Reviewed, UniProtKB/Swiss-Prot P0AC47 (FRDB_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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
Gene Ontology (GO)
Biological process	anaerobic respiration Inferred from mutant phenotype. Source: UniProtKB ciliary or flagellar motility Inferred from mutant phenotype. Source: UniProtKB electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW fermentation Inferred from mutant phenotype. Source: UniProtKB flagellum assembly Inferred from mutant phenotype. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Ref.7 Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	2 iron, 2 sulfur cluster binding Ref.7 Inferred from direct assay. Source: UniProtKB 3 iron, 4 sulfur cluster binding Ref.7 Inferred from direct assay. Source: UniProtKB 4 iron, 4 sulfur cluster binding Ref.7 Inferred from direct assay. Source: UniProtKB electron carrier activity Inferred from direct assay. Source: UniProtKB 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
ompW	P0A915	1	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

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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

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)
	P0AC47-1 [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: 6751816] [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: 7610040] [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: 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]	"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: 7041115] [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: 2174169] [Abstract] Cited for: MUTAGENESIS.
[7]	"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: 10373108] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
[8]	"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: 11850430] [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

AP_004656.1.
NP_418577.1.

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AC47. 2 interactions.

STRING

P0AC47.

2-D gel databases

ECO2DBASE

H024.7. 6TH EDITION.

Genome annotation databases

GeneID

948666.

GenomeReviews

Gene locus JW4114 in contig AP009048_GR.
Gene locus b4153 in contig U00096_GR.

KEGG

ecj:JW4114.
eco:b4153.

Organism-specific databases

EchoBASE

EB0327.

EcoGene

EG10331. frdB.

CMR

Search...

Phylogenomic databases

eggNOG

COG0479.

HOGENOM

HBG616382.

OMA

YAACPQY.

Enzyme and pathway databases

BioCyc

EcoCyc:FUM-FE-S.
ECOL168927:B4153-MONOMER.
MetaCyc:FUM-FE-S.

Gene expression databases

Genevestigator

P0AC47.

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.
IPR009051. Helical_ferredxn.
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. 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_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:	February 9, 2010
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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