P0AC47 (FRDB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	frdB
Ordered Locus Names:	b4153, JW4114

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	244 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	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.
Subunit structure	Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins.
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
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anaerobic respiration Inferred from mutant phenotype PubMed 14109218. Source: EcoCyc ciliary or flagellar motility Inferred from mutant phenotype PubMed 18337747. Source: EcoCyc electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW fermentation Inferred from mutant phenotype PubMed 14109218. Source: EcoCyc flagellum assembly Inferred from mutant phenotype PubMed 18337747. Source: EcoCyc tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.8. Source: EcoCyc membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from direct assay Ref.8. Source: EcoCyc 3 iron, 4 sulfur cluster binding Inferred from direct assay Ref.8. Source: EcoCyc 4 iron, 4 sulfur cluster binding Inferred from direct assay Ref.8. Source: EcoCyc electron carrier activity Inferred from direct assay PubMed 8499449. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
frdA	P00363	5	EBI-906724,EBI-550480
ompW	P0A915	2	EBI-906724,EBI-1132929

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 244

243

Fumarate reductase iron-sulfur subunit

PRO_0000158698

Regions

Domain

16 – 97

82

2Fe-2S ferredoxin-type

Domain

140 – 169

30

4Fe-4S ferredoxin-type

Sites

Metal binding

58

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

63

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

66

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

78

1

Iron-sulfur 1 (2Fe-2S)

Metal binding

149

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

152

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

155

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

159

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

205

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

211

1

Iron-sulfur 3 (3Fe-4S)

Metal binding

215

1

Iron-sulfur 2 (4Fe-4S)

Experimental info

Mutagenesis

58

1

C → S: Affects center 1 (2Fe-2S).

Mutagenesis

63

1

C → S: Affects center 1 (2Fe-2S).

Mutagenesis

66

1

C → S: Affects center 1 (2Fe-2S).

Mutagenesis

78

1

C → S: Affects center 1 (2Fe-2S).

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

244

Helix Strand Turn

Details...

Beta strand

5 – 13

9

Turn

16 – 18

3

Beta strand

23 – 31

9

Helix

37 – 47

11

Beta strand

59 – 63

5

Beta strand

67 – 70

4

Beta strand

73 – 76

4

Helix

77 – 79

3

Helix

82 – 84

3

Beta strand

89 – 93

5

Beta strand

99 – 101

3

Helix

108 – 116

9

Helix

128 – 130

3

Helix

137 – 141

5

Helix

144 – 147

4

Helix

154 – 158

5

Helix

160 – 164

5

Beta strand

166 – 168

3

Helix

171 – 181

11

Helix

190 – 197

8

Turn

199 – 201

3

Helix

202 – 204

3

Helix

210 – 214

5

Helix

221 – 240

20

Sequences

	Sequence		Length	Mass (Da)
	P0AC47 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: AC1D7A73244D7AC0	FASTA	244	27,123
	10 20 30 40 50 60 MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP DLSYRWSCRM 70 80 90 100 110 120 AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE RDLVVDMTHF IESLEAIKPY 130 140 150 160 170 180 IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI NCGLCYAACP QFGLNPEFIG PAAITLAHRY 190 200 210 220 230 240 NEDSRDHGKK ERMAQLNSQN GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT LKPR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Location and nucleotide sequence of frdB, the gene coding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli." Cole S.T., Grundstroem T., Jaurin B., Robinson J.J., Weiner J.H. Eur. J. Biochem. 126:211-216(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Overlap between ampC and frd operons on the Escherichia coli chromosome." Grundstroem T., Jaurin B. Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-244.
[6]	"Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster." Werth M.T., Cecchini G., Manodori A., Ackrell B.A.C., Schroeder I., Gunsalus R.P., Johnson M.K. Proc. Natl. Acad. Sci. U.S.A. 87:8965-8969(1990) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[7]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[8]	"Structure of the Escherichia coli fumarate reductase respiratory complex." Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C. Science 284:1961-1966(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
[9]	"Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site." Iverson T.M., Luna-Chavez C., Croal L.R., Cecchini G., Rees D.C. J. Biol. Chem. 277:16124-16130(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01611 Genomic DNA. Translation: AAA23438.1.
U14003 Genomic DNA. Translation: AAA97052.1.
U00096 Genomic DNA. Translation: AAC77113.1.
AP009048 Genomic DNA. Translation: BAE78157.1.
V00277 Genomic DNA. Translation: CAA23534.1.

PIR

RDECFS. A00377.

RefSeq

NP_418577.1. NC_000913.2.
YP_492298.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KF6	X-ray	2.70	B/N	2-244	[»]
1KFY	X-ray	3.60	B/N	2-244	[»]
1L0V	X-ray	3.30	B/N	2-244	[»]
2B76	X-ray	3.30	B/N	2-244	[»]
3CIR	X-ray	3.65	B/N	2-244	[»]
3P4P	X-ray	2.80	B/N	2-244	[»]
3P4Q	X-ray	3.35	B/N	2-244	[»]
3P4R	X-ray	3.05	B/N	2-244	[»]
3P4S	X-ray	3.10	B/N	2-244	[»]

ProteinModelPortal

P0AC47.

SMR

P0AC47. Positions 2-244.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AC47. 2 interactions.

STRING

511145.b4153.

Proteomic databases

PaxDb

P0AC47.

PRIDE

P0AC47.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77113; AAC77113; b4153.
BAE78157; BAE78157; BAE78157.

GeneID

12933707.
948666.

KEGG

ecj:Y75_p4042.
eco:b4153.

PATRIC

32123879. VBIEscCol129921_4287.

Organism-specific databases

EchoBASE

EB0327.

EcoGene

EG10331. frdB.

Phylogenomic databases

eggNOG

COG0479.

HOGENOM

HOG000160590.

KO

K00245.

OMA

NPRTPDQ.

ProtClustDB

PRK12385.

Enzyme and pathway databases

BioCyc

EcoCyc:FUM-FE-S.
ECOL316407:JW4114-MONOMER.
MetaCyc:FUM-FE-S.

Gene expression databases

Genevestigator

P0AC47.

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

P0AC47.

Entry information

Entry name

FRDB_ECOLI

Accession

Primary (citable) accession number: P0AC47
Secondary accession number(s): P00364, Q2M6E9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program