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

Contribute

Send feedback

Read comments (?) or add your own

P37298 (DHSD_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 104. History...

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

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

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] cytochrome b small subunit, mitochondrial
Short name=CybS

Alternative name(s):
Succinate-ubiquinone reductase membrane anchor subunit

Gene names

Name:	SDH4
Synonyms:	ACN18
Ordered Locus Names:	YDR178W
ORF Names:	YD9395.11

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	181 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	Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in system II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH3 and SDH4 form the membrane dimer that anchors the catalytic dimer formed by SDH1 and SDH2 to the matrix surface of the mitochondrial inner membrane. Electrons originating from the catalytic dimer enter the membrane dimer for ubiquinone reduction.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
Subunit structure	Forms part of complex II containing 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; Multi-pass membrane protein.
Miscellaneous	Present with 7920 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the CybS family.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding
PTM	Quinone
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	mitochondrial electron transport, succinate to ubiquinone Traceable author statement. Source: SGD transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Traceable author statement. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial respiratory chain complex II Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	heme binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquinone binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
ARO8	P53090	1	EBI-16796,EBI-2042933
GLN1	P32288	1	EBI-16796,EBI-7665
IPP1	P00817	1	EBI-16796,EBI-9338
RNR1	P21524	1	EBI-16796,EBI-15234

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 31

Mitochondrion Ref.1

Chain

32 – 181

150

Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial

PRO_0000006496

Regions

Topological domain

32 – 66

Mitochondrial matrix Potential

Transmembrane

67 – 88

Helical; Potential

Topological domain

89 – 98

Mitochondrial intermembrane Potential

Transmembrane

99 – 118

Helical; Potential

Topological domain

119 – 127

Mitochondrial matrix Potential

Transmembrane

128 – 148

Helical; Potential

Topological domain

149 – 181

Mitochondrial intermembrane Potential

Sites

Metal binding

109

Iron (heme axial ligand) Probable

Binding site

120

Ubiquinone; shared with IP/SDHB By similarity

Experimental info

Mutagenesis

100

F → V: Impairs respiratory growth and reduces quinone reductase activity. Ref.5

Mutagenesis

102

S → A: Impairs respiratory growth and reduces quinone reductase activity. Ref.5

Mutagenesis

109

C → A: Decreases SDH cytochrome b content. Ref.8

Mutagenesis

120

Y → C: Abolishes quinone reductase activity. Little effect on complex assembly. Ref.9

Mutagenesis

130

H → L: Reduces SDH FAD content. Probably impairs complex assembly. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P37298 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 80D76A32E7E6DA70
Show »

FASTA

181

20,249

        10         20         30         40         50         60 
MMLPRSMKFM TGRRIFHTAT VRAFQSTAKK SLTIPFLPVL PQKPGGVRGT PNDAYVPPPE 

        70         80         90        100        110        120 
NKLEGSYHWY MEKIFALSVV PLATTAMLTT GPLSTAADSF FSVMLLGYCY MEFNSCITDY 

       130        140        150        160        170        180 
ISERVYGVWH KYAMYMLGLG SAVSLFGIYK LETENDGVVG LVKSLWDSSE KDNSQKIEAK 


K

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 32-62. Strain: S288c / GRF88.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"The quinone-binding sites of the Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase." Oyedotun K.S., Lemire B.D. J. Biol. Chem. 276:16936-16943(2001) [PubMed: 11279023] [Abstract] Cited for: MUTAGENESIS OF PHE-100; SER-102 AND HIS-130.
[6]	"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.
[7]	"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].
[8]	"Identification of the heme axial ligands in the cytochrome b562 of the Saccharomyces cerevisiae succinate dehydrogenase." Oyedotun K.S., Yau P.F., Lemire B.D. J. Biol. Chem. 279:9432-9439(2004) [PubMed: 14672930] [Abstract] Cited for: MUTAGENESIS OF CYS-109.
[9]	"The role of Sdh4p Tyr-89 in ubiquinone reduction by the Saccharomyces cerevisiae succinate dehydrogenase." Silkin Y., Oyedotun K.S., Lemire B.D. Biochim. Biophys. Acta 1767:143-150(2007) [PubMed: 17208193] [Abstract] Cited for: MUTAGENESIS OF TYR-120.
[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: 14672929] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 32-181.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L26333 Unassigned RNA. Translation: AAA19637.1.
Z46727 Genomic DNA. Translation: CAA86683.1.
AY557671 Genomic DNA. Translation: AAS55997.1.
BK006938 Genomic DNA. Translation: DAA12020.1.

PIR

A54380.

RefSeq

NP_010463.1. NM_001180485.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ORZ	model	-	D	32-181	[»]
1PB4	model	-	D	32-181	[»]

ProteinModelPortal

P37298.

SMR

P37298. Positions 61-167.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5704N.

IntAct

P37298. 5 interactions.

MINT

MINT-472835.

STRING

P37298.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR178W; YDR178W; YDR178W.

GeneID

851758.

KEGG

sce:YDR178W.

NMPDR

fig|4932.3.peg.1213.

Organism-specific databases

CYGD

YDR178w.

SGD

S000002585. SDH4.

Phylogenomic databases

eggNOG

fuNOG11696.

GeneTree

EFGT00050000005635.

HOGENOM

HBG734876.

OMA

RIFHTAT.

OrthoDB

EOG4W9NDM.

Gene expression databases

ArrayExpress

P37298.

Genevestigator

P37298.

GermOnline

YDR178W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR007992. Cyt_b_succ_DH_CybS.
[Graphical view]

K00237.

PANTHER

PTHR13337. CybS. 1 hit.

Pfam

PF05328. CybS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

969528.

Entry information

Entry name

DHSD_YEAST

Accession

Primary (citable) accession number: P37298
Secondary accession number(s): D6VSG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	December 14, 2011
This is version 104 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

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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents