Succinate dehydrogenase [ubiquinone] iron-sulfur subunit

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Reviewed, UniProtKB/Swiss-Prot P48932 (DHSB_CHOCR)

Last modified June 16, 2009. Version 68. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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 names

Name:	SDH2
Synonyms:	SDHB

Encoded on

Mitochondrion

Organism

Chondrus crispus (Carragheen)

Taxonomic identifier

2769 [NCBI]

Taxonomic lineage

Eukaryota › Rhodophyta › Florideophyceae › Gigartinales › Gigartinaceae › Chondrus

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Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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 + ubiquinone = fumarate + ubiquinol.
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.
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.

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Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 250

250

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit

PRO_0000158694

Regions

Domain

30 – 110

2Fe-2S ferredoxin-type

Domain

153 – 183

4Fe-4S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

163

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

166

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

169

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

173

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

220

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

226

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

230

Iron-sulfur 2 (4Fe-4S) By similarity

Binding site

178

Ubiquinone; shared with DHSD By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P48932-1 [UniParc].

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

250

28,887

        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

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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: 8821668] [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: 7616569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Apices.

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Cross-references

Sequence databases
	Z47547 Genomic DNA. Translation: CAA87611.1.
PIR	S59114.
RefSeq	NP_062488.1.
3D structure databases
HSSP	HSSP built from PDB template 1NEK based on UniProtKB P07014.
ModBase	Search...
Genome annotation databases
GeneID	809396.
Enzyme and pathway databases
BRENDA	1.3.5.1. 190989.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR004489. Succ_DH/fum_Rdtase_Fe-S. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
TIGRFAMs	TIGR00384. dhsB. 1 hit.
PROSITE	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]
ProtoNet	Search...

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Entry information

Entry name

DHSB_CHOCR

Accession

Primary (citable) accession number: P48932

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents