Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P21801 (DHSB_YEAST)

Last modified July 22, 2008. Version 94. History...

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

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Names and origin

Protein names

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(s)=Ip

Gene names

Name:	SDH2
Synonyms:	SDH, SDHB
Ordered Locus Names:	YLL041C

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	266 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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 + ubiquinone = fumarate + ubiquinol.
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.
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.

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Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	mitochondrial electron transport, succinate to ubiquinone Traceable author statement. Source: SGD tricarboxylic acid cycle Traceable author statement. Source: SGD
Cellular component	mitochondrial respiratory chain complex II Traceable author statement. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct succinate dehydrogenase (ubiquinone) activity Traceable author statement. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
SDH1	Q00711	1	EBI-5856,EBI-5851

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Transit peptide

1 – ?20

Mitochondrion

Chain

?21 – 266

246

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Regions

Domain

36 – 127

2Fe-2S ferredoxin-type

Domain

169 – 199

4Fe-4S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

107

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

179

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

182

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

185

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

189

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

236

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

242

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

246

Iron-sulfur 2 (4Fe-4S) By similarity

Binding site

194

Ubiquinone; shared with DHSD By similarity

Experimental info

Mutagenesis

260 – 266

Missing: Abolishes SDH activity and complex assembly

Mutagenesis

260

K → T: Abolishes SDH activity. No effect on complex assembly and stability; when associated with T-261

Mutagenesis

261

K → T: Abolishes SDH activity. No effect on complex assembly and stability; when associated with T-260

Secondary structure

266

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P21801-1 [UniParc].

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

266

30,231

        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

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References

	« Hide 'large scale' referencesShow '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: 2191948] [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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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.
[4]	"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: 2494655] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-242.
[5]	Erratum Gould S.J., Subramani S., Scheffler I.E. Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)
[6]	"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: 1390628] [Abstract] Cited for: MUTAGENESIS OF LYS-260; LYS-261 AND 260-LYS--ALA-266.
[7]	"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.
[8]	"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].
[9]	"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 21-266.

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Cross-references

Sequence databases

J05487 Genomic DNA. Translation: AAA35021.1.
Z73146 Genomic DNA. Translation: CAA97492.1.
AY558189 Genomic DNA. Translation: AAS56515.1.

PIR

RDBYIS. A35435.

RefSeq

NP_013059.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ORZ	model	-	B	21-266	[»]
1PB4	model	-	B	21-266	[»]

SMR

P21801. Positions 30-264.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5856N.

IntAct

P21801.

Proteomic databases

PeptideAtlas

P21801.

Genome annotation databases

Ensembl

YLL041C. Saccharomyces cerevisiae. [Contig view]

GeneID

850685.

GenomeReviews

Gene locus YLL041C in contig Y13138_GR.

KEGG

sce:YLL041C.

NMPDR

fig|4932.3.peg.4050.

Organism-specific databases

CYGD

YLL041c.

SGD

S000003964. SDH2.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P21801.

Gene expression databases

GermOnline

YLL041C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR006058. 2Fe2S_fd_BS.
IPR001450. 4Fe4S_Fe_S_bd.
IPR012675. b-grasp_ferredoxin-like.
IPR001041. Ferredoxin.
IPR012285. Fum_reductase_C.
IPR004489. Succ_DHase/fum_Rdtase_Fe-S.
[Graphical view]

Gene3D

G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.

Pfam

PF00111. Fer2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00384. dhsB. 1 hit.

PROSITE

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]

ProDom

P21801.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

LinkHub

P21801.

ProtoNet

Search...

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Entry information

Entry name

DHSB_YEAST

Accession

Primary (citable) accession number: P21801

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	July 22, 2008
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents