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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:

Pathwayi: 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)DescriptionActionsGraphical viewLength
Metal bindingi93Iron-sulfur 1 (2Fe-2S)1
Metal bindingi98Iron-sulfur 1 (2Fe-2S)1
Metal bindingi101Iron-sulfur 1 (2Fe-2S)1
Metal bindingi113Iron-sulfur 1 (2Fe-2S)1
Metal bindingi186Iron-sulfur 2 (4Fe-4S)1
Metal bindingi189Iron-sulfur 2 (4Fe-4S)1
Metal bindingi192Iron-sulfur 2 (4Fe-4S)1
Metal bindingi196Iron-sulfur 3 (3Fe-4S)1
Binding sitei201Ubiquinone; shared with DHSD1 Publication1
Metal bindingi243Iron-sulfur 3 (3Fe-4S)1
Metal bindingi249Iron-sulfur 3 (3Fe-4S)1
Metal bindingi253Iron-sulfur 2 (4Fe-4S)1

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: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
  • succinate dehydrogenase activity Source: GO_Central
  • 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
Proteomesi
  • UP000008227 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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2366485.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 28MitochondrionAdd BLAST28
ChainiPRO_000034379929 – 280Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialAdd BLAST252

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei51N6-acetyllysineBy similarity1
Modified residuei55N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ007T0.
PeptideAtlasiQ007T0.
PRIDEiQ007T0.

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

1280
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 46Combined sources8
Beta strandi51 – 53Combined sources3
Beta strandi57 – 64Combined sources8
Helixi65 – 67Combined sources3
Helixi72 – 81Combined sources10
Beta strandi94 – 98Combined sources5
Beta strandi103 – 105Combined sources3
Beta strandi108 – 110Combined sources3
Turni112 – 114Combined sources3
Beta strandi123 – 128Combined sources6
Beta strandi130 – 132Combined sources3
Beta strandi133 – 137Combined sources5
Helixi144 – 152Combined sources9
Turni163 – 167Combined sources5
Helixi174 – 178Combined sources5
Turni179 – 185Combined sources7
Helixi193 – 195Combined sources3
Helixi197 – 202Combined sources6
Turni203 – 205Combined sources3
Helixi208 – 219Combined sources12
Helixi227 – 232Combined sources6
Beta strandi236 – 238Combined sources3
Turni239 – 242Combined sources4
Helixi250 – 252Combined sources3
Helixi259 – 270Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4YTPX-ray3.10B1-280[»]
4YXDX-ray3.00B1-280[»]
ProteinModelPortaliQ007T0.
SMRiQ007T0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ007T0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 1312Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST92
Domaini176 – 2064Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd BLAST31

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

eggNOGiKOG3049. Eukaryota.
COG0479. LUCA.
HOVERGENiHBG005483.
InParanoidiQ007T0.
KOiK00235.

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.

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
PDB 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[»]
4YTPX-ray3.10B1-280[»]
4YXDX-ray3.00B1-280[»]
ProteinModelPortaliQ007T0.
SMRiQ007T0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000022052.

Chemistry databases

ChEMBLiCHEMBL2366485.

Proteomic databases

PaxDbiQ007T0.
PeptideAtlasiQ007T0.
PRIDEiQ007T0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi414412.
KEGGissc:414412.

Organism-specific databases

CTDi6390.

Phylogenomic databases

eggNOGiKOG3049. Eukaryota.
COG0479. LUCA.
HOVERGENiHBG005483.
InParanoidiQ007T0.
KOiK00235.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

Miscellaneous databases

EvolutionaryTraceiQ007T0.

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 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: November 2, 2016
This is version 67 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

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.