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Protein

Fumarate reductase flavoprotein subunit

Gene

frdA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Succinate + a quinone = fumarate + a quinol.1 Publication

Cofactori

FADNote: Binds 1 FAD covalently per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei233 – 2331
Active sitei249 – 2491

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 2315FADSequence analysisAdd
BLAST

GO - Molecular functioni

  • electron carrier activity Source: EcoCyc
  • FAD binding Source: EcoCyc
  • succinate dehydrogenase activity Source: EcoCyc

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • bacterial-type flagellum assembly Source: EcoCyc
  • bacterial-type flagellum-dependent cell motility Source: EcoCyc
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • electron transport chain Source: InterPro
  • fermentation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciEcoCyc:FUM-FLAVO.
ECOL316407:JW4115-MONOMER.
MetaCyc:FUM-FLAVO.
BRENDAi1.3.5.4. 2026.
SABIO-RKP00363.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate reductase flavoprotein subunit (EC:1.3.5.4)
Gene namesi
Name:frdA
Ordered Locus Names:b4154, JW4115
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10330. frdA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB
  • plasma membrane fumarate reductase complex Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451H → R: Inactivates enzyme. 1 Publication
Mutagenesisi45 – 451H → S, C or Y: Decreased ability (greater than 70%) to reduce fumarate. 1 Publication
Mutagenesisi233 – 2331H → S: Severely affect succinate oxidation and decrease fumarate oxidation by 75%. 1 Publication
Mutagenesisi248 – 2481C → S or A: Does not inactivate enzyme. 1 Publication
Mutagenesisi249 – 2491R → H or L: Inactivates enzyme. 1 Publication

Chemistry

DrugBankiDB00730. Thiabendazole.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 602601Fumarate reductase flavoprotein subunitPRO_0000158660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451Tele-8alpha-FAD histidine

Proteomic databases

EPDiP00363.
PaxDbiP00363.
PRIDEiP00363.

Interactioni

Subunit structurei

Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins.

Binary interactionsi

WithEntry#Exp.IntActNotes
frdBP0AC474EBI-550480,EBI-906724

Protein-protein interaction databases

BioGridi4260883. 163 interactions.
DIPiDIP-9681N.
IntActiP00363. 14 interactions.
MINTiMINT-1310079.
STRINGi511145.b4154.

Structurei

Secondary structure

1
602
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi7 – 115Combined sources
Helixi15 – 2713Combined sources
Beta strandi33 – 397Combined sources
Helixi41 – 433Combined sources
Helixi45 – 484Combined sources
Beta strandi58 – 603Combined sources
Helixi63 – 7311Combined sources
Turni74 – 763Combined sources
Helixi80 – 9920Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi128 – 1303Combined sources
Helixi132 – 14413Combined sources
Beta strandi150 – 1545Combined sources
Beta strandi156 – 1649Combined sources
Beta strandi167 – 1759Combined sources
Turni176 – 1794Combined sources
Beta strandi180 – 1856Combined sources
Beta strandi189 – 1913Combined sources
Helixi197 – 1993Combined sources
Beta strandi200 – 2056Combined sources
Helixi212 – 2187Combined sources
Turni219 – 2213Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi230 – 2367Combined sources
Turni238 – 2403Combined sources
Helixi247 – 2504Combined sources
Beta strandi254 – 2563Combined sources
Helixi263 – 2664Combined sources
Turni267 – 2693Combined sources
Helixi283 – 2853Combined sources
Helixi288 – 30114Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi312 – 3165Combined sources
Helixi318 – 3203Combined sources
Helixi322 – 3287Combined sources
Helixi330 – 34011Combined sources
Turni344 – 3463Combined sources
Beta strandi349 – 35810Combined sources
Beta strandi361 – 3633Combined sources
Beta strandi371 – 3733Combined sources
Beta strandi375 – 3773Combined sources
Helixi379 – 3813Combined sources
Beta strandi385 – 3873Combined sources
Helixi395 – 41622Combined sources
Helixi423 – 44220Combined sources
Helixi449 – 46315Combined sources
Beta strandi464 – 4685Combined sources
Helixi470 – 48718Combined sources
Beta strandi497 – 4993Combined sources
Helixi501 – 52525Combined sources
Beta strandi533 – 5353Combined sources
Turni545 – 5473Combined sources
Beta strandi550 – 5567Combined sources
Beta strandi562 – 5687Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KF6X-ray2.70A/M1-602[»]
1KFYX-ray3.60A/M1-602[»]
1L0VX-ray3.30A/M1-602[»]
2B76X-ray3.30A/M1-602[»]
3CIRX-ray3.65A/M1-602[»]
3P4PX-ray2.80A/M1-577[»]
3P4QX-ray3.35A/M1-577[»]
3P4RX-ray3.05A/M1-577[»]
3P4SX-ray3.10A/M1-577[»]
4KX6X-ray2.95A/M1-577[»]
ProteinModelPortaliP00363.
SMRiP00363. Positions 1-577.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00363.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C00. Bacteria.
COG1053. LUCA.
HOGENOMiHOG000160475.
InParanoidiP00363.
KOiK00244.
OMAiAAPSIIH.
OrthoDBiEOG6M3PC4.
PhylomeDBiP00363.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.50.50.60. 2 hits.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD-binding_2.
IPR023753. FAD/NAD-binding_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR005884. Fum_red_fp.
IPR030664. SdhA/FrdA/AprA.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000171. SDHA_APRA_LASPO. 1 hit.
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF51905. SSF51905. 2 hits.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01176. fum_red_Fp. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00363-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTFQADLAI VGAGGAGLRA AIAAAQANPN AKIALISKVY PMRSHTVAAE
60 70 80 90 100
GGSAAVAQDH DSFEYHFHDT VAGGDWLCEQ DVVDYFVHHC PTEMTQLELW
110 120 130 140 150
GCPWSRRPDG SVNVRRFGGM KIERTWFAAD KTGFHMLHTL FQTSLQFPQI
160 170 180 190 200
QRFDEHFVLD ILVDDGHVRG LVAMNMMEGT LVQIRANAVV MATGGAGRVY
210 220 230 240 250
RYNTNGGIVT GDGMGMALSH GVPLRDMEFV QYHPTGLPGS GILMTEGCRG
260 270 280 290 300
EGGILVNKNG YRYLQDYGMG PETPLGEPKN KYMELGPRDK VSQAFWHEWR
310 320 330 340 350
KGNTISTPRG DVVYLDLRHL GEKKLHERLP FICELAKAYV GVDPVKEPIP
360 370 380 390 400
VRPTAHYTMG GIETDQNCET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL
410 420 430 440 450
VVFGRLAGEQ ATERAATAGN GNEAAIEAQA AGVEQRLKDL VNQDGGENWA
460 470 480 490 500
KIRDEMGLAM EEGCGIYRTP ELMQKTIDKL AELQERFKRV RITDTSSVFN
510 520 530 540 550
TDLLYTIELG HGLNVAECMA HSAMARKESR GAHQRLDEGC TERDDVNFLK
560 570 580 590 600
HTLAFRDADG TTRLEYSDVK ITTLPPAKRV YGGEADAADK AEAANKKEKA

NG
Length:602
Mass (Da):65,972
Last modified:January 23, 2007 - v3
Checksum:i3306D7FF6E198AE9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti386 – 3861L → P in AAA23437 (PubMed:7037404).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01611 Genomic DNA. Translation: AAA23437.1.
U14003 Genomic DNA. Translation: AAA97053.1.
U00096 Genomic DNA. Translation: AAC77114.1.
AP009048 Genomic DNA. Translation: BAE78158.1.
PIRiA00376. RDECFF.
RefSeqiNP_418578.1. NC_000913.3.
WP_001192973.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77114; AAC77114; b4154.
BAE78158; BAE78158; BAE78158.
GeneIDi948667.
KEGGiecj:JW4115.
eco:b4154.
PATRICi32123881. VBIEscCol129921_4288.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01611 Genomic DNA. Translation: AAA23437.1.
U14003 Genomic DNA. Translation: AAA97053.1.
U00096 Genomic DNA. Translation: AAC77114.1.
AP009048 Genomic DNA. Translation: BAE78158.1.
PIRiA00376. RDECFF.
RefSeqiNP_418578.1. NC_000913.3.
WP_001192973.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KF6X-ray2.70A/M1-602[»]
1KFYX-ray3.60A/M1-602[»]
1L0VX-ray3.30A/M1-602[»]
2B76X-ray3.30A/M1-602[»]
3CIRX-ray3.65A/M1-602[»]
3P4PX-ray2.80A/M1-577[»]
3P4QX-ray3.35A/M1-577[»]
3P4RX-ray3.05A/M1-577[»]
3P4SX-ray3.10A/M1-577[»]
4KX6X-ray2.95A/M1-577[»]
ProteinModelPortaliP00363.
SMRiP00363. Positions 1-577.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260883. 163 interactions.
DIPiDIP-9681N.
IntActiP00363. 14 interactions.
MINTiMINT-1310079.
STRINGi511145.b4154.

Chemistry

DrugBankiDB00730. Thiabendazole.

Proteomic databases

EPDiP00363.
PaxDbiP00363.
PRIDEiP00363.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77114; AAC77114; b4154.
BAE78158; BAE78158; BAE78158.
GeneIDi948667.
KEGGiecj:JW4115.
eco:b4154.
PATRICi32123881. VBIEscCol129921_4288.

Organism-specific databases

EchoBASEiEB0326.
EcoGeneiEG10330. frdA.

Phylogenomic databases

eggNOGiENOG4105C00. Bacteria.
COG1053. LUCA.
HOGENOMiHOG000160475.
InParanoidiP00363.
KOiK00244.
OMAiAAPSIIH.
OrthoDBiEOG6M3PC4.
PhylomeDBiP00363.

Enzyme and pathway databases

BioCyciEcoCyc:FUM-FLAVO.
ECOL316407:JW4115-MONOMER.
MetaCyc:FUM-FLAVO.
BRENDAi1.3.5.4. 2026.
SABIO-RKP00363.

Miscellaneous databases

EvolutionaryTraceiP00363.
PROiP00363.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.50.50.60. 2 hits.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD-binding_2.
IPR023753. FAD/NAD-binding_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR005884. Fum_red_fp.
IPR030664. SdhA/FrdA/AprA.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000171. SDHA_APRA_LASPO. 1 hit.
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF51905. SSF51905. 2 hits.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01176. fum_red_Fp. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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), CATALYTIC ACTIVITY.

Entry informationi

Entry nameiFRDA_ECOLI
AccessioniPrimary (citable) accession number: P00363
Secondary accession number(s): Q2M6E8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.