Reviewed, UniProtKB/Swiss-Prot Q007T0 (DHSB_PIG)

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

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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).
Catalytic activity	Succinate + ubiquinone = fumarate + ubiquinol.
Cofactor	Binds 1 2Fe-2S cluster. Binds 1 3Fe-4S cluster. Binds 1 4Fe-4S cluster.
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 b560 composed of SDHC and SDHD.
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.

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	3D-structure
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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 28

28

Mitochondrion

Chain

29 – 280

252

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

PRO_0000343799

Regions

Domain

40 – 131

92

2Fe-2S ferredoxin-type

Domain

176 – 206

31

4Fe-4S ferredoxin-type

Sites

Metal binding

93

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

98

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

101

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

113

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

186

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

189

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

192

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

196

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

243

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

249

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

253

1

Iron-sulfur 2 (4Fe-4S)

Binding site

201

1

Ubiquinone; shared with DHSD

Secondary structure

1

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280

Helix Strand Turn

Details...

Beta strand

39 – 46

8

Beta strand

57 – 64

8

Helix

65 – 67

3

Helix

72 – 81

10

Beta strand

94 – 98

5

Beta strand

103 – 105

3

Beta strand

108 – 110

3

Turn

112 – 114

3

Beta strand

123 – 128

6

Beta strand

130 – 137

8

Helix

144 – 151

8

Turn

163 – 167

5

Helix

174 – 178

5

Turn

179 – 185

7

Helix

193 – 195

3

Helix

197 – 202

6

Turn

203 – 205

3

Helix

208 – 219

12

Helix

227 – 232

6

Turn

237 – 242

6

Turn

248 – 252

5

Helix

259 – 270

12

Sequences

	Sequence		Length	Mass (Da)
	Q007T0-1 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 096B11189EF1ED59	FASTA	280	31,586
	10 20 30 40 50 60 MAAVVAVSLK RWFPATTLGG ACLQACRGAQ TAAATAPRIK KFAIYRWDPD KTGDKPHMQT 70 80 90 100 110 120 YEIDLNNCGP MVLDALIKIK NEIDSTLTFR RSCREGICGS CAMNINGGNT LACTRRIDTN 130 140 150 160 170 180 LDKVSKIYPL PHMYVIKDLV PDLSNFYAQY KSIEPYLKKK DESQEGKQQY LQSIEEREKL 190 200 210 220 230 240 DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDFTEER LAKLQDPFSL 250 260 270 280 YRCHTIMNCT GTCPKGLNPG KAIAEIKKMM ATYKEKKASA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Liu G.Y. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"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 13-264. Tissue: Liver.
[3]	"Crystal structure of mitochondrial respiratory membrane protein complex II." Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z. Cell 121:1043-1057(2005) [PubMed: 15989954] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 29-279 IN COMPLEX WITH IRON-SULFUR CLUSTERS AND UBIQUINONE, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

DQ915498 mRNA. Translation: ABJ09403.1.
DQ403018 mRNA. Translation: ABD77151.1.

RefSeq

NP_001098423.1.

UniGene

Ssc.55804

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZOY	X-ray	2.40	B	29-279	[»]
1ZP0	X-ray	3.50	B	29-279	[»]

ModBase

Search...

Genome annotation databases

GeneID

414412.

KEGG

ssc:414412.

Phylogenomic databases

HOVERGEN

Q007T0.

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...

Entry information

Entry name

DHSB_PIG

Accession

Primary (citable) accession number: Q007T0
Secondary accession number(s): Q0QEX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	November 14, 2006
Last modified:	November 25, 2008
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)