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P48932 (SDHB_CHOCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit

EC=1.3.5.1
Alternative name(s):
Iron-sulfur subunit of complex II
Short name=Ip
Gene names
Name:SDH2
Synonyms:SDHB
Encoded onMitochondrion
OrganismChondrus crispus (Carragheen moss) (Irish moss)
Taxonomic identifier2769 [NCBI]
Taxonomic lineageEukaryotaRhodophytaFlorideophyceaeGigartinalesGigartinaceaeChondrus

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

Succinate + a quinone = fumarate + a quinol.

Cofactor

Binds 1 2Fe-2S cluster By similarity.

Binds 1 3Fe-4S cluster By similarity.

Binds 1 4Fe-4S cluster By similarity.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.

Subunit structure

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.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.

Sequence similarities

Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 4Fe-4S ferredoxin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 250250Succinate dehydrogenase [ubiquinone] iron-sulfur subunit
PRO_0000158694

Regions

Domain30 – 110812Fe-2S ferredoxin-type
Domain153 – 183314Fe-4S ferredoxin-type

Sites

Metal binding731Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding781Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding811Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding931Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1631Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1661Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1691Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1731Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2201Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2261Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2301Iron-sulfur 2 (4Fe-4S) By similarity
Binding site1781Ubiquinone; shared with DHSD By similarity

Sequences

Sequence LengthMass (Da)Tools
P48932 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 09511AE52A4CA149

FASTA25028,887
        10         20         30         40         50         60 
MIIKNLNQKI ITIDNSSPYQ KFIRIYRWNP NLNLNPWFSI FPISTNNCGP MILDALIQIK 

        70         80         90        100        110        120 
NIQDSSLTFR RSCREGICGS CSMNIDGTNS LACLRSLNTK SNFITIYPLP HTYIIKDLVP 

       130        140        150        160        170        180 
DLSNFYAQYK LIKPWLINKI GFSLKENLQS KIDRLELDGL YECILCACCS ASCPSYWWNQ 

       190        200        210        220        230        240 
DKYLGPAILL QAYRWIVDSR DNSTENRLNF LNNKMRLFRC HTIMNCSKTC PKSLNPGKAI 

       250 
ASIKYRIINN 

« Hide

References

[1]"Genes for two subunits of succinate dehydrogenase form a cluster on the mitochondrial genome of Rhodophyta."
Viehmann S., Richard O., Boyen C., Zetsche K.
Curr. Genet. 29:199-201(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of the mitochondrial DNA of the rhodophyte Chondrus crispus (Gigartinales). Gene content and genome organization."
Leblanc C., Boyen C., Richard O., Bonnard G., Grienenberger J.-M., Kloareg B.
J. Mol. Biol. 250:484-495(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Apices.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z47547 Genomic DNA. Translation: CAA87611.1.
PIRS59114.
RefSeqNP_062488.1. NC_001677.2.

3D structure databases

ProteinModelPortalP48932.
SMRP48932. Positions 18-244.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID809396.
KEGGccp:ChcroMp09.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 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]
PfamPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR00384. dhsB. 1 hit.
PROSITEPS00197. 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]
ProtoNetSearch...

Entry information

Entry nameSDHB_CHOCR
AccessionPrimary (citable) accession number: P48932
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways