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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)DescriptionActionsGraphical viewLength
Active sitei2331
Active sitei2491

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi9 – 23FADSequence analysisAdd BLAST15

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi45H → R: Inactivates enzyme. 1 Publication1
Mutagenesisi45H → S, C or Y: Decreased ability (greater than 70%) to reduce fumarate. 1 Publication1
Mutagenesisi233H → S: Severely affect succinate oxidation and decrease fumarate oxidation by 75%. 1 Publication1
Mutagenesisi248C → S or A: Does not inactivate enzyme. 1 Publication1
Mutagenesisi249R → H or L: Inactivates enzyme. 1 Publication1

Chemistry databases

DrugBankiDB00730. Thiabendazole.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001586602 – 602Fumarate reductase flavoprotein subunitAdd BLAST601

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei45Tele-8alpha-FAD histidine1

Proteomic databases

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 interactors.
DIPiDIP-9681N.
IntActiP00363. 14 interactors.
MINTiMINT-1310079.
STRINGi511145.b4154.

Structurei

Secondary structure

1602
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 5Combined sources4
Beta strandi7 – 11Combined sources5
Helixi15 – 27Combined sources13
Beta strandi33 – 39Combined sources7
Helixi41 – 43Combined sources3
Helixi45 – 48Combined sources4
Beta strandi58 – 60Combined sources3
Helixi63 – 73Combined sources11
Turni74 – 76Combined sources3
Helixi80 – 99Combined sources20
Beta strandi110 – 112Combined sources3
Beta strandi128 – 130Combined sources3
Helixi132 – 144Combined sources13
Beta strandi150 – 154Combined sources5
Beta strandi156 – 164Combined sources9
Beta strandi167 – 175Combined sources9
Turni176 – 179Combined sources4
Beta strandi180 – 185Combined sources6
Beta strandi189 – 191Combined sources3
Helixi197 – 199Combined sources3
Beta strandi200 – 205Combined sources6
Helixi212 – 218Combined sources7
Turni219 – 221Combined sources3
Beta strandi224 – 226Combined sources3
Beta strandi230 – 236Combined sources7
Turni238 – 240Combined sources3
Helixi247 – 250Combined sources4
Beta strandi254 – 256Combined sources3
Helixi263 – 266Combined sources4
Turni267 – 269Combined sources3
Helixi283 – 285Combined sources3
Helixi288 – 301Combined sources14
Beta strandi304 – 306Combined sources3
Beta strandi312 – 316Combined sources5
Helixi318 – 320Combined sources3
Helixi322 – 328Combined sources7
Helixi330 – 340Combined sources11
Turni344 – 346Combined sources3
Beta strandi349 – 358Combined sources10
Beta strandi361 – 363Combined sources3
Beta strandi371 – 373Combined sources3
Beta strandi375 – 377Combined sources3
Helixi379 – 381Combined sources3
Beta strandi385 – 387Combined sources3
Helixi395 – 416Combined sources22
Helixi423 – 442Combined sources20
Helixi449 – 463Combined sources15
Beta strandi464 – 468Combined sources5
Helixi470 – 487Combined sources18
Beta strandi497 – 499Combined sources3
Helixi501 – 525Combined sources25
Beta strandi533 – 535Combined sources3
Turni545 – 547Combined sources3
Beta strandi550 – 556Combined sources7
Beta strandi562 – 568Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00363.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C00. Bacteria.
COG1053. LUCA.
HOGENOMiHOG000160475.
InParanoidiP00363.
KOiK00244.
OMAiAAPSIIH.
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)DescriptionActionsGraphical viewLength
Sequence conflicti386L → P in AAA23437 (PubMed:7037404).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

DrugBankiDB00730. Thiabendazole.

Proteomic databases

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.
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...

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: November 2, 2016
This is version 173 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.