Reviewed, UniProtKB/Swiss-Prot P0AC48 (FRDB_ECOL6)

Names and origin

Protein names

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

Gene names

Name:	frdB
Ordered Locus Names:	c5241

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [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	Inferred from homology.

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 By similarity.
Catalytic activity	Succinate + acceptor = fumarate + reduced acceptor.
Cofactor	Binds 1 2Fe-2S cluster By similarity. Binds 1 3Fe-4S cluster By similarity. Binds 1 4Fe-4S cluster By similarity.
Subunit structure	Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins By similarity.
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	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: 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 244	243	Fumarate reductase iron-sulfur subunit		PRO_0000158700
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) By similarity
	Metal binding	63	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	66	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	78	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	205	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	211	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	215	1	Iron-sulfur 2 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AC48-1 [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

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN83663.1.
RefSeq	NP_757089.1.
3D structure databases
SMR	P0AC48. Positions 2-244.
ModBase	Search...
Genome annotation databases
GeneID	1037508.
GenomeReviews	Gene locus c5241 in contig AE014075_GR.
KEGG	ecc:c5241.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0AC48.
OMA	P0AC48. YAACPQY.
Enzyme and pathway databases
BRENDA	1.3.99.1. 292881.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR001450. 4Fe4S_Fe_S_bd_subgr. 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.
Pfam	PF00037. Fer4. 1 hit. [Graphical view]
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_ECOL6

Accession

Primary (citable) accession number: P0AC48
Secondary accession number(s): P00364

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 30 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)