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Protein

Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial

Gene

SDHD

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Membrane-anchoring 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).

Pathwayi: tricarboxylic acid cycle

This protein is involved in the pathway tricarboxylic acid cycle, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi102Iron (heme axial ligand); shared with SDHC1
Binding sitei114Ubiquinone; shared with IP/SDHB1 Publication1

GO - Molecular functioni

  • heme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • ubiquinone binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00223.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
Short name:
CybS
Alternative name(s):
CII-4
QPs3
Succinate dehydrogenase complex subunit D
Succinate-ubiquinone oxidoreductase cytochrome b small subunit
Succinate-ubiquinone reductase membrane anchor subunit
Gene namesi
Name:SDHD
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini37 – 63Mitochondrial matrixCuratedAdd BLAST27
Transmembranei64 – 85HelicalAdd BLAST22
Topological domaini86 – 90Mitochondrial intermembraneCurated5
Transmembranei91 – 111HelicalAdd BLAST21
Topological domaini112 – 120Mitochondrial matrixCurated9
Transmembranei121 – 142HelicalAdd BLAST22
Topological domaini143 – 159Mitochondrial intermembraneCuratedAdd BLAST17

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2366564.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 36MitochondrionSequence analysisAdd BLAST36
ChainiPRO_000034380437 – 159Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrialAdd BLAST123

Proteomic databases

PaxDbiA5GZW8.
PeptideAtlasiA5GZW8.
PRIDEiA5GZW8.

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.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015958.

Chemistry databases

BindingDBiA5GZW8.

Structurei

Secondary structure

1159
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi61 – 85Combined sources25
Helixi89 – 114Combined sources26
Helixi118 – 144Combined sources27
Beta strandi145 – 147Combined sources3
Helixi149 – 157Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZOYX-ray2.40D57-159[»]
1ZP0X-ray3.50D57-159[»]
3ABVX-ray3.24D57-159[»]
3AE1X-ray3.14D57-159[»]
3AE2X-ray3.10D57-159[»]
3AE3X-ray3.35D57-159[»]
3AE4X-ray2.91D57-159[»]
3AE5X-ray3.41D57-159[»]
3AE6X-ray3.40D57-159[»]
3AE7X-ray3.62D57-159[»]
3AE8X-ray3.40D57-159[»]
3AE9X-ray3.31D57-159[»]
3AEAX-ray3.39D57-159[»]
3AEBX-ray3.00D57-159[»]
3AECX-ray3.61D57-159[»]
3AEDX-ray3.52D57-159[»]
3AEEX-ray3.22D57-159[»]
3AEFX-ray2.80D57-159[»]
3AEGX-ray3.27D57-159[»]
3SFDX-ray2.61D57-159[»]
3SFEX-ray2.81D57-159[»]
4YTPX-ray3.10D1-159[»]
4YXDX-ray3.00D1-159[»]
ProteinModelPortaliA5GZW8.
SMRiA5GZW8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA5GZW8.

Family & Domainsi

Sequence similaritiesi

Belongs to the CybS family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4097. Eukaryota.
ENOG4111RTW. LUCA.
HOGENOMiHOG000290645.
HOVERGENiHBG003003.
InParanoidiA5GZW8.
KOiK00237.

Family and domain databases

CDDicd03496. SQR_TypeC_CybS. 1 hit.
InterProiIPR007992. CybS.
[Graphical view]
PANTHERiPTHR13337. PTHR13337. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A5GZW8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLWRLSVL CGARGGGALV LRTSVVRPAH VSAFLQDRHT PGWCGVQHIH
60 70 80 90 100
LSPSHQASSK AASLHWTGER VVSVLLLGLL PAAYLNPCSA MDYSLAAALT
110 120 130 140 150
LHGHWGIGQV VTDYVRGDAL QKVAKAGLLA LSAFTFAGLC YFNYHDVGIC

KAVAMLWKL
Length:159
Mass (Da):17,005
Last modified:July 22, 2008 - v2
Checksum:i9D70540010B0F8E3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti123V → A in AAW29970 (PubMed:17651329).Curated1
Sequence conflicti123V → A in ABF29393 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ486897 mRNA. Translation: ABF29393.1.
AY682832 mRNA. Translation: AAW29970.1.
AY682219 mRNA. Translation: AAW30631.1.
AY682222 mRNA. Translation: AAW30633.1.
RefSeqiNP_001090985.1. NM_001097516.1.
UniGeneiSsc.48868.
Ssc.95416.

Genome annotation databases

GeneIDi100048954.
KEGGissc:100048954.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ486897 mRNA. Translation: ABF29393.1.
AY682832 mRNA. Translation: AAW29970.1.
AY682219 mRNA. Translation: AAW30631.1.
AY682222 mRNA. Translation: AAW30633.1.
RefSeqiNP_001090985.1. NM_001097516.1.
UniGeneiSsc.48868.
Ssc.95416.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZOYX-ray2.40D57-159[»]
1ZP0X-ray3.50D57-159[»]
3ABVX-ray3.24D57-159[»]
3AE1X-ray3.14D57-159[»]
3AE2X-ray3.10D57-159[»]
3AE3X-ray3.35D57-159[»]
3AE4X-ray2.91D57-159[»]
3AE5X-ray3.41D57-159[»]
3AE6X-ray3.40D57-159[»]
3AE7X-ray3.62D57-159[»]
3AE8X-ray3.40D57-159[»]
3AE9X-ray3.31D57-159[»]
3AEAX-ray3.39D57-159[»]
3AEBX-ray3.00D57-159[»]
3AECX-ray3.61D57-159[»]
3AEDX-ray3.52D57-159[»]
3AEEX-ray3.22D57-159[»]
3AEFX-ray2.80D57-159[»]
3AEGX-ray3.27D57-159[»]
3SFDX-ray2.61D57-159[»]
3SFEX-ray2.81D57-159[»]
4YTPX-ray3.10D1-159[»]
4YXDX-ray3.00D1-159[»]
ProteinModelPortaliA5GZW8.
SMRiA5GZW8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015958.

Chemistry databases

BindingDBiA5GZW8.
ChEMBLiCHEMBL2366564.

Proteomic databases

PaxDbiA5GZW8.
PeptideAtlasiA5GZW8.
PRIDEiA5GZW8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100048954.
KEGGissc:100048954.

Organism-specific databases

CTDi6392.

Phylogenomic databases

eggNOGiKOG4097. Eukaryota.
ENOG4111RTW. LUCA.
HOGENOMiHOG000290645.
HOVERGENiHBG003003.
InParanoidiA5GZW8.
KOiK00237.

Enzyme and pathway databases

UniPathwayiUPA00223.

Miscellaneous databases

EvolutionaryTraceiA5GZW8.

Family and domain databases

CDDicd03496. SQR_TypeC_CybS. 1 hit.
InterProiIPR007992. CybS.
[Graphical view]
PANTHERiPTHR13337. PTHR13337. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDHSD_PIG
AccessioniPrimary (citable) accession number: A5GZW8
Secondary accession number(s): A7E1T4, A7E1T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: November 30, 2016
This is version 66 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.