189 – 1891Iron-sulfur 3 (3Fe-4S)By similarity
Binding sitei194 – 1941Ubiquinone; shared with DHSDBy similarity
Metal bindingi236 – 2361Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi242 – 2421Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi246 – 2461Iron-sulfur 2 (4Fe-4S)By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 3 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  4. electron carrier activity Source: InterPro
  5. metal ion binding Source: UniProtKB-KW
  6. succinate dehydrogenase (ubiquinone) activity Source: SGD

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:YLL041C-MONOMER.
YEAST:YLL041C-MONOMER.
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SDH2
Synonyms:SDH, SDHB
Ordered Locus Names:YLL041C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLL041c.
SGDiS000003964. SDH2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial membrane Source: SGD
  2. mitochondrial respiratory chain complex II Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi260 – 2667Missing: Abolishes SDH activity and complex assembly. 1 Publication
Mutagenesisi260 – 2601K → T: Abolishes SDH activity. No effect on complex assembly and stability; when associated with T-261. 1 Publication
Mutagenesisi261 – 2611K → T: Abolishes SDH activity. No effect on complex assembly and stability; when associated with T-260. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – ?2020MitochondrionAdd
BLAST
Chaini?21 – 266246Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000010353Add
BLAST

Proteomic databases

MaxQBiP21801.
PaxDbiP21801.
PeptideAtlasiP21801.

Expressioni

Gene expression databases

GenevestigatoriP21801.

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.By similarity

Protein-protein interaction databases

BioGridi31272. 51 interactions.
DIPiDIP-5856N.
IntActiP21801. 5 interactions.
MINTiMINT-695166.
STRINGi4932.YLL041C.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ORZmodel-B21-266[»]
1PB4model-B21-266[»]
ProteinModelPortaliP21801.
SMRiP21801. Positions 30-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 127922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini169 – 199314Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0479.
GeneTreeiENSGT00390000013558.
HOGENOMiHOG000160590.
InParanoidiP21801.
KOiK00235.
OMAiIMNCSRT.
OrthoDBiEOG7X9GJ0.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 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]

Sequencei

Sequence statusi: Complete.

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

P21801-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLNVLLRRKA FCLVTKKGMA TATTAAATHT PRLKTFKVYR WNPDEPSAKP
60 70 80 90 100
HLQSYQVDLN DCGPMVLDAL LKIKDEQDST LTFRRSCREG ICGSCAMNIG
110 120 130 140 150
GRNTLACICK IDQNESKQLK IYPLPHMFIV KDLVPDLTNF YQQYKSIQPY
160 170 180 190 200
LQRSSFPKDG TEVLQSIEDR KKLDGLYECI LCACCSTSCP SYWWNQEQYL
210 220 230 240 250
GPAVLMQAYR WLIDSRDQAT KTRKAMLNNS MSLYRCHTIM NCTRTCPKGL
260
NPGLAIAEIK KSLAFA
Length:266
Mass (Da):30,231
Last modified:May 1, 1991 - v1
Checksum:iC14170F3670F6930
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05487 Genomic DNA. Translation: AAA35021.1.
Z73146 Genomic DNA. Translation: CAA97492.1.
AY558189 Genomic DNA. Translation: AAS56515.1.
BK006945 Genomic DNA. Translation: DAA09281.1.
PIRiA35435. RDBYIS.
RefSeqiNP_013059.1. NM_001181861.1.

Genome annotation databases

EnsemblFungiiYLL041C; YLL041C; YLL041C.
GeneIDi850685.
KEGGisce:YLL041C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05487 Genomic DNA. Translation: AAA35021.1 .
Z73146 Genomic DNA. Translation: CAA97492.1 .
AY558189 Genomic DNA. Translation: AAS56515.1 .
BK006945 Genomic DNA. Translation: DAA09281.1 .
PIRi A35435. RDBYIS.
RefSeqi NP_013059.1. NM_001181861.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ORZ model - B 21-266 [» ]
1PB4 model - B 21-266 [» ]
ProteinModelPortali P21801.
SMRi P21801. Positions 30-264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31272. 51 interactions.
DIPi DIP-5856N.
IntActi P21801. 5 interactions.
MINTi MINT-695166.
STRINGi 4932.YLL041C.

Proteomic databases

MaxQBi P21801.
PaxDbi P21801.
PeptideAtlasi P21801.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLL041C ; YLL041C ; YLL041C .
GeneIDi 850685.
KEGGi sce:YLL041C.

Organism-specific databases

CYGDi YLL041c.
SGDi S000003964. SDH2.

Phylogenomic databases

eggNOGi COG0479.
GeneTreei ENSGT00390000013558.
HOGENOMi HOG000160590.
InParanoidi P21801.
KOi K00235.
OMAi IMNCSRT.
OrthoDBi EOG7X9GJ0.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01006 .
BioCyci MetaCyc:YLL041C-MONOMER.
YEAST:YLL041C-MONOMER.

Miscellaneous databases

NextBioi 966692.
PROi P21801.

Gene expression databases

Genevestigatori P21801.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 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 ]
Pfami PF13085. Fer2_3. 1 hit.
[Graphical view ]
SUPFAMi SSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR00384. dhsB. 1 hit.
PROSITEi PS00197. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. 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.

Entry informationi

Entry nameiSDHB_YEAST
AccessioniPrimary (citable) accession number: P21801
Secondary accession number(s): D6VXW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 29, 2014
This is version 149 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 9540 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3