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Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene
N/A
Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Status
Unreviewed-Annotation score: Annotation score: 3 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).UniRule annotation

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.UniRule annotation

Cofactori

FADUniRule annotation

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes fumarate from succinate (eukaryal route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (SDHA2), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial, Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (ASU_13063), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial, Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial, Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial, Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial, Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (ASU_11971), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial, Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial, Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (ASU_07771)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei235 – 2351FAD; via carbonyl oxygenCombined sources
Binding sitei255 – 2551FADCombined sources
Binding sitei387 – 3871FADCombined sources
Binding sitei421 – 4211FADCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 524FADCombined sources
Nucleotide bindingi71 – 722FADCombined sources
Nucleotide bindingi78 – 869FADCombined sources
Nucleotide bindingi200 – 2012FADCombined sources
Nucleotide bindingi432 – 4387FADCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

Electron transportUniRule annotation, Transport, Tricarboxylic acid cycleUniRule annotation

Keywords - Ligandi

FADUniRule annotationCombined sources, Flavoprotein, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18284.
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialUniRule annotation (EC:1.3.5.1UniRule annotation)
OrganismiAscaris suum (Pig roundworm) (Ascaris lumbricoides)Imported
Taxonomic identifieri6253 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

Subcellular locationi

  • Mitochondrion inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Matrix side UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

MembraneUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi191 ↔ 193Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VR8X-ray2.81A/E1-645[»]
3VR9X-ray3.01A/E1-645[»]
3VRAX-ray3.44A/E1-645[»]
3VRBX-ray2.91A/E1-645[»]
ProteinModelPortaliQ33862.
SMRiQ33862. Positions 34-645.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 438396FAD_binding_2InterPro annotationAdd
BLAST
Domaini493 – 645153Succ_DH_flav_CInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transit peptideUniRule annotation

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.

Q33862-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRAVRALIC RIGARRTLSV SSSRLDVSTS NIAQYKVIDH AYDVVIIGAG
60 70 80 90 100
GAGLRAAMGL GEAGFKTAVV TKMFPTRSHT TAAQGGINAA LGSMNPDDWK
110 120 130 140 150
WHFYDTAKGS DWLGDQNAMH YLTRNAVEAV TELENFGMPF SRTPEGKIYQ
160 170 180 190 200
RSFGGQSNNY GKGGVAKRTC CVADRTGHSM LHTLYGNSLR CHCTFFIEYF
210 220 230 240 250
ALDLLMDKGR CVGVIALCLE DGTIHRFRSK RTIVATGGYG RAYFSCTTAH
260 270 280 290 300
MNTGDGTALA TRAGIALEDL EFIQFHPTGI YGVGCLITEG SRGEGGFLVN
310 320 330 340 350
SEGERFMERY APKAKDLASR DVVSRAETIE IMEGRGVGPE KDHIYLQLHH
360 370 380 390 400
LPAEQLHQRL PGISETAKIF AGVDVTKEPI PVIPTVHYNM GGIPTNYKAQ
410 420 430 440 450
VIKYTKEGGD KIVPGLYACG ECACHSVHGA NRLGANSLLD AVVFGRACSI
460 470 480 490 500
NIKEELKPDE KIPELPEGAG EESIANLDAV RYANGDVPTA ELRLTMQKTM
510 520 530 540 550
QKHAGVFRRG DILAEGVKKM MDLSKELKRL KTTDRSLIWN SDLTESLELQ
560 570 580 590 600
NLMLNATQTI VAAENRKESR GAHARDDFPK REDEYDYSKP IEGQTKRPFE
610 620 630 640
KHWRKHTLTK QDPRTGHITL DYRPVIDKTL DPAEVDWIPP IIRSY
Length:645
Mass (Da):71,201
Last modified:January 1, 1998 - v2
Checksum:i0F894C36D3B2D68E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30650 mRNA. Translation: BAA21636.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30650 mRNA. Translation: BAA21636.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VR8X-ray2.81A/E1-645[»]
3VR9X-ray3.01A/E1-645[»]
3VRAX-ray3.44A/E1-645[»]
3VRBX-ray2.91A/E1-645[»]
ProteinModelPortaliQ33862.
SMRiQ33862. Positions 34-645.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.
BioCyciMetaCyc:MONOMER-18284.

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...

Publicationsi

  1. "Sequence comparison between the flavoprotein subunit of the fumarate reductase (complex II) of the anaerobic parasitic nematode, Ascaris suum and the succinate dehydrogenase of the aerobic, free-living nematode, Caenorhabditis elegans."
    Kuramochi T., Hirawake H., Kojima S., Takamiya S., Furushima R., Aoki T., Komuniecki R., Kita K.
    Mol. Biochem. Parasitol. 68:177-187(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum."
    Shimizu H., Osanai A., Sakamoto K., Inaoka D.K., Shiba T., Harada S., Kita K.
    J. Biochem. 151:589-592(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH FAD, DISULFIDE BONDS.
  3. "Crystal structure of mitochondrial quinol-fumarate reductase from parasitic nematode Ascaris suum."
    Shimizu H., Shiba T., Inaoka D.K., Osanai A., Kita K., Sakamoto K., Harada S.
    Submitted (APR-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH FAD, X-RAY CRYSTALLOGRAPHY (3.44 ANGSTROMS) IN COMPLEX WITH FAD.

Entry informationi

Entry nameiQ33862_ASCSU
AccessioniPrimary (citable) accession number: Q33862
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.