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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] 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, 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)DescriptionActionsGraphical viewLength
Metal bindingi88Iron-sulfur (2Fe-2S); via amide nitrogenCombined sources1
Metal bindingi89Iron-sulfur (2Fe-2S)Combined sources1
Metal bindingi94Iron-sulfur (2Fe-2S)Combined sources1
Metal bindingi95Iron-sulfur (2Fe-2S); via amide nitrogenCombined sources1
Metal bindingi97Iron-sulfur (2Fe-2S)Combined sources1
Metal bindingi109Iron-sulfur (2Fe-2S)Combined sources1
Metal bindingi182Iron-sulfur (4Fe-4S)Combined sources1
Metal bindingi185Iron-sulfur (4Fe-4S)Combined sources1
Metal bindingi188Iron-sulfur (4Fe-4S)Combined sources1
Metal bindingi192Iron-sulfur (3Fe-4S)Combined sources1
Metal bindingi239Iron-sulfur (3Fe-4S)Combined sources1
Metal bindingi241Iron-sulfur (3Fe-4S); via amide nitrogenCombined sources1
Metal bindingi242Iron-sulfur (3Fe-4S); via amide nitrogenCombined sources1
Metal bindingi243Iron-sulfur (3Fe-4S); via amide nitrogenCombined sources1
Metal bindingi245Iron-sulfur (3Fe-4S)Combined sources1
Metal bindingi249Iron-sulfur (4Fe-4S)Combined sources1

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)DescriptionActionsGraphical viewLength
Disulfide bondi89 ↔ 94Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5C3JX-ray2.80B/F1-282[»]
ProteinModelPortaliO44074.
SMRiO44074.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 1292Fe-2S ferredoxin-typeInterPro annotationAdd BLAST91
Domaini172 – 2024Fe-4S ferredoxin-typeInterPro annotationAdd BLAST31

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

CDDicd00207. fer2. 1 hit.
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
PDB 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[»]
5C3JX-ray2.80B/F1-282[»]
ProteinModelPortaliO44074.
SMRiO44074.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

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

Family and domain databases

CDDicd00207. fer2. 1 hit.
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...

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: November 2, 2016
This is version 102 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.