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Protein

Fumarate reductase iron-sulfur subunit

Gene

frdB

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.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi58Iron-sulfur 1 (2Fe-2S)1
Metal bindingi63Iron-sulfur 1 (2Fe-2S)1
Metal bindingi66Iron-sulfur 1 (2Fe-2S)1
Metal bindingi78Iron-sulfur 1 (2Fe-2S)1
Metal bindingi149Iron-sulfur 2 (4Fe-4S)1
Metal bindingi152Iron-sulfur 2 (4Fe-4S)1
Metal bindingi155Iron-sulfur 2 (4Fe-4S)1
Metal bindingi159Iron-sulfur 3 (3Fe-4S)1
Metal bindingi205Iron-sulfur 3 (3Fe-4S)1
Metal bindingi211Iron-sulfur 3 (3Fe-4S)1
Metal bindingi215Iron-sulfur 2 (4Fe-4S)1

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: EcoCyc
  • 3 iron, 4 sulfur cluster binding Source: EcoCyc
  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • electron carrier activity Source: EcoCyc
  • iron-sulfur cluster binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
  • 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
  • fermentation Source: EcoCyc
  • tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:FUM-FE-S.
ECOL316407:JW4114-MONOMER.
MetaCyc:FUM-FE-S.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate reductase iron-sulfur subunit (EC:1.3.5.1)
Gene namesi
Name:frdB
Ordered Locus Names:b4153, JW4114
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10331. frdB.

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
Mutagenesisi58C → S: Affects center 1 (2Fe-2S). 1 Publication1
Mutagenesisi63C → S: Affects center 1 (2Fe-2S). 1 Publication1
Mutagenesisi66C → S: Affects center 1 (2Fe-2S). 1 Publication1
Mutagenesisi78C → S: Affects center 1 (2Fe-2S). 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001586982 – 244Fumarate reductase iron-sulfur subunitAdd BLAST243

Proteomic databases

PaxDbiP0AC47.
PRIDEiP0AC47.

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
frdAP003634EBI-906724,EBI-550480
mutTP083374EBI-906724,EBI-1121389
ompWP0A9152EBI-906724,EBI-1132929

Protein-protein interaction databases

BioGridi4262701. 382 interactors.
DIPiDIP-9682N.
IntActiP0AC47. 7 interactors.
STRINGi511145.b4153.

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 13Combined sources9
Turni16 – 18Combined sources3
Beta strandi23 – 31Combined sources9
Helixi37 – 47Combined sources11
Beta strandi59 – 63Combined sources5
Beta strandi67 – 70Combined sources4
Beta strandi73 – 76Combined sources4
Helixi77 – 79Combined sources3
Helixi82 – 84Combined sources3
Beta strandi89 – 93Combined sources5
Beta strandi99 – 101Combined sources3
Helixi108 – 116Combined sources9
Helixi128 – 130Combined sources3
Helixi137 – 141Combined sources5
Helixi144 – 147Combined sources4
Helixi154 – 158Combined sources5
Helixi160 – 164Combined sources5
Beta strandi166 – 168Combined sources3
Helixi171 – 181Combined sources11
Helixi190 – 197Combined sources8
Turni199 – 201Combined sources3
Helixi202 – 204Combined sources3
Helixi210 – 214Combined sources5
Helixi221 – 240Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KF6X-ray2.70B/N2-244[»]
1KFYX-ray3.60B/N2-244[»]
1L0VX-ray3.30B/N2-244[»]
2B76X-ray3.30B/N2-244[»]
3CIRX-ray3.65B/N2-244[»]
3P4PX-ray2.80B/N2-244[»]
3P4QX-ray3.35B/N2-244[»]
3P4RX-ray3.05B/N2-244[»]
3P4SX-ray3.10B/N2-244[»]
ProteinModelPortaliP0AC47.
SMRiP0AC47.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC47.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 972Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST82
Domaini140 – 1694Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd BLAST30

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105E33. Bacteria.
COG0479. LUCA.
HOGENOMiHOG000160590.
InParanoidiP0AC47.
KOiK00245.
OMAiFKNFFGS.
PhylomeDBiP0AC47.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamiPF13085. Fer2_3. 1 hit.
PF13183. Fer4_8. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 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]

Sequencei

Sequence statusi: Complete.

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

P0AC47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP
60 70 80 90 100
DLSYRWSCRM AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE
110 120 130 140 150
RDLVVDMTHF IESLEAIKPY IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI
160 170 180 190 200
NCGLCYAACP QFGLNPEFIG PAAITLAHRY NEDSRDHGKK ERMAQLNSQN
210 220 230 240
GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT LKPR
Length:244
Mass (Da):27,123
Last modified:January 23, 2007 - v2
Checksum:iAC1D7A73244D7AC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01611 Genomic DNA. Translation: AAA23438.1.
U14003 Genomic DNA. Translation: AAA97052.1.
U00096 Genomic DNA. Translation: AAC77113.1.
AP009048 Genomic DNA. Translation: BAE78157.1.
V00277 Genomic DNA. Translation: CAA23534.1.
PIRiA00377. RDECFS.
RefSeqiNP_418577.1. NC_000913.3.
WP_000829498.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77113; AAC77113; b4153.
BAE78157; BAE78157; BAE78157.
GeneIDi948666.
KEGGiecj:JW4114.
eco:b4153.
PATRICi32123879. VBIEscCol129921_4287.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01611 Genomic DNA. Translation: AAA23438.1.
U14003 Genomic DNA. Translation: AAA97052.1.
U00096 Genomic DNA. Translation: AAC77113.1.
AP009048 Genomic DNA. Translation: BAE78157.1.
V00277 Genomic DNA. Translation: CAA23534.1.
PIRiA00377. RDECFS.
RefSeqiNP_418577.1. NC_000913.3.
WP_000829498.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KF6X-ray2.70B/N2-244[»]
1KFYX-ray3.60B/N2-244[»]
1L0VX-ray3.30B/N2-244[»]
2B76X-ray3.30B/N2-244[»]
3CIRX-ray3.65B/N2-244[»]
3P4PX-ray2.80B/N2-244[»]
3P4QX-ray3.35B/N2-244[»]
3P4RX-ray3.05B/N2-244[»]
3P4SX-ray3.10B/N2-244[»]
ProteinModelPortaliP0AC47.
SMRiP0AC47.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262701. 382 interactors.
DIPiDIP-9682N.
IntActiP0AC47. 7 interactors.
STRINGi511145.b4153.

Proteomic databases

PaxDbiP0AC47.
PRIDEiP0AC47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77113; AAC77113; b4153.
BAE78157; BAE78157; BAE78157.
GeneIDi948666.
KEGGiecj:JW4114.
eco:b4153.
PATRICi32123879. VBIEscCol129921_4287.

Organism-specific databases

EchoBASEiEB0327.
EcoGeneiEG10331. frdB.

Phylogenomic databases

eggNOGiENOG4105E33. Bacteria.
COG0479. LUCA.
HOGENOMiHOG000160590.
InParanoidiP0AC47.
KOiK00245.
OMAiFKNFFGS.
PhylomeDBiP0AC47.

Enzyme and pathway databases

BioCyciEcoCyc:FUM-FE-S.
ECOL316407:JW4114-MONOMER.
MetaCyc:FUM-FE-S.

Miscellaneous databases

EvolutionaryTraceiP0AC47.
PROiP0AC47.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamiPF13085. Fer2_3. 1 hit.
PF13183. Fer4_8. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiFRDB_ECOLI
AccessioniPrimary (citable) accession number: P0AC47
Secondary accession number(s): P00364, Q2M6E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 99 of the entry and version 2 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.