Reviewed, UniProtKB/Swiss-Prot P07014 (DHSB_ECOLI)

Names and origin

Protein names

Recommended name:
    Succinate dehydrogenase iron-sulfur subunit
    EC=1.3.99.1

Gene names

Name:	sdhB
Ordered Locus Names:	b0724, JW0714

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	238 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.
Catalytic activity	Succinate + acceptor = fumarate + reduced acceptor.
Cofactor	Binds 1 2Fe-2S cluster. Binds 1 3Fe-4S cluster. Binds 1 4Fe-4S cluster.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
Subunit structure	Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, cytochrome b-556, and an hydrophobic anchor protein. The complex forms trimers. Ref.7
Subcellular location	Cell inner membrane; Peripheral membrane protein. Ref.7
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	Cell inner membrane Cell membrane Membrane
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
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	plasma 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 protein binding Inferred from physical interaction. Source: IntAct succinate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	1	EBI-1035514,EBI-543750

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 238

238

Succinate dehydrogenase iron-sulfur subunit

PRO_0000158688

Regions

Domain

8 – 97

90

2Fe-2S ferredoxin-type

Domain

139 – 169

31

4Fe-4S ferredoxin-type

Sites

Metal binding

55

1

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

Metal binding

60

1

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

Metal binding

63

1

Iron-sulfur 1 (2Fe-2S) Potential

Metal binding

75

1

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

Metal binding

149

1

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

Metal binding

152

1

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

Metal binding

155

1

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

Metal binding

159

1

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

Metal binding

206

1

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

Metal binding

212

1

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

Metal binding

216

1

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

Secondary structure

1

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238

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Turn

12 – 14

3

Beta strand

19 – 24

6

Beta strand

29 – 31

3

Helix

35 – 45

11

Beta strand

55 – 58

4

Beta strand

64 – 67

4

Beta strand

70 – 73

4

Turn

79 – 82

4

Beta strand

89 – 92

4

Beta strand

95 – 101

7

Helix

108 – 116

9

Beta strand

130 – 132

3

Helix

137 – 141

5

Turn

142 – 146

5

Helix

154 – 157

4

Helix

160 – 164

5

Turn

166 – 168

3

Helix

172 – 182

11

Helix

190 – 195

6

Beta strand

199 – 201

3

Turn

202 – 205

4

Helix

211 – 215

5

Helix

222 – 236

15

Sequences

	Sequence		Length	Mass (Da)
	P07014-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 226F60C55F5AC35A	FASTA	238	26,770
	10 20 30 40 50 60 MRLEFSIYRY NPDVDDAPRM QDYTLEADEG RDMMLLDALI QLKEKDPSLS FRRSCREGVC 70 80 90 100 110 120 GSDGLNMNGK NGLACITPIS ALNQPGKKIV IRPLPGLPVI RDLVVDMGQF YAQYEKIKPY 130 140 150 160 170 180 LLNNGQNPPA REHLQMPEQR EKLDGLYECI LCACCSTSCP SFWWNPDKFI GPAGLLAAYR 190 200 210 220 230 FLIDSRDTET DSRLDGLSDA FSVFRCHSIM NCVSVCPKGL NPTRAIGHIK SMLLQRNA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli." Darlison M.G., Guest J.R. Biochem. J. 223:507-517(1984) [PubMed: 6388571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12." Darlison M.G., Spencer M.E., Guest J.R. Eur. J. Biochem. 141:351-359(1984) [PubMed: 6376123] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-238.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-11. Strain: K12 / EMG2.
[7]	"Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed: 16079137] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION. Strain: BL21-DE3.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J01619 Genomic DNA. Translation: AAA23896.1.
X01070 Genomic DNA. Translation: CAA25534.1.
U00096 Genomic DNA. Translation: AAC73818.1.
AP009048 Genomic DNA. Translation: BAA35391.1.
X00661 Genomic DNA. Translation: CAA25279.1.

PIR

DEECSI. A28837.

RefSeq

AP_001362.1.
NP_415252.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NEK	X-ray	2.60	B	1-238	[»]
1NEN	X-ray	2.90	B	1-238	[»]
2ACZ	X-ray	3.10	B	1-238	[»]
2AD0	model	-	B	1-238	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10836N.

IntAct

P07014. 4 interactions.

Genome annotation databases

GeneID

945300.

GenomeReviews

Gene locus JW0714 in contig AP009048_GR.
Gene locus b0724 in contig U00096_GR.

KEGG

ecj:JW0714.
eco:b0724.

Organism-specific databases

EchoBASE

EB0925.

EcoGene

EG10932. sdhB.

CMR

Search...

Phylogenomic databases

HOGENOM

P07014.

OMA

P07014. ADSRDDN.

Enzyme and pathway databases

BioCyc

EcoCyc:SDH-FE-S.
MetaCyc:SDH-FE-S.

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. False negative.
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_ECOLI

Accession

Primary (citable) accession number: P07014

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	June 16, 2009
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)