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Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

SDHB

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 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).

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Protein has several cofactor binding sites:

Pathway: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes fumarate from succinate (eukaryal route).
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SDHB), Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (SDHA), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SDHB), 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi93 – 931Iron-sulfur 1 (2Fe-2S)
Metal bindingi98 – 981Iron-sulfur 1 (2Fe-2S)
Metal bindingi101 – 1011Iron-sulfur 1 (2Fe-2S)
Metal bindingi113 – 1131Iron-sulfur 1 (2Fe-2S)
Metal bindingi186 – 1861Iron-sulfur 2 (4Fe-4S)
Metal bindingi189 – 1891Iron-sulfur 2 (4Fe-4S)
Metal bindingi192 – 1921Iron-sulfur 2 (4Fe-4S)
Metal bindingi196 – 1961Iron-sulfur 3 (3Fe-4S)
Binding sitei201 – 2011Ubiquinone; shared with DHSD1 Publication
Metal bindingi243 – 2431Iron-sulfur 3 (3Fe-4S)
Metal bindingi249 – 2491Iron-sulfur 3 (3Fe-4S)
Metal bindingi253 – 2531Iron-sulfur 2 (4Fe-4S)

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB
  • 3 iron, 4 sulfur cluster binding Source: UniProtKB
  • 4 iron, 4 sulfur cluster binding Source: UniProtKB
  • electron carrier activity Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
  • ubiquinone binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC:1.3.5.1)
Alternative name(s):
Iron-sulfur subunit of complex II
Short name:
Ip
Gene namesi
Name:SDHB
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionAdd
BLAST
Chaini29 – 280252Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000343799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysineBy similarity
Modified residuei55 – 551N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ007T0.

Expressioni

Gene expression databases

GenevisibleiQ007T0. SS.

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.ENSSSCP00000022052.

Structurei

Secondary structure

1
280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 468Combined sources
Beta strandi51 – 533Combined sources
Beta strandi57 – 648Combined sources
Helixi65 – 673Combined sources
Helixi72 – 8110Combined sources
Beta strandi94 – 985Combined sources
Beta strandi103 – 1053Combined sources
Beta strandi108 – 1103Combined sources
Turni112 – 1143Combined sources
Beta strandi123 – 1286Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi133 – 1375Combined sources
Helixi144 – 1529Combined sources
Turni163 – 1675Combined sources
Helixi174 – 1785Combined sources
Turni179 – 1857Combined sources
Helixi193 – 1953Combined sources
Helixi197 – 2026Combined sources
Turni203 – 2053Combined sources
Helixi208 – 21912Combined sources
Helixi227 – 2326Combined sources
Beta strandi236 – 2383Combined sources
Turni239 – 2424Combined sources
Helixi250 – 2523Combined sources
Helixi259 – 27012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZOYX-ray2.40B29-279[»]
1ZP0X-ray3.50B29-279[»]
3ABVX-ray3.24B29-280[»]
3AE1X-ray3.14B29-280[»]
3AE2X-ray3.10B29-280[»]
3AE3X-ray3.35B29-280[»]
3AE4X-ray2.91B29-280[»]
3AE5X-ray3.41B29-280[»]
3AE6X-ray3.40B29-280[»]
3AE7X-ray3.62B29-280[»]
3AE8X-ray3.40B29-280[»]
3AE9X-ray3.31B29-280[»]
3AEAX-ray3.39B29-280[»]
3AEBX-ray3.00B29-280[»]
3AECX-ray3.61B29-280[»]
3AEDX-ray3.52B29-280[»]
3AEEX-ray3.22B29-280[»]
3AEFX-ray2.80B29-280[»]
3AEGX-ray3.27B29-280[»]
3SFDX-ray2.61B29-280[»]
3SFEX-ray2.81B29-280[»]
ProteinModelPortaliQ007T0.
SMRiQ007T0. Positions 37-275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ007T0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 131922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini176 – 206314Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG005483.
InParanoidiQ007T0.
KOiK00235.

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.

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

Q007T0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVVAVSLK RWFPATTLGG ACLQACRGAQ TAAATAPRIK KFAIYRWDPD
60 70 80 90 100
KTGDKPHMQT YEIDLNNCGP MVLDALIKIK NEIDSTLTFR RSCREGICGS
110 120 130 140 150
CAMNINGGNT LACTRRIDTN LDKVSKIYPL PHMYVIKDLV PDLSNFYAQY
160 170 180 190 200
KSIEPYLKKK DESQEGKQQY LQSIEEREKL DGLYECILCA CCSTSCPSYW
210 220 230 240 250
WNGDKYLGPA VLMQAYRWMI DSRDDFTEER LAKLQDPFSL YRCHTIMNCT
260 270 280
GTCPKGLNPG KAIAEIKKMM ATYKEKKASA
Length:280
Mass (Da):31,586
Last modified:November 14, 2006 - v1
Checksum:i096B11189EF1ED59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ915498 mRNA. Translation: ABJ09403.1.
DQ403018 mRNA. Translation: ABD77151.1.
RefSeqiNP_001098423.1. NM_001104953.1.
UniGeneiSsc.55804.

Genome annotation databases

GeneIDi414412.
KEGGissc:414412.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ915498 mRNA. Translation: ABJ09403.1.
DQ403018 mRNA. Translation: ABD77151.1.
RefSeqiNP_001098423.1. NM_001104953.1.
UniGeneiSsc.55804.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZOYX-ray2.40B29-279[»]
1ZP0X-ray3.50B29-279[»]
3ABVX-ray3.24B29-280[»]
3AE1X-ray3.14B29-280[»]
3AE2X-ray3.10B29-280[»]
3AE3X-ray3.35B29-280[»]
3AE4X-ray2.91B29-280[»]
3AE5X-ray3.41B29-280[»]
3AE6X-ray3.40B29-280[»]
3AE7X-ray3.62B29-280[»]
3AE8X-ray3.40B29-280[»]
3AE9X-ray3.31B29-280[»]
3AEAX-ray3.39B29-280[»]
3AEBX-ray3.00B29-280[»]
3AECX-ray3.61B29-280[»]
3AEDX-ray3.52B29-280[»]
3AEEX-ray3.22B29-280[»]
3AEFX-ray2.80B29-280[»]
3AEGX-ray3.27B29-280[»]
3SFDX-ray2.61B29-280[»]
3SFEX-ray2.81B29-280[»]
ProteinModelPortaliQ007T0.
SMRiQ007T0. Positions 37-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000022052.

Chemistry

ChEMBLiCHEMBL2366485.

Proteomic databases

PRIDEiQ007T0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi414412.
KEGGissc:414412.

Organism-specific databases

CTDi6390.

Phylogenomic databases

HOVERGENiHBG005483.
InParanoidiQ007T0.
KOiK00235.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

Miscellaneous databases

EvolutionaryTraceiQ007T0.

Gene expression databases

GenevisibleiQ007T0. SS.

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

« Hide 'large scale' publications
  1. Liu G.Y.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "Housekeeping genes for phylogenetic analysis of eutherian relationships."
    Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
    Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-264.
    Tissue: Liver.
  3. "Crystal structure of mitochondrial respiratory membrane protein complex II."
    Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z.
    Cell 121:1043-1057(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 29-279 IN COMPLEX WITH IRON-SULFUR CLUSTERS AND UBIQUINONE, SUBUNIT.

Entry informationi

Entry nameiSDHB_PIG
AccessioniPrimary (citable) accession number: Q007T0
Secondary accession number(s): Q0QEX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: November 14, 2006
Last modified: June 24, 2015
This is version 58 of the entry and version 1 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

External Data

Dasty 3

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 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.