Reviewed, UniProtKB/Swiss-Prot Q9YHT2 (DHSB_CHICK)

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

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	290 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 side.
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 – 38

38

Mitochondrion

Chain

39 – 290

252

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

PRO_0000343800

Regions

Domain

50 – 143

94

2Fe-2S ferredoxin-type

Domain

186 – 216

31

4Fe-4S ferredoxin-type

Sites

Metal binding

103

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

108

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

111

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

123

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

196

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

199

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

202

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

206

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

253

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

259

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

263

1

Iron-sulfur 2 (4Fe-4S)

Binding site

211

1

Ubiquinone; shared with DHSD

Secondary structure

1

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290

Helix Strand Turn

Details...

Beta strand

49 – 56

8

Beta strand

67 – 74

8

Helix

75 – 77

3

Helix

82 – 92

11

Beta strand

104 – 108

5

Beta strand

112 – 115

4

Beta strand

118 – 121

4

Helix

122 – 124

3

Beta strand

133 – 138

6

Beta strand

144 – 147

4

Helix

154 – 162

9

Turn

173 – 177

5

Helix

184 – 188

5

Turn

189 – 195

7

Helix

203 – 205

3

Helix

207 – 212

6

Turn

213 – 215

3

Helix

219 – 229

11

Helix

237 – 242

6

Beta strand

246 – 248

3

Turn

249 – 252

4

Helix

258 – 262

5

Helix

269 – 282

14

Sequences

	Sequence		Length	Mass (Da)
	Q9YHT2-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 313E698866B3FDFC	FASTA	290	32,597
	10 20 30 40 50 60 MAAAVVGVSL RRGVPARFLR AGLRPVRGLE AVHGICRGAQ TAAAATSRIK KFSIYRWDPD 70 80 90 100 110 120 KPGDKPRMQT YEVDLNKCGP MVLDALIKIK NELDSTLTFR RSCREGICGS CAMNIAGGNT 130 140 150 160 170 180 LACTKKIDPD LSKTTKIYPL PHMYVVKDLV PDLSNFYAQY KSIEPYLKKK DESKQGKEQY 190 200 210 220 230 240 LQSIEDRQKL DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDYTEER 250 260 270 280 290 LAQLQDPFSL YRCHTIMNCT RTCPKGLNPG KAIAEIKKMM ATYKEKAAAA

References

[1]	"OXPHOS genes in mammals and the molecular clock." Weinreich D.M. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	"Crystallization of mitochondrial respiratory complex II from chicken heart: a membrane-protein complex diffracting to 2.0 A." Huang L.-S., Borders T.M., Shen J.T., Wang C.-J., Berry E.A. Acta Crystallogr. D 61:380-387(2005) [PubMed: 15805592] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OF 39-290, SUBUNIT, SUBCELLULAR LOCATION.
[3]	"Crystallographic studies of the binding of ligands to the dicarboxylate site of complex II, and the identity of the ligand in the 'oxaloacetate-inhibited' state." Huang L.-S., Shen J.T., Wang A.C., Berry E.A. Biochim. Biophys. Acta 1757:1073-1083(2006) [PubMed: 16935256] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF OF 39-290 IN COMPLEX WITH UBIQUINONE AND IRON-SULFUR CENTERS, SUBUNIT, SUBCELLULAR LOCATION.
[4]	"3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme." Huang L.-S., Sun G., Cobessi D., Wang A.C., Shen J.T., Tung E.Y., Anderson V.E., Berry E.A. J. Biol. Chem. 281:5965-5972(2006) [PubMed: 16371358] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 39-290 IN COMPLEX WITH UBIQUINONE AND IRON-SULFUR CENTERS, SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF095937 mRNA. Translation: AAC72372.1.

RefSeq

NP_001074344.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YQ3	X-ray	2.20	B	39-290	[»]
1YQ4	X-ray	2.33	B	39-290	[»]
2FBW	X-ray	2.10	B/O	39-290	[»]
2H88	X-ray	1.74	B/O	39-290	[»]
2H89	X-ray	2.40	B	39-290	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSGALG00000000508. Gallus gallus. [Contig view]

GeneID

770063.

KEGG

gga:770063.

Phylogenomic databases

HOGENOM

Q9YHT2.

HOVERGEN

Q9YHT2.

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.

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_CHICK

Accession

Primary (citable) accession number: Q9YHT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	May 1, 1999
Last modified:	November 25, 2008
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)