Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial precursor

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P21913 (DHSB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 107. History...

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

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Sdhb
Synonyms:	Sdh1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

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; fumarate from succinate (eukaryal route): step 1/1.
Subunit structure	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 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.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	respiratory electron transport chain Inferred from mutant phenotype. Source: RGD succinate metabolic process Inferred from mutant phenotype. Source: RGD transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial respiratory chain complex II Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	2 iron, 2 sulfur cluster binding Inferred from sequence or structural similarity. Source: UniProtKB 3 iron, 4 sulfur cluster binding Inferred from sequence or structural similarity. Source: UniProtKB 4 iron, 4 sulfur cluster binding Inferred from sequence or structural similarity. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase (ubiquinone) activity Inferred from mutant phenotype. Source: RGD ubiquinone binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 30

Mitochondrion By similarity

Chain

31 – 282

252

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

PRO_0000158693

Regions

Domain

56 – 135

2Fe-2S ferredoxin-type

Domain

178 – 208

4Fe-4S ferredoxin-type

Sites

Metal binding

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

Metal binding

100

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

Metal binding

103

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

Metal binding

115

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

Metal binding

188

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

Metal binding

191

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

Metal binding

194

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

Metal binding

198

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

Metal binding

245

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

Metal binding

251

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

Metal binding

255

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

Binding site

203

Ubiquinone; shared with DHSD By similarity

Experimental info

Sequence conflict

122 – 124

DLG → NLN no nucleotide entry Ref.4

Sequence conflict

153

K → R no nucleotide entry Ref.4

Sequence conflict

178

D → E no nucleotide entry Ref.4

Sequence conflict

227

E → D no nucleotide entry Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P21913 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 6600EBC8201529A9
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FASTA

282

31,830

        10         20         30         40         50         60 
MAAVVGVSLK RGFSATALGR VGLQFQACRE AQTAAAAAPR IKTFAIYRWD PDKAGDKPRM 

        70         80         90        100        110        120 
QTYKVDLNKC GPMVLDALIK IKNEIDSTLT FRRSCREGIC GSCAMNINGG NTLACTRRID 

       130        140        150        160        170        180 
TDLGKVSKIY PLPHMYVIKD LVPDLSNFYA QYKSIEPYLK KKDESQEGKQ QYLQSIEDRE 

       190        200        210        220        230        240 
KLDGLYECIL CACCSTSCPS YWWNGDKYLG PAVLMQAYRW MIDSRDEFTE ERLAKLQDPF 

       250        260        270        280 
SLYRCHTIMN CTQTCPKGLN PGKAIAEIKK MMATYKEKRA LA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[3]	"Housekeeping genes for phylogenetic analysis of eutherian relationships." Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A. Mol. Biol. Evol. 23:1493-1503(2006) [PubMed: 16751257] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-257. Tissue: Liver.
[4]	"Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species." Gould S.J., Subramani S., Scheffler I.E. Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989) [PubMed: 2494655] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-251. Tissue: Brain cortex.
[5]	Erratum Gould S.J., Subramani S., Scheffler I.E. Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH473968 Genomic DNA. Translation: EDL80954.1. BC158620 mRNA. Translation: AAI58621.1. DQ403001 mRNA. Translation: ABD77134.1.
IPI	IPI00785564.
PIR	B32394.
RefSeq	NP_001094009.1. NM_001100539.1.
UniGene	Rn.3902.
3D structure databases
ProteinModelPortal	P21913.
SMR	P21913. Positions 39-277.
ModBase	Search...
Protein-protein interaction databases
STRING	P21913.
PTM databases
PhosphoSite	P21913.
Proteomic databases
PRIDE	P21913.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000010593; ENSRNOP00000010593; ENSRNOG00000007967.
GeneID	298596.
KEGG	rno:298596.
Organism-specific databases
CTD	6390.
RGD	1308598. Sdhb.
Phylogenomic databases
eggNOG	roNOG06326.
GeneTree	ENSGT00390000013558.
HOVERGEN	HBG005483.
InParanoid	P21913.
OMA	IQVTQAI.
OrthoDB	EOG4T4CW4.
PhylomeDB	P21913.
Gene expression databases
ArrayExpress	P21913.
Genevestigator	P21913.
GermOnline	ENSRNOG00000007967. Rattus norvegicus.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012675. Beta-grasp_ferredoxin-type. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR009051. Helical_ferredxn. 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.
KO	K00235.
SUPFAM	SSF54292. Ferredoxin. 1 hit. SSF46548. Helical_ferredxn. 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...

Entry information

Entry name

DHSB_RAT

Accession

Primary (citable) accession number: P21913
Secondary accession number(s): B0BMZ2, Q0QEZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	September 2, 2008
Last modified:	November 16, 2011
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents