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Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene

SDHA

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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).1 Publication

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.1 Publication

Cofactori

FAD3 Publications

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes fumarate from succinate (eukaryal route).1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SDHB), Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (SDHA), Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (SDHA)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes fumarate from succinate (eukaryal route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei276FAD3 Publications1
Binding sitei297Substrate2 Publications1
Binding sitei309Substrate2 Publications1
Active sitei341Proton acceptor1 Publication1
Binding sitei408Substrate2 Publications1
Binding sitei441FAD3 Publications1
Binding sitei452Substrate2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi69 – 74FAD3 Publications6
Nucleotide bindingi92 – 107FAD3 PublicationsAdd BLAST16
Nucleotide bindingi457 – 458FAD3 Publications2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-GGA-372987. The tricarboxylic acid cycle.
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC:1.3.5.11 Publication)
Alternative name(s):
Flavoprotein subunit of complex II
Short name:
Fp
Gene namesi
Name:SDHA
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 44Mitochondrion3 PublicationsAdd BLAST44
ChainiPRO_000034498445 – 665Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialAdd BLAST621

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei100Tele-8alpha-FAD histidine2 Publications1

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.3 Publications

Protein-protein interaction databases

STRINGi9031.ENSGALP00000021475.

Structurei

Secondary structure

1665
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi58 – 68Combined sources11
Helixi72 – 83Combined sources12
Beta strandi88 – 94Combined sources7
Helixi96 – 98Combined sources3
Helixi100 – 103Combined sources4
Beta strandi114 – 116Combined sources3
Helixi120 – 130Combined sources11
Turni131 – 133Combined sources3
Helixi137 – 156Combined sources20
Beta strandi167 – 169Combined sources3
Beta strandi171 – 179Combined sources9
Turni180 – 183Combined sources4
Beta strandi186 – 191Combined sources6
Helixi197 – 209Combined sources13
Beta strandi215 – 218Combined sources4
Beta strandi220 – 228Combined sources9
Beta strandi231 – 239Combined sources9
Turni240 – 242Combined sources3
Beta strandi245 – 255Combined sources11
Helixi261 – 263Combined sources3
Beta strandi264 – 269Combined sources6
Helixi276 – 283Combined sources8
Beta strandi294 – 301Combined sources8
Turni302 – 304Combined sources3
Helixi311 – 314Combined sources4
Beta strandi318 – 320Combined sources3
Helixi328 – 331Combined sources4
Turni333 – 335Combined sources3
Helixi336 – 338Combined sources3
Helixi341 – 353Combined sources13
Turni354 – 356Combined sources3
Turni359 – 362Combined sources4
Beta strandi364 – 368Combined sources5
Helixi374 – 380Combined sources7
Helixi382 – 392Combined sources11
Turni396 – 398Combined sources3
Beta strandi401 – 411Combined sources11
Beta strandi413 – 416Combined sources4
Beta strandi420 – 426Combined sources7
Beta strandi429 – 438Combined sources10
Helixi440 – 442Combined sources3
Beta strandi446 – 448Combined sources3
Helixi457 – 475Combined sources19
Turni487 – 490Combined sources4
Helixi491 – 501Combined sources11
Beta strandi504 – 508Combined sources5
Helixi509 – 523Combined sources15
Beta strandi524 – 528Combined sources5
Helixi530 – 545Combined sources16
Helixi546 – 549Combined sources4
Helixi561 – 585Combined sources25
Beta strandi595 – 598Combined sources4
Helixi619 – 621Combined sources3
Beta strandi625 – 632Combined sources8
Turni633 – 636Combined sources4
Beta strandi637 – 644Combined sources8
Turni652 – 654Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9YHT1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2403. Eukaryota.
COG1053. LUCA.
HOGENOMiHOG000160475.
HOVERGENiHBG001461.
InParanoidiQ9YHT1.
KOiK00234.
PhylomeDBiQ9YHT1.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.50.50.60. 2 hits.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD-binding_2.
IPR023753. FAD/NAD-binding_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR030664. SdhA/FrdA/AprA.
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]
PIRSFiPIRSF000171. SDHA_APRA_LASPO. 1 hit.
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF51905. SSF51905. 2 hits.
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.
RefSeqiNP_001264327.1. NM_001277398.1.
UniGeneiGga.993.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000021475.

Proteomic databases

PaxDbiQ9YHT1.
PRIDEiQ9YHT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi395758.
KEGGigga:395758.

Organism-specific databases

CTDi6389.

Phylogenomic databases

eggNOGiKOG2403. Eukaryota.
COG1053. LUCA.
HOGENOMiHOG000160475.
HOVERGENiHBG001461.
InParanoidiQ9YHT1.
KOiK00234.
PhylomeDBiQ9YHT1.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.
ReactomeiR-GGA-372987. The tricarboxylic acid cycle.

Miscellaneous databases

EvolutionaryTraceiQ9YHT1.
PROiQ9YHT1.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.50.50.60. 2 hits.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD-binding_2.
IPR023753. FAD/NAD-binding_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR030664. SdhA/FrdA/AprA.
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]
PIRSFiPIRSF000171. SDHA_APRA_LASPO. 1 hit.
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF51905. SSF51905. 2 hits.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.