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Q09545

- SDHB_CAEEL

UniProt

Q09545 - SDHB_CAEEL

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Protein
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
Gene
sdhb-1, tag-55, F42A8.2
Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript 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) By similarity.

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Binds 1 2Fe-2S cluster By similarity.
Binds 1 3Fe-4S cluster By similarity.
Binds 1 4Fe-4S cluster By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi107 – 1071Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi112 – 1121Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi115 – 1151Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi127 – 1271Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi200 – 2001Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi203 – 2031Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi206 – 2061Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi210 – 2101Iron-sulfur 3 (3Fe-4S) By similarity
Binding sitei215 – 2151Ubiquinone; shared with DHSD By similarity
Metal bindingi257 – 2571Iron-sulfur 3 (3Fe-4S) By similarity
Metal bindingi263 – 2631Iron-sulfur 3 (3Fe-4S) By similarity
Metal bindingi267 – 2671Iron-sulfur 2 (4Fe-4S) By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. 3 iron, 4 sulfur cluster binding Source: UniProtKB
  3. 4 iron, 4 sulfur cluster binding Source: UniProtKB
  4. electron carrier activity Source: InterPro
  5. metal ion binding Source: UniProtKB-KW
  6. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
  7. ubiquinone binding Source: UniProtKB

GO - Biological processi

  1. tricarboxylic acid cycle Source: UniProtKB-UniPathway
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-1
Synonyms:tag-55
ORF Names:F42A8.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome II

Organism-specific databases

WormBaseiF42A8.2; CE01579; WBGene00006433; sdhb-1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB
  2. mitochondrial respiratory chain complex II Source: UniProtKB
  3. mitochondrion Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 298Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000010354
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Proteomic databases

PaxDbiQ09545.

Interactioni

Subunit structurei

Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit By similarity.

Protein-protein interaction databases

BioGridi39806. 1 interaction.
STRINGi6239.F42A8.2.2.

Structurei

3D structure databases

ProteinModelPortaliQ09545.
SMRiQ09545. Positions 52-296.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 147892Fe-2S ferredoxin-type
Add
BLAST
Domaini190 – 220314Fe-4S ferredoxin-type
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0479.
GeneTreeiENSGT00390000013558.
HOGENOMiHOG000160590.
InParanoidiQ09545.
KOiK00235.
OMAiHARDPIS.
PhylomeDBiQ09545.

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.

Q09545-1 [UniParc]FASTAAdd to Basket

« Hide

MLARSARLLH SAELAANAIR AASGAPATAA AAEASFPSTD DVAAKTKKTG    50
NRIKTFEIYR FNPEAPGAKP TVQKFDVDLD QCGTMILDAL IKIKNEVDPT 100
LTFRRSCREG ICGSCAMNIG GQNTLACICK IDSDTSKSTK IYPLPHMFVV 150
KDLVPDMNLF YAQYASIQPW IQKKTPLTLG EKQMHQSVAE RDRLDGLYEC 200
ILCACCSTSC PSYWWNADKY LGPAVLMQAY RWVIDSRDDY ATERLHRMHD 250
SFSAFKCHTI MNCTKTCPKH LNPAKAIGEI KSLLTGFTSK PAAEPSAF 298
Length:298
Mass (Da):32,891
Last modified:October 1, 1996 - v1
Checksum:i0FDD148A6C9AB824
GO

Sequence cautioni

The sequence BAA23717.1 differs from that shown. Reason: Frameshift at positions 4, 15 and 28.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB008569 mRNA. Translation: BAA23717.1. Frameshift.
Z47809 Genomic DNA. Translation: CAA87780.1.
PIRiT22083.
T37260.
RefSeqiNP_495992.1. NM_063591.6.
UniGeneiCel.19522.

Genome annotation databases

EnsemblMetazoaiF42A8.2.1; F42A8.2.1; WBGene00006433.
F42A8.2.2; F42A8.2.2; WBGene00006433.
GeneIDi174482.
KEGGicel:CELE_F42A8.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB008569 mRNA. Translation: BAA23717.1 . Frameshift.
Z47809 Genomic DNA. Translation: CAA87780.1 .
PIRi T22083.
T37260.
RefSeqi NP_495992.1. NM_063591.6.
UniGenei Cel.19522.

3D structure databases

ProteinModelPortali Q09545.
SMRi Q09545. Positions 52-296.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 39806. 1 interaction.
STRINGi 6239.F42A8.2.2.

Proteomic databases

PaxDbi Q09545.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai F42A8.2.1 ; F42A8.2.1 ; WBGene00006433 .
F42A8.2.2 ; F42A8.2.2 ; WBGene00006433 .
GeneIDi 174482.
KEGGi cel:CELE_F42A8.2.

Organism-specific databases

CTDi 174482.
WormBasei F42A8.2 ; CE01579 ; WBGene00006433 ; sdhb-1.

Phylogenomic databases

eggNOGi COG0479.
GeneTreei ENSGT00390000013558.
HOGENOMi HOG000160590.
InParanoidi Q09545.
KOi K00235.
OMAi HARDPIS.
PhylomeDBi Q09545.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01006 .

Miscellaneous databases

NextBioi 884224.
PROi Q09545.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 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 ]
Pfami PF13085. Fer2_3. 1 hit.
[Graphical view ]
SUPFAMi SSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR00384. dhsB. 1 hit.
PROSITEi PS00197. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 [MRNA].
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiSDHB_CAEEL
AccessioniPrimary (citable) accession number: Q09545
Secondary accession number(s): O44075
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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