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Q9YHT2 (SDHB_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:SDHB
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Iron-sulfur protein (IP) 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).

Catalytic activity

Succinate + a quinone = fumarate + a quinol.

Cofactor

Binds 1 2Fe-2S cluster.

Binds 1 3Fe-4S cluster.

Binds 1 4Fe-4S cluster.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.

Subunit structure

Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD. Ref.2 Ref.3 Ref.4

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Ref.2 Ref.3 Ref.4.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion
Chain39 – 290252Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
PRO_0000343800

Regions

Domain50 – 143942Fe-2S ferredoxin-type
Domain186 – 216314Fe-4S ferredoxin-type

Sites

Metal binding1031Iron-sulfur 1 (2Fe-2S)
Metal binding1081Iron-sulfur 1 (2Fe-2S)
Metal binding1111Iron-sulfur 1 (2Fe-2S)
Metal binding1231Iron-sulfur 1 (2Fe-2S)
Metal binding1961Iron-sulfur 2 (4Fe-4S)
Metal binding1991Iron-sulfur 2 (4Fe-4S)
Metal binding2021Iron-sulfur 2 (4Fe-4S)
Metal binding2061Iron-sulfur 3 (3Fe-4S)
Metal binding2531Iron-sulfur 3 (3Fe-4S)
Metal binding2591Iron-sulfur 3 (3Fe-4S)
Metal binding2631Iron-sulfur 2 (4Fe-4S)
Binding site2111Ubiquinone; shared with DHSD

Secondary structure

........................................... 290
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9YHT2 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 313E698866B3FDFC

FASTA29032,597
        10         20         30         40         50         60 
MAAAVVGVSL RRGVPARFLR AGLRPVRGLE AVHGICRGAQ TAAAATSRIK KFSIYRWDPD 

        70         80         90        100        110        120 
KPGDKPRMQT YEVDLNKCGP MVLDALIKIK NELDSTLTFR RSCREGICGS CAMNIAGGNT 

       130        140        150        160        170        180 
LACTKKIDPD LSKTTKIYPL PHMYVVKDLV PDLSNFYAQY KSIEPYLKKK DESKQGKEQY 

       190        200        210        220        230        240 
LQSIEDRQKL DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDYTEER 

       250        260        270        280        290 
LAQLQDPFSL YRCHTIMNCT RTCPKGLNPG KAIAEIKKMM ATYKEKAAAA 

« Hide

References

[1]"OXPHOS genes in mammals and the molecular clock."
Weinreich D.M.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"Crystallization of mitochondrial respiratory complex II from chicken heart: a membrane-protein complex diffracting to 2.0 A."
Huang L.-S., Borders T.M., Shen J.T., Wang C.-J., Berry E.A.
Acta Crystallogr. D 61:380-387(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OF 39-290, SUBUNIT, SUBCELLULAR LOCATION.
[3]"Crystallographic studies of the binding of ligands to the dicarboxylate site of complex II, and the identity of the ligand in the 'oxaloacetate-inhibited' state."
Huang L.-S., Shen J.T., Wang A.C., Berry E.A.
Biochim. Biophys. Acta 1757:1073-1083(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF OF 39-290 IN COMPLEX WITH UBIQUINONE AND IRON-SULFUR CENTERS, SUBUNIT, SUBCELLULAR LOCATION.
[4]"3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme."
Huang L.-S., Sun G., Cobessi D., Wang A.C., Shen J.T., Tung E.Y., Anderson V.E., Berry E.A.
J. Biol. Chem. 281:5965-5972(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 39-290 IN COMPLEX WITH UBIQUINONE AND IRON-SULFUR CENTERS, SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF095937 mRNA. Translation: AAC72372.1.
UniGeneGga.4743.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YQ3X-ray2.20B39-290[»]
1YQ4X-ray2.33B39-290[»]
2FBWX-ray2.10B/O39-290[»]
2H88X-ray1.74B/O39-290[»]
2H89X-ray2.40B39-290[»]
2WQYX-ray2.10B/O39-290[»]
ProteinModelPortalQ9YHT2.
SMRQ9YHT2. Positions 44-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000000693.

Proteomic databases

PaxDbQ9YHT2.
PRIDEQ9YHT2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0479.
HOGENOMHOG000160590.
HOVERGENHBG005483.
InParanoidQ9YHT2.
PhylomeDBQ9YHT2.

Enzyme and pathway databases

ReactomeREACT_115655. Metabolism.
UniPathwayUPA00223; UER01006.

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

EvolutionaryTraceQ9YHT2.
NextBio20920287.
PROQ9YHT2.

Entry information

Entry nameSDHB_CHICK
AccessionPrimary (citable) accession number: Q9YHT2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

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