Fumarate reductase flavoprotein subunit - Escherichia coli (strain K12)

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P00363 (FRDA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 145. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Fumarate reductase flavoprotein subunit
EC=1.3.99.1

Gene names

Name:	frdA
Ordered Locus Names:	b4154, JW4115

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	602 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 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
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 response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki
Cellular_component	cytoplasm Inferred from direct assay Ref.9. Source: EcoCyc membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	electron carrier activity Inferred from direct assay PubMed 8499449. Source: EcoCyc flavin adenine dinucleotide binding Inferred from direct assay PubMed 381310. Source: EcoCyc succinate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
frdB	P0AC47	5	EBI-550480,EBI-906724

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 602

601

Fumarate reductase flavoprotein subunit

PRO_0000158660

Regions

Nucleotide binding

9 – 23

FAD Potential

Sites

Active site

233

Active site

249

Amino acid modifications

Modified residue

Tele-8alpha-FAD histidine

Experimental info

Mutagenesis

H → R: Inactivates enzyme. Ref.5

Mutagenesis

H → S, C or Y: Decreased ability (greater than 70%) to reduce fumarate. Ref.5

Mutagenesis

233

H → S: Severely affect succinate oxidation and decrease fumarate oxidation by 75%. Ref.6

Mutagenesis

248

C → S or A: Does not inactivate enzyme. Ref.6

Mutagenesis

249

R → H or L: Inactivates enzyme. Ref.6

Sequence conflict

386

L → P in AAA23437. Ref.1

Secondary structure

602

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00363 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3306D7FF6E198AE9
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FASTA

602

65,972

        10         20         30         40         50         60 
MQTFQADLAI VGAGGAGLRA AIAAAQANPN AKIALISKVY PMRSHTVAAE GGSAAVAQDH 

        70         80         90        100        110        120 
DSFEYHFHDT VAGGDWLCEQ DVVDYFVHHC PTEMTQLELW GCPWSRRPDG SVNVRRFGGM 

       130        140        150        160        170        180 
KIERTWFAAD KTGFHMLHTL FQTSLQFPQI QRFDEHFVLD ILVDDGHVRG LVAMNMMEGT 

       190        200        210        220        230        240 
LVQIRANAVV MATGGAGRVY RYNTNGGIVT GDGMGMALSH GVPLRDMEFV QYHPTGLPGS 

       250        260        270        280        290        300 
GILMTEGCRG EGGILVNKNG YRYLQDYGMG PETPLGEPKN KYMELGPRDK VSQAFWHEWR 

       310        320        330        340        350        360 
KGNTISTPRG DVVYLDLRHL GEKKLHERLP FICELAKAYV GVDPVKEPIP VRPTAHYTMG 

       370        380        390        400        410        420 
GIETDQNCET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL VVFGRLAGEQ ATERAATAGN 

       430        440        450        460        470        480 
GNEAAIEAQA AGVEQRLKDL VNQDGGENWA KIRDEMGLAM EEGCGIYRTP ELMQKTIDKL 

       490        500        510        520        530        540 
AELQERFKRV RITDTSSVFN TDLLYTIELG HGLNVAECMA HSAMARKESR GAHQRLDEGC 

       550        560        570        580        590        600 
TERDDVNFLK HTLAFRDADG TTRLEYSDVK ITTLPPAKRV YGGEADAADK AEAANKKEKA 


NG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli." Cole S.T. Eur. J. Biochem. 122:479-484(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]	"Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin." Blaut M., Whittaker K., Valdovinos A., Ackrell B.A., Gunsalus R.P., Cecchini G. J. Biol. Chem. 264:13599-13604(1989) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-45.
[6]	"Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis." Schroeder I., Gunsalus R.P., Ackrell B.A.C., Cochran B., Cecchini G. J. Biol. Chem. 266:13572-13579(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF HIS-233; CYS-248 AND ARG-249.
[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]	"Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue." Yi X., Mroczko M., Manoj K.M., Wang X., Hager L.P. Proc. Natl. Acad. Sci. U.S.A. 96:12412-12417(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-51.
[9]	"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).
[10]	"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: AAA23437.1.
U14003 Genomic DNA. Translation: AAA97053.1.
U00096 Genomic DNA. Translation: AAC77114.1.
AP009048 Genomic DNA. Translation: BAE78158.1.

PIR

RDECFF. A00376.

RefSeq

NP_418578.1. NC_000913.2.
YP_492299.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KF6	X-ray	2.70	A/M	1-602	[»]
1KFY	X-ray	3.60	A/M	1-602	[»]
1L0V	X-ray	3.30	A/M	1-602	[»]
2B76	X-ray	3.30	A/M	1-602	[»]
3CIR	X-ray	3.65	A/M	1-602	[»]
3P4P	X-ray	2.80	A/M	1-577	[»]
3P4Q	X-ray	3.35	A/M	1-577	[»]
3P4R	X-ray	3.05	A/M	1-577	[»]
3P4S	X-ray	3.10	A/M	1-577	[»]

ProteinModelPortal

P00363.

SMR

P00363. Positions 1-577.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9681N.

IntAct

P00363. 14 interactions.

MINT

MINT-1310079.

STRING

511145.b4154.

Proteomic databases

PaxDb

P00363.

PRIDE

P00363.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77114; AAC77114; b4154.
BAE78158; BAE78158; BAE78158.

GeneID

12931889.
948667.

KEGG

ecj:Y75_p4043.
eco:b4154.

PATRIC

32123881. VBIEscCol129921_4288.

Organism-specific databases

EchoBASE

EB0326.

EcoGene

EG10330. frdA.

Phylogenomic databases

eggNOG

COG1053.

HOGENOM

HOG000160475.

K00244.

OMA

RKGNTIP.

ProtClustDB

PRK09231.

Enzyme and pathway databases

BioCyc

EcoCyc:FUM-FLAVO.
ECOL316407:JW4115-MONOMER.
MetaCyc:FUM-FLAVO.

SABIO-RK

P00363.

Gene expression databases

Genevestigator

P00363.

Family and domain databases

Gene3D

1.20.58.100. 1 hit.

InterPro

IPR003953. FAD_bind_dom.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR005884. Fum_red_fp.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]

PANTHER

PTHR11632:SF5. PTHR11632:SF5. 1 hit.

Pfam

PF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

SUPFAM

SSF46977. Succ_DH_flav_C. 1 hit.

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...

Other

ChEMBL

CHEMBL1819.

DrugBank

DB00730. Thiabendazole.

EvolutionaryTrace

P00363.

Entry information

Entry name

FRDA_ECOLI

Accession

Primary (citable) accession number: P00363
Secondary accession number(s): Q2M6E8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 145 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents