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Q9YHT1

- SDHA_CHICK

UniProt

Q9YHT1 - SDHA_CHICK

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Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene

SDHA

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Enzyme regulationi

Inhibited by oxaloacetate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei276 – 2761FAD1 Publication
Binding sitei297 – 2971Substrate
Binding sitei309 – 3091Substrate
Active sitei341 – 3411Proton acceptor1 Publication
Binding sitei408 – 4081Substrate
Binding sitei441 – 4411FAD1 Publication
Binding sitei452 – 4521Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi69 – 746FAD1 Publication
Nucleotide bindingi92 – 10716FAD1 PublicationAdd
BLAST
Nucleotide bindingi457 – 4582FAD1 Publication

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

GO - Biological processi

  1. respiratory electron transport chain Source: UniProtKB
  2. small molecule metabolic process Source: Reactome
  3. succinate metabolic process Source: UniProtKB
  4. tricarboxylic acid cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_115536. The tricarboxylic acid cycle.
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC:1.3.5.1)
Alternative name(s):
Flavoprotein subunit of complex II
Short name:
Fp
Gene namesi
Name:SDHA
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Mitochondrion inner membrane 3 Publications; Peripheral membrane protein 3 Publications; Matrix side 3 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4444MitochondrionAdd
BLAST
Chaini45 – 665621Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialPRO_0000344984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001Tele-8alpha-FAD histidine

Proteomic databases

PaxDbiQ9YHT1.
PRIDEiQ9YHT1.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi9031.ENSGALP00000021475.

Structurei

Secondary structure

1
665
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 6811Combined sources
Helixi72 – 8312Combined sources
Beta strandi88 – 947Combined sources
Helixi96 – 983Combined sources
Helixi100 – 1034Combined sources
Beta strandi114 – 1163Combined sources
Helixi120 – 13011Combined sources
Turni131 – 1333Combined sources
Helixi137 – 15620Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi171 – 1799Combined sources
Turni180 – 1834Combined sources
Beta strandi186 – 1916Combined sources
Helixi197 – 20913Combined sources
Beta strandi215 – 2184Combined sources
Beta strandi220 – 2289Combined sources
Beta strandi231 – 2399Combined sources
Turni240 – 2423Combined sources
Beta strandi245 – 25511Combined sources
Helixi261 – 2633Combined sources
Beta strandi264 – 2696Combined sources
Helixi276 – 2838Combined sources
Beta strandi294 – 3018Combined sources
Turni302 – 3043Combined sources
Helixi311 – 3144Combined sources
Beta strandi318 – 3203Combined sources
Helixi328 – 3314Combined sources
Turni333 – 3353Combined sources
Helixi336 – 3383Combined sources
Helixi341 – 35313Combined sources
Turni354 – 3563Combined sources
Turni359 – 3624Combined sources
Beta strandi364 – 3685Combined sources
Helixi374 – 3807Combined sources
Helixi382 – 39211Combined sources
Turni396 – 3983Combined sources
Beta strandi401 – 41111Combined sources
Beta strandi413 – 4164Combined sources
Beta strandi420 – 4267Combined sources
Beta strandi429 – 43810Combined sources
Helixi440 – 4423Combined sources
Beta strandi446 – 4483Combined sources
Helixi457 – 47519Combined sources
Turni487 – 4904Combined sources
Helixi491 – 50111Combined sources
Beta strandi504 – 5085Combined sources
Helixi509 – 52315Combined sources
Beta strandi524 – 5285Combined sources
Helixi530 – 54516Combined sources
Helixi546 – 5494Combined sources
Helixi561 – 58525Combined sources
Beta strandi595 – 5984Combined sources
Helixi619 – 6213Combined sources
Beta strandi625 – 6328Combined sources
Turni633 – 6364Combined sources
Beta strandi637 – 6448Combined sources
Turni652 – 6543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9YHT1.
SMRiQ9YHT1. Positions 52-665.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9YHT1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1053.
HOGENOMiHOG000160475.
HOVERGENiHBG001461.
InParanoidiQ9YHT1.
KOiK00234.
PhylomeDBiQ9YHT1.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9YHT1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVVAASRS LAKCWLRPAV RAWPAACQTH ARNFHFTVDG KKNASTKVSD
60 70 80 90 100
SISTQYPVVD HEFDAVVVGA GGAGLRAAFG LSEAGFNTAC VTKLFPTRSH
110 120 130 140 150
TVAAQGGINA ALGNMEDDNW RWHFYDTVKG SDWLGDQDAI HYMTEQAPAA
160 170 180 190 200
VIELENYGMP FSRTEEGKIY QRAFGGQSLQ FGKGGQAHRC CCVADRTGHS
210 220 230 240 250
LLHTLYGRSL RYDTSYFVEY FALDLLMENG ECRGVIALCI EDGTIHRFRA
260 270 280 290 300
KNTVIATGGY GRTYFSCTSA HTSTGDGTAM VTRAGLPCQD LEFVQFHPTG
310 320 330 340 350
IYGAGCLITE GCRGEGGILI NSQGERFMER YAPVAKDLAS RDVVSRSMTI
360 370 380 390 400
EIREGRGCGP EKDHVYLQLH HLPPQQLATR LPGISETAMI FAGVDVTKEP
410 420 430 440 450
IPVLPTVHYN MGGIPTNYKG QVITHVNGED KVVPGLYACG EAASASVHGA
460 470 480 490 500
NRLGANSLLD LVVFGRACAL TIAETCKPGE PVPSIKPNAG EESVANLDKL
510 520 530 540 550
RFADGTIRTS EARLNMQKTM QSHAAVFRTG SILQEGCEKL SQIYCDLAHL
560 570 580 590 600
KTFDRGIVWN TDLVETLELQ NLMLCALQTI YGAEARKESR GAHAREDYKF
610 620 630 640 650
RIDDFDYSKP LQGQQKRPFE EHWRKHTLSY VDVKSGKVTL KYRPVIDRTL
660
NEEDCSSVPP AIRSY
Length:665
Mass (Da):72,931
Last modified:July 22, 2008 - v2
Checksum:i9476AA19A7A3AE84
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CO635738 mRNA. No translation available.
AF095939 mRNA. Translation: AAC72374.1.
RefSeqiNP_001264327.1. NM_001277398.1.
UniGeneiGga.993.

Genome annotation databases

GeneIDi395758.
KEGGigga:395758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CO635738 mRNA. No translation available.
AF095939 mRNA. Translation: AAC72374.1 .
RefSeqi NP_001264327.1. NM_001277398.1.
UniGenei Gga.993.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YQ3 X-ray 2.20 A 45-665 [» ]
1YQ4 X-ray 2.33 A 45-665 [» ]
2FBW X-ray 2.10 A/N 45-665 [» ]
2H88 X-ray 1.74 A/N 45-665 [» ]
2H89 X-ray 2.40 A 45-665 [» ]
2WQY X-ray 2.10 A/N 45-665 [» ]
ProteinModelPortali Q9YHT1.
SMRi Q9YHT1. Positions 52-665.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000021475.

Proteomic databases

PaxDbi Q9YHT1.
PRIDEi Q9YHT1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 395758.
KEGGi gga:395758.

Organism-specific databases

CTDi 6389.

Phylogenomic databases

eggNOGi COG1053.
HOGENOMi HOG000160475.
HOVERGENi HBG001461.
InParanoidi Q9YHT1.
KOi K00234.
PhylomeDBi Q9YHT1.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01006 .
Reactomei REACT_115536. The tricarboxylic acid cycle.

Miscellaneous databases

EvolutionaryTracei Q9YHT1.
PROi Q9YHT1.

Family and domain databases

Gene3Di 1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProi IPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view ]
Pfami PF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view ]
SUPFAMi SSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsi TIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEi PS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSDHA_CHICK
AccessioniPrimary (citable) accession number: Q9YHT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: November 26, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3