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Q9YHT1 (DHSA_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. 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
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] flavoprotein subunit, mitochondrial
EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit of complex II
Short name=Fp
Gene names
Name:SDHA
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Flavoprotein (FP) 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 + ubiquinone = fumarate + ubiquinol.

Cofactor

FAD.

Enzyme regulation

Inhibited by oxaloacetate.

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. Interacts with SDHAF2/SDH5; interaction is required for FAD attachment By similarity. Ref.3 Ref.4 Ref.5

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Ref.3 Ref.4 Ref.5.

Miscellaneous

The complex, present in mitochondria, can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone By similarity.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4444Mitochondrion
Chain45 – 665621Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
PRO_0000344984

Regions

Nucleotide binding69 – 746FAD
Nucleotide binding92 – 10716FAD
Nucleotide binding457 – 4582FAD

Sites

Active site3411Proton acceptor Ref.5
Binding site2761FAD
Binding site2971Substrate
Binding site3091Substrate
Binding site4081Substrate
Binding site4411FAD
Binding site4521Substrate

Amino acid modifications

Modified residue1001Tele-8alpha-FAD histidine

Secondary structure

1 ...................................................................................................... 665
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9YHT1 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 9476AA19A7A3AE84

FASTA66572,931
        10         20         30         40         50         60 
MAAVVAASRS LAKCWLRPAV RAWPAACQTH ARNFHFTVDG KKNASTKVSD SISTQYPVVD 

        70         80         90        100        110        120 
HEFDAVVVGA GGAGLRAAFG LSEAGFNTAC VTKLFPTRSH TVAAQGGINA ALGNMEDDNW 

       130        140        150        160        170        180 
RWHFYDTVKG SDWLGDQDAI HYMTEQAPAA VIELENYGMP FSRTEEGKIY QRAFGGQSLQ 

       190        200        210        220        230        240 
FGKGGQAHRC CCVADRTGHS LLHTLYGRSL RYDTSYFVEY FALDLLMENG ECRGVIALCI 

       250        260        270        280        290        300 
EDGTIHRFRA KNTVIATGGY GRTYFSCTSA HTSTGDGTAM VTRAGLPCQD LEFVQFHPTG 

       310        320        330        340        350        360 
IYGAGCLITE GCRGEGGILI NSQGERFMER YAPVAKDLAS RDVVSRSMTI EIREGRGCGP 

       370        380        390        400        410        420 
EKDHVYLQLH HLPPQQLATR LPGISETAMI FAGVDVTKEP IPVLPTVHYN MGGIPTNYKG 

       430        440        450        460        470        480 
QVITHVNGED KVVPGLYACG EAASASVHGA NRLGANSLLD LVVFGRACAL TIAETCKPGE 

       490        500        510        520        530        540 
PVPSIKPNAG EESVANLDKL RFADGTIRTS EARLNMQKTM QSHAAVFRTG SILQEGCEKL 

       550        560        570        580        590        600 
SQIYCDLAHL KTFDRGIVWN TDLVETLELQ NLMLCALQTI YGAEARKESR GAHAREDYKF 

       610        620        630        640        650        660 
RIDDFDYSKP LQGQQKRPFE EHWRKHTLSY VDVKSGKVTL KYRPVIDRTL NEEDCSSVPP 


AIRSY

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References

[1]"Detection of sequence polymorphisms in red junglefowl and white leghorn ESTs."
Fitzsimmons C.J., Savolainen P., Amini B., Hjaelm G., Lundeberg J., Andersson L.
Anim. Genet. 35:391-396(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-324.
[2]"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] OF 167-665.
Tissue: Heart.
[3]"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 45-665 IN COMPLEX WITH FAD, SUBUNIT, SUBCELLULAR LOCATION.
[4]"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 45-665 IN COMPLEXES WITH FAD AND MALONATE, SUBUNIT, SUBCELLULAR LOCATION.
[5]"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 45-665 IN COMPLEXES WITH FAD; OXALOACETATE AND 3-NITROPROPIONIC ACID, ACTIVE SITE, SUBUNIT, MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CO635738 mRNA. No translation available.
AF095939 mRNA. Translation: AAC72374.1.
IPIIPI00682371.
UniGeneGga.993.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YQ3X-ray2.20A45-665[»]
1YQ4X-ray2.33A45-665[»]
2FBWX-ray2.10A/N45-665[»]
2H88X-ray1.74A/N45-665[»]
2H89X-ray2.40A45-665[»]
2WQYX-ray2.10A/N45-665[»]
ProteinModelPortalQ9YHT1.
SMRQ9YHT1. Positions 52-665.
ModBaseSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000021475.

Proteomic databases

PaxDbQ9YHT1.
PRIDEQ9YHT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1053.
HOGENOMHOG000160475.
HOVERGENHBG001461.
InParanoidQ9YHT1.
OrthoDBEOG47H5PJ.

Enzyme and pathway databases

ReactomeREACT_115655. Metabolism.
UniPathwayUPA00223; UER01006.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PANTHERPTHR11632:SF5. PTHR11632:SF5. 1 hit.
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF46977. Succ_DH_flav_C. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9YHT1.

Entry information

Entry nameDHSA_CHICK
AccessionPrimary (citable) accession number: Q9YHT1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: April 3, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

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