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P48932

- SDHB_CHOCR

UniProt

P48932 - SDHB_CHOCR

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Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit

Gene
SDH2, SDHB
Organism
Chondrus crispus (Carragheen moss) (Irish moss)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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 bindingi73 – 731Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi78 – 781Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi81 – 811Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi93 – 931Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi166 – 1661Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi169 – 1691Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi173 – 1731Iron-sulfur 3 (3Fe-4S) By similarity
Binding sitei178 – 1781Ubiquinone; shared with DHSD By similarity
Metal bindingi220 – 2201Iron-sulfur 3 (3Fe-4S) By similarity
Metal bindingi226 – 2261Iron-sulfur 3 (3Fe-4S) By similarity
Metal bindingi230 – 2301Iron-sulfur 2 (4Fe-4S) By similarity

GO - Molecular functioni

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

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 (EC:1.3.5.1)
Alternative name(s):
Iron-sulfur subunit of complex II
Short name:
Ip
Gene namesi
Name:SDH2
Synonyms:SDHB
Encoded oniMitochondrion
OrganismiChondrus crispus (Carragheen moss) (Irish moss)
Taxonomic identifieri2769 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaFlorideophyceaeGigartinalesGigartinaceaeChondrus

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Succinate dehydrogenase [ubiquinone] iron-sulfur subunitPRO_0000158694Add
BLAST

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.

Structurei

3D structure databases

ProteinModelPortaliP48932.
SMRiP48932. Positions 18-244.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 110812Fe-2S ferredoxin-typeAdd
BLAST
Domaini153 – 183314Fe-4S ferredoxin-typeAdd
BLAST

Sequence similaritiesi

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.

P48932-1 [UniParc]FASTAAdd to Basket

« Hide

MIIKNLNQKI ITIDNSSPYQ KFIRIYRWNP NLNLNPWFSI FPISTNNCGP    50
MILDALIQIK NIQDSSLTFR RSCREGICGS CSMNIDGTNS LACLRSLNTK 100
SNFITIYPLP HTYIIKDLVP DLSNFYAQYK LIKPWLINKI GFSLKENLQS 150
KIDRLELDGL YECILCACCS ASCPSYWWNQ DKYLGPAILL QAYRWIVDSR 200
DNSTENRLNF LNNKMRLFRC HTIMNCSKTC PKSLNPGKAI ASIKYRIINN 250
Length:250
Mass (Da):28,887
Last modified:February 1, 1996 - v1
Checksum:i09511AE52A4CA149
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z47547 Genomic DNA. Translation: CAA87611.1.
PIRiS59114.
RefSeqiNP_062488.1. NC_001677.2.

Genome annotation databases

GeneIDi809396.
KEGGiccp:ChcroMp09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z47547 Genomic DNA. Translation: CAA87611.1 .
PIRi S59114.
RefSeqi NP_062488.1. NC_001677.2.

3D structure databases

ProteinModelPortali P48932.
SMRi P48932. Positions 18-244.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 809396.
KEGGi ccp:ChcroMp09.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01006 .

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

  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.

Entry informationi

Entry nameiSDHB_CHOCR
AccessioniPrimary (citable) accession number: P48932
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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