Reviewed, UniProtKB/Swiss-Prot P17596 (FRDB_WOLSU)

Names and origin

Protein names

Recommended name:
    Fumarate reductase iron-sulfur subunit
    EC=1.3.99.1

Gene names

Name:	frdB
Ordered Locus Names:	WS0830

Organism

Wolinella succinogenes [Complete proteome] [HAMAP]

Taxonomic identifier

844 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Wolinella

Protein attributes

Sequence length	239 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor.
Catalytic activity	Succinate + acceptor = fumarate + reduced acceptor.
Cofactor	Binds 1 2Fe-2S cluster. Binds 1 3Fe-4S cluster. Binds 1 4Fe-4S cluster.
Subunit structure	Part of an enzyme complex containing three subunits: a flavoprotein, an iron-sulfur protein, and cytochrome b-556.
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 Respiratory chain Transport Tricarboxylic acid cycle
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
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 respiratory chain 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 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

Chain

1 – 239

239

Fumarate reductase iron-sulfur subunit

PRO_0000158708

Regions

Domain

5 – 95

91

2Fe-2S ferredoxin-type

Domain

142 – 171

30

4Fe-4S ferredoxin-type

Sites

Metal binding

57

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

62

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

65

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

77

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

151

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

154

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

157

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

161

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

208

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

214

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

218

1

Iron-sulfur 2 (4Fe-4S)

Secondary structure

1

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239

Helix Strand Turn

Details...

Beta strand

4 – 11

8

Beta strand

22 – 29

8

Helix

36 – 46

11

Beta strand

58 – 62

5

Beta strand

66 – 69

4

Beta strand

72 – 75

4

Helix

76 – 78

3

Helix

81 – 83

3

Beta strand

87 – 92

6

Beta strand

97 – 101

5

Beta strand

104 – 106

3

Helix

108 – 117

10

Helix

139 – 149

11

Helix

156 – 159

4

Helix

162 – 166

5

Helix

172 – 183

12

Helix

192 – 199

8

Turn

202 – 204

3

Helix

205 – 207

3

Helix

213 – 217

5

Helix

224 – 235

12

Sequences

	Sequence		Length	Mass (Da)
	P17596-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 24D1992489B8FFD1	FASTA	239	27,165
	10 20 30 40 50 60 MGRMLTIRVF KYDPQSAVSK PHFQEYKIEE APSMTIFIVL NMIRETYDPD LNFDFVCRAG 70 80 90 100 110 120 ICGSCGMMIN GRPSLACRTL TKDFEDGVIT LLPLPAFKLI KDLSVDTGNW FNGMSQRVES 130 140 150 160 170 180 WIHAQKEHDI SKLEERIEPE VAQEVFELDR CIECGCCIAA CGTKIMREDF VGAAGLNRVV 190 200 210 220 230 RFMIDPHDER TDEDYYELIG DDDGVFGCMT LLACHDVCPK NLPLQSKIAY LRRKMVSVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The fumarate reductase operon of Wolinella succinogenes. Sequence and expression of the frdA and frdB genes." Lauterbach F., Koertner C., Albracht S.P., Unden G., Kroeger A. Arch. Microbiol. 154:386-393(1990) [PubMed: 2244791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon." Simon J., Gross R., Ringel M., Schmidt E., Kroeger A. Eur. J. Biochem. 251:418-426(1998) [PubMed: 9492313] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]	"Complete genome sequence and analysis of Wolinella succinogenes." Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., Meyer F., Lederer H., Schuster S.C. Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003) [PubMed: 14500908] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSMZ 1740.
[4]	"Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution." Lancaster C.R.D., Kroeger A., Auer M., Michel H. Nature 402:377-385(1999) [PubMed: 10586875] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]	"A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction." Lancaster C.R.D., Gross R., Simon J. Eur. J. Biochem. 268:1820-1827(2001) [PubMed: 11248702] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ000662 Genomic DNA. Translation: CAA04215.1.
BX571659 Genomic DNA. Translation: CAE09941.1.

PIR

C44954.

RefSeq

NP_907041.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E7P	X-ray	3.10	B/E/H/K	1-239	[»]
1QLB	X-ray	2.33	B/E	1-239	[»]
2BS2	X-ray	1.78	B/E	1-239	[»]
2BS3	X-ray	2.19	B/E	1-239	[»]
2BS4	X-ray	2.76	B/E	1-239	[»]

ModBase

Search...

Genome annotation databases

GeneID

2555194.

GenomeReviews

Gene locus WS0830 in contig BX571656_GR.

KEGG

wsu:WS0830.

NMPDR

fig|273121.1.peg.768.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P17596.

Enzyme and pathway databases

BioCyc

WSUC273121:WS0830-MON.

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

PF00037. Fer4. 1 hit.
[Graphical view]

PRINTS

PR00353. 4FE4SFRDOXIN.

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

FRDB_WOLSU

Accession

Primary (citable) accession number: P17596

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	November 25, 2008
This is version 90 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)