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Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene

SDHA

Organism
Sus scrofa (Pig)
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) (Probable). Can act as a tumor suppressor (By similarity).By similarity1 Publication

Catalytic activityi

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

Cofactori

FAD1 Publication

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] 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 sitei275FAD1 Publication1
Binding sitei296Substrate1 Publication1
Binding sitei308Substrate1 Publication1
Active sitei340Proton acceptorBy similarity1
Binding sitei407Substrate1 Publication1
Binding sitei440FAD1 Publication1
Binding sitei451Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi68 – 73FAD1 Publication6
Nucleotide bindingi91 – 106FAD1 PublicationAdd BLAST16
Nucleotide bindingi456 – 457FAD1 Publication2

GO - Molecular functioni

GO - Biological processi

  • anaerobic respiration Source: GO_Central
  • mitochondrial electron transport, succinate to ubiquinone Source: GO_Central
  • oxidation-reduction process Source: UniProtKB
  • respiratory electron transport chain Source: UniProtKB
  • tricarboxylic acid cycle Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 42Mitochondrion1 PublicationAdd BLAST42
ChainiPRO_000039171843 – 664Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialAdd BLAST622

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei99Tele-8alpha-FAD histidine1 Publication1
Modified residuei167N6-acetyllysineBy similarity1
Modified residuei179N6-acetyllysine; alternateBy similarity1
Modified residuei179N6-succinyllysine; alternateBy similarity1
Modified residuei182N6-acetyllysineBy similarity1
Modified residuei215Phosphotyrosine; by SRCBy similarity1
Modified residuei335N6-acetyllysine; alternateBy similarity1
Modified residuei335N6-succinyllysine; alternateBy similarity1
Modified residuei480N6-acetyllysineBy similarity1
Modified residuei485N6-acetyllysine; alternateBy similarity1
Modified residuei485N6-succinyllysine; alternateBy similarity1
Modified residuei498N6-acetyllysine; alternateBy similarity1
Modified residuei498N6-succinyllysine; alternateBy similarity1
Modified residuei517N6-acetyllysineBy similarity1
Modified residuei538N6-acetyllysine; alternateBy similarity1
Modified residuei538N6-succinyllysine; alternateBy similarity1
Modified residuei550N6-acetyllysineBy similarity1
Modified residuei598N6-acetyllysineBy similarity1
Modified residuei608N6-acetyllysineBy similarity1
Modified residuei615N6-succinyllysineBy similarity1
Modified residuei624N6-acetyllysineBy similarity1
Modified residuei633N6-acetyllysineBy similarity1
Modified residuei636N6-acetyllysineBy similarity1
Modified residuei647N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylation at Tyr-215 is important for efficient electron transfer in complex II and the prevention of ROS generation.By similarity
Acetylated. Deacetylated by SIRT3.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PeptideAtlasiQ0QF01.
PRIDEiQ0QF01.

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 (PubMed:15989954, PubMed:17480203). Interacts with SDHAF2/SDH5; interaction is required for FAD attachment (By similarity). Interacts with TRAP1 (By similarity).By similarity2 Publications

Structurei

Secondary structure

1664
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi57 – 61Combined sources5
Beta strandi63 – 67Combined sources5
Helixi71 – 82Combined sources12
Beta strandi87 – 93Combined sources7
Helixi95 – 97Combined sources3
Helixi99 – 102Combined sources4
Beta strandi113 – 115Combined sources3
Helixi119 – 129Combined sources11
Turni130 – 132Combined sources3
Helixi136 – 156Combined sources21
Beta strandi166 – 168Combined sources3
Beta strandi170 – 178Combined sources9
Turni179 – 182Combined sources4
Beta strandi185 – 190Combined sources6
Helixi196 – 208Combined sources13
Turni209 – 212Combined sources4
Beta strandi214 – 217Combined sources4
Beta strandi219 – 227Combined sources9
Beta strandi230 – 238Combined sources9
Turni239 – 241Combined sources3
Beta strandi244 – 248Combined sources5
Beta strandi250 – 254Combined sources5
Helixi260 – 262Combined sources3
Beta strandi263 – 268Combined sources6
Helixi275 – 282Combined sources8
Turni289 – 291Combined sources3
Beta strandi293 – 297Combined sources5
Turni301 – 303Combined sources3
Helixi310 – 314Combined sources5
Beta strandi317 – 319Combined sources3
Beta strandi323 – 325Combined sources3
Turni327 – 329Combined sources3
Turni332 – 336Combined sources5
Helixi340 – 353Combined sources14
Beta strandi357 – 361Combined sources5
Beta strandi365 – 367Combined sources3
Beta strandi369 – 371Combined sources3
Helixi375 – 378Combined sources4
Helixi381 – 391Combined sources11
Turni395 – 397Combined sources3
Beta strandi400 – 402Combined sources3
Beta strandi405 – 409Combined sources5
Beta strandi412 – 415Combined sources4
Beta strandi419 – 425Combined sources7
Beta strandi428 – 437Combined sources10
Helixi439 – 441Combined sources3
Beta strandi442 – 444Combined sources3
Helixi456 – 474Combined sources19
Turni486 – 489Combined sources4
Helixi490 – 500Combined sources11
Beta strandi505 – 507Combined sources3
Helixi508 – 522Combined sources15
Beta strandi523 – 527Combined sources5
Helixi529 – 545Combined sources17
Beta strandi548 – 550Combined sources3
Helixi560 – 584Combined sources25
Beta strandi587 – 589Combined sources3
Beta strandi594 – 596Combined sources3
Beta strandi606 – 608Combined sources3
Beta strandi610 – 613Combined sources4
Helixi618 – 620Combined sources3
Beta strandi624 – 628Combined sources5
Turni632 – 634Combined sources3
Beta strandi639 – 643Combined sources5
Turni651 – 653Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZOYX-ray2.40A43-599[»]
1ZP0X-ray3.50A43-664[»]
3ABVX-ray3.24A43-664[»]
3AE1X-ray3.14A43-664[»]
3AE2X-ray3.10A43-664[»]
3AE3X-ray3.35A43-664[»]
3AE4X-ray2.91A43-664[»]
3AE5X-ray3.41A43-664[»]
3AE6X-ray3.40A43-664[»]
3AE7X-ray3.62A43-664[»]
3AE8X-ray3.40A43-664[»]
3AE9X-ray3.31A43-664[»]
3AEAX-ray3.39A43-664[»]
3AEBX-ray3.00A43-664[»]
3AECX-ray3.61A43-664[»]
3AEDX-ray3.52A43-664[»]
3AEEX-ray3.22A43-664[»]
3AEFX-ray2.80A43-664[»]
3AEGX-ray3.27A43-664[»]
3SFDX-ray2.61A43-664[»]
3SFEX-ray2.81A43-664[»]
4YTPX-ray3.10A1-664[»]
4YXDX-ray3.00A1-664[»]
ProteinModelPortaliQ0QF01.
SMRiQ0QF01.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0QF01.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG001461.
InParanoidiQ0QF01.

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.

Q0QF01-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGVRAVSRL LRARRLALTW AQPAASPIGA RSFHFTVDGN KRSSAKVSDA
60 70 80 90 100
ISTQYPVVDH EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT
110 120 130 140 150
VAAQGGINAA LGNMEEDNWR WHFYDTVKGS DWLGDQDAIH YMTEQAPASV
160 170 180 190 200
VELENYGMPF SRTEDGKIYQ RAFGGQSLKF GKGGQAHRCC CVADRTGHSL
210 220 230 240 250
LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE DGSIHRIRAR
260 270 280 290 300
NTVVATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI
310 320 330 340 350
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE
360 370 380 390 400
IREGRGCGPE KDHVYLQLHH LPPEQLAVRL PGISETAMIF AGVDVTKEPI
410 420 430 440 450
PVLPTVHYNM GGIPTNYKGQ VLRHVNGQDQ VVPGLYACGE AACASVHGAN
460 470 480 490 500
RLGANSLLDL VVFGRACALS IAESCRPGDK VPSIKPNAGE ESVMNLDKLR
510 520 530 540 550
FANGTIRTSE LRLSMQKSMQ SHAAVFRVGS VLQEGCEKIL RLYGDLQHLK
560 570 580 590 600
TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDFKER
610 620 630 640 650
VDEYDYSKPI QGQQKKPFQE HWRKHTLSYV DVKTGKVSLE YRPVIDKTLN
660
EADCATVPPA IRSY
Length:664
Mass (Da):72,832
Last modified:March 2, 2010 - v2
Checksum:i0120E14F7F6F60EE
GO

Sequence cautioni

The sequence ABI29191 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti165 – 171DGKIYQR → LQESARG in ABI29191 (PubMed:17697375).Curated7
Sequence conflicti222L → S no nucleotide entry (PubMed:17480203).Curated1
Sequence conflicti235I → T no nucleotide entry (PubMed:17480203).Curated1
Sequence conflicti358G → N no nucleotide entry (PubMed:17480203).Curated1
Sequence conflicti453G → E no nucleotide entry (PubMed:17480203).Curated1
Sequence conflicti509S → W in ABD77326 (PubMed:16751257).Curated1
Sequence conflicti566L → P in ABD77326 (PubMed:16751257).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ402993 mRNA. Translation: ABD77326.1.
DQ845177 mRNA. Translation: ABI29191.1. Different initiation.
UniGeneiSsc.24988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ402993 mRNA. Translation: ABD77326.1.
DQ845177 mRNA. Translation: ABI29191.1. Different initiation.
UniGeneiSsc.24988.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZOYX-ray2.40A43-599[»]
1ZP0X-ray3.50A43-664[»]
3ABVX-ray3.24A43-664[»]
3AE1X-ray3.14A43-664[»]
3AE2X-ray3.10A43-664[»]
3AE3X-ray3.35A43-664[»]
3AE4X-ray2.91A43-664[»]
3AE5X-ray3.41A43-664[»]
3AE6X-ray3.40A43-664[»]
3AE7X-ray3.62A43-664[»]
3AE8X-ray3.40A43-664[»]
3AE9X-ray3.31A43-664[»]
3AEAX-ray3.39A43-664[»]
3AEBX-ray3.00A43-664[»]
3AECX-ray3.61A43-664[»]
3AEDX-ray3.52A43-664[»]
3AEEX-ray3.22A43-664[»]
3AEFX-ray2.80A43-664[»]
3AEGX-ray3.27A43-664[»]
3SFDX-ray2.61A43-664[»]
3SFEX-ray2.81A43-664[»]
4YTPX-ray3.10A1-664[»]
4YXDX-ray3.00A1-664[»]
ProteinModelPortaliQ0QF01.
SMRiQ0QF01.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PeptideAtlasiQ0QF01.
PRIDEiQ0QF01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG001461.
InParanoidiQ0QF01.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

Miscellaneous databases

EvolutionaryTraceiQ0QF01.

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_PIG
AccessioniPrimary (citable) accession number: Q0QF01
Secondary accession number(s): A0SNV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: March 2, 2010
Last modified: November 30, 2016
This is version 63 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, Direct protein sequencing, 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.