Fumarate reductase iron-sulfur subunit - Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W)

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P17596 (FRDB_WOLSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes) [Complete proteome] [HAMAP]

Taxonomic identifier

273121 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Wolinella ›

Protein attributes

Sequence length	239 AA.
Sequence status	Complete.
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. Ref.2
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 tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	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 metal 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

2Fe-2S ferredoxin-type

Domain

142 – 171

4Fe-4S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

Iron-sulfur 1 (2Fe-2S)

Metal binding

151

Iron-sulfur 2 (4Fe-4S)

Metal binding

154

Iron-sulfur 2 (4Fe-4S)

Metal binding

157

Iron-sulfur 2 (4Fe-4S)

Metal binding

161

Iron-sulfur 3 (3Fe-4S)

Metal binding

208

Iron-sulfur 3 (3Fe-4S)

Metal binding

214

Iron-sulfur 3 (3Fe-4S)

Metal binding

218

Iron-sulfur 2 (4Fe-4S)

Secondary structure

239

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P17596 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 24D1992489B8FFD1
Show »

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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PIR

C44954.

RefSeq

NP_907041.1. NC_005090.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P17596.

SMR

P17596. Positions 1-239.

ModBase

Search...

Protein-protein interaction databases

STRING

273121.WS0830.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAE09941; CAE09941; WS0830.

GeneID

2555194.

KEGG

wsu:WS0830.

PATRIC

24038706. VBIWolSuc63014_0782.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0479.

HOGENOM

HOG000160590.

K00245.

OMA

CRTLTKD.

ProtClustDB

PRK13552.

Family and domain databases

Gene3D

1.10.1060.10. 1 hit.
3.10.20.30. 1 hit.

InterPro

IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR012285. Fum_reductase_C.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]

Pfam

PF13085. Fer2_3. 1 hit.
PF13183. Fer4_8. 1 hit.
[Graphical view]

SUPFAM

SSF54292. Ferredoxin. 1 hit.
SSF46548. Helical_ferredxn. 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...

Other

EvolutionaryTrace

P17596.

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:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents