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

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Reviewed, UniProtKB/Swiss-Prot Q3B8J8 (DHSB_XENLA)

Last modified November 25, 2008. Version 30. History...

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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, mitochondrial
    EC=1.3.5.1
Alternative name(s):
    Iron-sulfur subunit of complex II
      Short name=Ip

Gene names

Name:

sdhb

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

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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.

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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: the flavoprotein (FP) sdha, iron-sulfur protein (IP) sdhb, and a cytochrome b composed of sdhc and sdhd By similarity.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix sideBy 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
Domain	Transit peptide
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: InterPro
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW
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

Transit peptide

1 – 26

Mitochondrion By similarity

Chain

27 – 282

256

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

PRO_0000343802

Regions

Domain

42 – 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

164

K → E in AAH43859. Ref.1

Sequence conflict

279

A → V in AAH43859. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q3B8J8-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: FCEE9AA00E84E689
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FASTA

282

31,777

        10         20         30         40         50         60 
MAAVVFSLRR SGPVLRLSGA LQVSRGAQTA AAPASQAAAR IKKFAIYRWD PDKPGDKPRM 

        70         80         90        100        110        120 
QTYEVDLNTC GPMVLDALIK IKNEVDPTLT FRRSCREGIC GSCAMNINGG NTLACTVRID 

       130        140        150        160        170        180 
TNLSKVSKIY PLPHMYVVKD LVPDLSNFYA QYKSIEPYLK KKDKSQQGKE QYLQSIEDRD 

       190        200        210        220        230        240 
KLDGLYECIL CACCSTSCPS YWWNADKYLG PAVLMQAYRW MIDSRDDFTE ERLSKLQDPF 

       250        260        270        280 
SLYRCHTIMN CTRTCPKGLN PGKAIAEIKK MMAMYKERAV SA

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References

[1]	NIH - Xenopus Gene Collection (XGC) project Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo and Testis.

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Cross-references

Sequence databases
	BC043859 mRNA. Translation: AAH43859.1. BC106300 mRNA. Translation: AAI06301.1.
RefSeq	NP_001080247.1.
UniGene	Xl.12560
3D structure databases
SMR	Q3B8J8. Positions 40-277.
ModBase	Search...
Genome annotation databases
GeneID	379939.
KEGG	xla:379939.
Organism-specific databases
Xenbase	XB-FEAT-970192. sdhb.
Phylogenomic databases
HOVERGEN	Q3B8J8.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR001450. 4Fe4S_Fe_S_bd. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR004489. Succ_DHase/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.
Pfam	PF00111. Fer2. 1 hit. [Graphical view]
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_XENLA

Accession

Primary (citable) accession number: Q3B8J8
Secondary accession number(s): Q7ZYB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	November 22, 2005
Last modified:	November 25, 2008
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project

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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

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents