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Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur 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

Iron-sulfur protein (IP) 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

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster.UniRule annotation
  • [3Fe-4S] clusterUniRule annotationNote: Binds 1 [3Fe-4S] cluster.UniRule annotation
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster.UniRule 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
Metal bindingi88 – 881Iron-sulfur (2Fe-2S); via amide nitrogenCombined sources
Metal bindingi89 – 891Iron-sulfur (2Fe-2S)Combined sources
Metal bindingi94 – 941Iron-sulfur (2Fe-2S)Combined sources
Metal bindingi95 – 951Iron-sulfur (2Fe-2S); via amide nitrogenCombined sources
Metal bindingi97 – 971Iron-sulfur (2Fe-2S)Combined sources
Metal bindingi109 – 1091Iron-sulfur (2Fe-2S)Combined sources
Metal bindingi182 – 1821Iron-sulfur (4Fe-4S)Combined sources
Metal bindingi185 – 1851Iron-sulfur (4Fe-4S)Combined sources
Metal bindingi188 – 1881Iron-sulfur (4Fe-4S)Combined sources
Metal bindingi192 – 1921Iron-sulfur (3Fe-4S)Combined sources
Metal bindingi239 – 2391Iron-sulfur (3Fe-4S)Combined sources
Metal bindingi241 – 2411Iron-sulfur (3Fe-4S); via amide nitrogenCombined sources
Metal bindingi242 – 2421Iron-sulfur (3Fe-4S); via amide nitrogenCombined sources
Metal bindingi243 – 2431Iron-sulfur (3Fe-4S); via amide nitrogenCombined sources
Metal bindingi245 – 2451Iron-sulfur (3Fe-4S)Combined sources
Metal bindingi249 – 2491Iron-sulfur (4Fe-4S)Combined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

2Fe-2SUniRule annotationCombined sources, 3Fe-4SUniRule annotationCombined sources, 4Fe-4SUniRule annotationCombined sources, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18285.
SABIO-RKO44074.
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] iron-sulfur 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

Membrane, Mitochondrion, Mitochondrion inner membraneUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi89 ↔ 94Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VR8X-ray2.81B/F1-282[»]
3VR9X-ray3.01B/F1-282[»]
3VRAX-ray3.44B/F1-282[»]
3VRBX-ray2.91B/F1-282[»]
4YSXX-ray2.25B/F1-282[»]
4YSYX-ray3.10B/F1-282[»]
4YSZX-ray3.30B/F1-282[»]
4YT0X-ray3.66B/F1-282[»]
4YTMX-ray3.40B/F1-282[»]
4YTNX-ray3.00B/F1-282[»]
5C2TX-ray2.75B/F1-282[»]
ProteinModelPortaliO44074.
SMRiO44074. Positions 34-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 129912Fe-2S ferredoxin-typeInterPro annotationAdd
BLAST
Domaini172 – 202314Fe-4S ferredoxin-typeInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.UniRule annotation
Contains 1 2Fe-2S ferredoxin-type domain.UniRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.UniRule annotation

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O44074-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRGSTSVCR SLELVTQAAR YASAATAAAP TGKRIKTFEI YRFNPEEPGA
60 70 80 90 100
KPKLQKFDVD LDKCGTMVLD ALIKIKNEVD PTLTFRRSCR EGICGSCAMN
110 120 130 140 150
IAGENTLACI CNIDQNTSKT TKIYPLPHMF VIKDLVPDMN LFYAQYASIQ
160 170 180 190 200
PWLQKKTKIN LGEKQQYQSI KEQEKLDGLY ECILCACCSA SCPSYWWNAD
210 220 230 240 250
KYLGPAVLMQ AYRWIIDSRD DSAAERLARM QDGFSAFKCH TIMNCTKTCP
260 270 280
KHLNPARAIG EIKMLLTKMK TKPAPLPTPA NF
Length:282
Mass (Da):31,633
Last modified:June 1, 1998 - v1
Checksum:iBFC5E4C7A4D6AF43
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008568 mRNA. Translation: BAA23716.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008568 mRNA. Translation: BAA23716.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VR8X-ray2.81B/F1-282[»]
3VR9X-ray3.01B/F1-282[»]
3VRAX-ray3.44B/F1-282[»]
3VRBX-ray2.91B/F1-282[»]
4YSXX-ray2.25B/F1-282[»]
4YSYX-ray3.10B/F1-282[»]
4YSZX-ray3.30B/F1-282[»]
4YT0X-ray3.66B/F1-282[»]
4YTMX-ray3.40B/F1-282[»]
4YTNX-ray3.00B/F1-282[»]
5C2TX-ray2.75B/F1-282[»]
ProteinModelPortaliO44074.
SMRiO44074. Positions 34-270.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.
BioCyciMetaCyc:MONOMER-18285.
SABIO-RKO44074.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Stage-specific isoforms of Ascaris suum complex. II: The fumarate reductase of the parasitic adult and the succinate dehydrogenase of free-living larvae share a common iron-sulfur subunit."
    Amino H., Wang H., Hirawake H., Saruta F., Mizuchi D., Mineki R., Shindo N., Murayama K., Takamiya S., Aoki T., Kojima S., Kita K.
    Mol. Biochem. Parasitol. 106:63-76(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: MuscleImported.
  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 IRON-SULFUR (2FE-2S); IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S).
  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 IRON-SULFUR (2FE-2S); IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), X-RAY CRYSTALLOGRAPHY (3.44 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S); IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S).
  4. "Structural Insights into the Molecular Design of Flutolanil Derivatives Targeted for Fumarate Respiration of Parasite Mitochondria."
    Inaoka D.K., Shiba T., Sato D., Balogun E.O., Sasaki T., Nagahama M., Oda M., Matsuoka S., Ohmori J., Honma T., Inoue M., Kita K., Harada S.
    Int. J. Mol. Sci. 16:15287-15308(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), DISULFIDE BONDS.
  5. "New Insights into the Design of Inhibitors Targeted for Parasitic Anaerobic Energy Metabolism."
    Harada S., Shiba T., Sato D., Yamamoto A., Nagahama M., Yone A., Inaoka D.K., Sakamoto K., Inoue M., Honma T., Kita K.
    Submitted (MAR-2015) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS).

Entry informationi

Entry nameiO44074_ASCSU
AccessioniPrimary (citable) accession number: O44074
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 99 of the entry and version 1 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.