Reviewed, UniProtKB/Swiss-Prot P20922 (FRDA_PROVU)

Names and origin

Protein names

Recommended name:
    Fumarate reductase flavoprotein subunit
    EC=1.3.99.1

Gene names

Name:

frdA

Organism

Proteus vulgaris

Taxonomic identifier

585 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus

Protein attributes

Sequence length	598 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 FAD covalently per subunit.
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 FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Ontologies

Keywords
Biological process	Electron transport Transport
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	anaerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro 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 – 598	598	Fumarate reductase flavoprotein subunit		PRO_0000158666
Regions
	Nucleotide binding	9 – 23	15	FAD Potential
Sites
	Active site	233	1	By similarity
	Active site	249	1	By similarity
Amino acid modifications
	Modified residue	45	1	Tele-8alpha-FAD histidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P20922-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: AB205F8CEAA186AD	FASTA	598	66,142
	10 20 30 40 50 60 MQTFNADIAI IGAGGAGLRA AIAAAEANPQ LKIALISKVY PMRSHTVAAE GGSAAVTQAH 70 80 90 100 110 120 DSYDFHFNDT VSGGDWLCEQ DVVDYFVEHC PTEMTQLELW GCPWSRKEDG SVNVRRFGGM 130 140 150 160 170 180 KIERTWFAAD KTGFHMLHTL FQTSLKYPQI QRFDEHFVLD ILVDEGHARG VVAINMMEGT 190 200 210 220 230 240 KVQIRANAVI MATGGAGRVY RFNTNGGIVT GDGMGIALRH GVPLRDMEFV QYHPTGLPGS 250 260 270 280 290 300 GILMTEGCRG EGGILVNKDG YRYLQDYGLG PETPLGKPEN KYMELGPRDK VSQAFWHEWR 310 320 330 340 350 360 AGRTIKTHRG DVVHLDLRHL GAKKLHERLP FICELAKAYV GVDPVNEPIP VRPTAHYTMG 370 380 390 400 410 420 GIETNQRTET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL VVFGRLAGEE AVRRAQEATP 430 440 450 460 470 480 ANASALDAQT RDIEDNLKKL MNQKGSENWA QIRDEMGEAM EEGCGIYRTP ELMQKTIDKL 490 500 510 520 530 540 TELKERFKHV EIKDTSSVFN TDLLYKIELG FGLDVAECMA HSAFNRKESR GAHQRLDEGC 550 560 570 580 590 TERDDVNFLK HTLAFYNPEG APRLEYSDVK ITKSAPAKRV YGGEATAQDK QNKEKANG

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: CAA29501.1.
PIR	RDEBFV. S00107.
3D structure databases
HSSP	HSSP built from PDB template 1KF6 based on UniProtKB P00363.
SMR	P20922. Positions 1-577.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.3.99.1. 641.
Family and domain databases
InterPro	IPR003953. FAD_bind2_N. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR003952. FRD_SDH_FAD_BS. IPR004112. Fum_Rdtase/Succ_DH_flav_C. IPR005884. Fum_red_fp. IPR014006. Succ_Dhase_frdA_Gneg. [Graphical view]
Pfam	PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
TIGRFAMs	TIGR01176. fum_red_Fp. 1 hit. TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITE	PS00504. FRD_SDH_FAD_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FRDA_PROVU

Accession

Primary (citable) accession number: P20922

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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