Reviewed, UniProtKB/Swiss-Prot P20921 (FRDB_PROVU)

Names and origin

Protein names

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

Gene names

Name:

frdB

Organism

Proteus vulgaris

Taxonomic identifier

585 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus

Protein attributes

Sequence length	245 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.
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
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 – 245	244	Fumarate reductase iron-sulfur subunit		PRO_0000158706
Regions
	Domain	13 – 98	86	2Fe-2S ferredoxin-type
	Domain	141 – 170	30	4Fe-4S ferredoxin-type
Sites
	Metal binding	59	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	64	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	67	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	79	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	150	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	153	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	156	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	160	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	206	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	212	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	216	1	Iron-sulfur 2 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P20921-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CEA17E28C8A390C2	FASTA	245	27,331
	10 20 30 40 50 60 MADDMKHVKM EVMRYNPETD DAPHFVTYDV PYDEQTSLLD ALGYIKDNLA PDLSYRWSCR 70 80 90 100 110 120 MAICGSCGMM VNRVPKLACK TFMRDYPNGV RIEALGNFPV ERDLVVDMTH FIESLEAIKP 130 140 150 160 170 180 YILGNDRKPS EGPNKQTPAQ MAKYHQFSGC INCGLCYAAC PQFGLNPEFI GPAAITLAQR 190 200 210 220 230 240 YNTDSRDHGA KERMPQLNGE NGVWSCTFVG YCSEVCPKHV DPAAAIQQGK AASAQDFVIA MLKPR

References

[1]

"Nucleotide sequence and comparative analysis of the frd operon encoding the fumarate reductase of Proteus vulgaris. Extensive sequence divergence of the membrane anchors and absence of an frd-linked ampC cephalosporinase gene." Cole S.T. Eur. J. Biochem. 167:481-488(1987) [PubMed: 3308458] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X06144 Genomic DNA. Translation: CAA29502.1.
PIR	RDEBIV. S00108.
3D structure databases
HSSP	HSSP built from PDB template 1KF6 based on UniProtKB P00364.
SMR	P20921. Positions 4-245.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.3.99.1. 641.
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_PROVU

Accession

Primary (citable) accession number: P20921

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 67 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)