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Protein

Fumarate reductase subunit D

Gene

frdD

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

Functioni

Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.

GO - Molecular functioni

  • succinate dehydrogenase (ubiquinone) activity Source: EcoCyc
  • succinate dehydrogenase activity Source: EcoCyc

GO - Biological processi

  • anaerobic respiration Source: EcoCyc
  • fermentation Source: EcoCyc
  • fumarate metabolic process Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:FUM-MEMB2.
ECOL316407:JW4112-MONOMER.
MetaCyc:FUM-MEMB2.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate reductase subunit D
Alternative name(s):
Fumarate reductase 13 kDa hydrophobic protein
Gene namesi
Name:frdD
Ordered Locus Names:b4151, JW4112
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10333. frdD.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88Cytoplasmic1 Publication
Transmembranei9 – 3527HelicalAdd
BLAST
Topological domaini36 – 6025Periplasmic1 PublicationAdd
BLAST
Transmembranei61 – 8929HelicalAdd
BLAST
Topological domaini90 – 967Cytoplasmic1 Publication
Transmembranei97 – 11519HelicalAdd
BLAST
Topological domaini116 – 1194Periplasmic1 Publication

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
  • plasma membrane fumarate reductase complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 119119Fumarate reductase subunit DPRO_0000196542Add
BLAST

Proteomic databases

PaxDbiP0A8Q3.

Expressioni

Inductioni

Regulated at the transcriptional level in response to the cellular availability of the alternate electron acceptors oxygen, nitrate, and fumarate.1 Publication

Interactioni

Subunit structurei

Part of an enzyme complex containing four subunits: a flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic anchor proteins (FrdC and FrdD).

Protein-protein interaction databases

BioGridi4262699. 457 interactions.
DIPiDIP-9684N.
IntActiP0A8Q3. 1 interaction.
STRINGi511145.b4151.

Structurei

Secondary structure

1
119
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2717Combined sources
Helixi29 – 379Combined sources
Helixi40 – 423Combined sources
Turni47 – 504Combined sources
Helixi52 – 598Combined sources
Helixi62 – 8928Combined sources
Helixi97 – 11620Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KF6X-ray2.70D/P1-119[»]
1KFYX-ray3.60D/P1-119[»]
1L0VX-ray3.30D/P1-119[»]
2B76X-ray3.30D/P1-119[»]
3CIRX-ray3.65D/P1-119[»]
3P4PX-ray2.80D/P1-119[»]
3P4QX-ray3.35D/P1-119[»]
3P4RX-ray3.05D/P1-119[»]
3P4SX-ray3.10D/P1-119[»]
4KX6X-ray2.95D/P1-119[»]
ProteinModelPortaliP0A8Q3.
SMRiP0A8Q3. Positions 1-119.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8Q3.

Family & Domainsi

Sequence similaritiesi

Belongs to the FrdD family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108VP9. Bacteria.
COG3080. LUCA.
HOGENOMiHOG000281495.
KOiK00247.
OMAiGMWSAIV.
OrthoDBiEOG6MPWX0.

Family and domain databases

HAMAPiMF_00709. Fumarate_red_D.
InterProiIPR003418. Fumarate_red_D.
[Graphical view]
PfamiPF02313. Fumarate_red_D. 1 hit.
[Graphical view]
PIRSFiPIRSF000179. FrdD. 1 hit.
ProDomiPD015693. Fumarate_red_D. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P0A8Q3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MINPNPKRSD EPVFWGLFGA GGMWSAIIAP VMILLVGILL PLGLFPGDAL
60 70 80 90 100
SYERVLAFAQ SFIGRVFLFL MIVLPLWCGL HRMHHAMHDL KIHVPAGKWV
110
FYGLAAILTV VTLIGVVTI
Length:119
Mass (Da):13,107
Last modified:July 21, 1986 - v1
Checksum:iE9D119342B1D5357
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01611 Genomic DNA. Translation: AAA23440.1.
V00277 Genomic DNA. Translation: CAA23536.1.
U14003 Genomic DNA. Translation: AAA97050.1.
U00096 Genomic DNA. Translation: AAC77111.1.
AP009048 Genomic DNA. Translation: BAE78155.1.
M11979 Genomic DNA. Translation: AAA23434.1.
PIRiA04431. WMEC13.
RefSeqiNP_418575.1. NC_000913.3.
WP_000609663.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77111; AAC77111; b4151.
BAE78155; BAE78155; BAE78155.
GeneIDi948668.
KEGGiecj:JW4112.
eco:b4151.
PATRICi32123875. VBIEscCol129921_4285.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01611 Genomic DNA. Translation: AAA23440.1.
V00277 Genomic DNA. Translation: CAA23536.1.
U14003 Genomic DNA. Translation: AAA97050.1.
U00096 Genomic DNA. Translation: AAC77111.1.
AP009048 Genomic DNA. Translation: BAE78155.1.
M11979 Genomic DNA. Translation: AAA23434.1.
PIRiA04431. WMEC13.
RefSeqiNP_418575.1. NC_000913.3.
WP_000609663.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KF6X-ray2.70D/P1-119[»]
1KFYX-ray3.60D/P1-119[»]
1L0VX-ray3.30D/P1-119[»]
2B76X-ray3.30D/P1-119[»]
3CIRX-ray3.65D/P1-119[»]
3P4PX-ray2.80D/P1-119[»]
3P4QX-ray3.35D/P1-119[»]
3P4RX-ray3.05D/P1-119[»]
3P4SX-ray3.10D/P1-119[»]
4KX6X-ray2.95D/P1-119[»]
ProteinModelPortaliP0A8Q3.
SMRiP0A8Q3. Positions 1-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262699. 457 interactions.
DIPiDIP-9684N.
IntActiP0A8Q3. 1 interaction.
STRINGi511145.b4151.

Proteomic databases

PaxDbiP0A8Q3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77111; AAC77111; b4151.
BAE78155; BAE78155; BAE78155.
GeneIDi948668.
KEGGiecj:JW4112.
eco:b4151.
PATRICi32123875. VBIEscCol129921_4285.

Organism-specific databases

EchoBASEiEB0329.
EcoGeneiEG10333. frdD.

Phylogenomic databases

eggNOGiENOG4108VP9. Bacteria.
COG3080. LUCA.
HOGENOMiHOG000281495.
KOiK00247.
OMAiGMWSAIV.
OrthoDBiEOG6MPWX0.

Enzyme and pathway databases

BioCyciEcoCyc:FUM-MEMB2.
ECOL316407:JW4112-MONOMER.
MetaCyc:FUM-MEMB2.

Miscellaneous databases

EvolutionaryTraceiP0A8Q3.
PROiP0A8Q3.

Family and domain databases

HAMAPiMF_00709. Fumarate_red_D.
InterProiIPR003418. Fumarate_red_D.
[Graphical view]
PfamiPF02313. Fumarate_red_D. 1 hit.
[Graphical view]
PIRSFiPIRSF000179. FrdD. 1 hit.
ProDomiPD015693. Fumarate_red_D. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Overlap between ampC and frd operons on the Escherichia coli chromosome."
    Grundstroem T., Jaurin B.
    Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(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. "ampC beta-lactamase hyperproduction in Escherichia coli: natural ampicillin resistance generated by horizontal chromosomal DNA transfer from Shigella."
    Olsson O., Bergstroem S., Lindberg F.P., Normark S.
    Proc. Natl. Acad. Sci. U.S.A. 80:7556-7560(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-119.
  6. "Transcription of the Escherichia coli fumarate reductase genes (frdABCD) and their coordinate regulation by oxygen, nitrate, and fumarate."
    Jones H.M., Gunsalus R.P.
    J. Bacteriol. 164:1100-1109(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-119, INDUCTION.
  7. "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-50.
  8. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  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).

Entry informationi

Entry nameiFRDD_ECOLI
AccessioniPrimary (citable) accession number: P0A8Q3
Secondary accession number(s): P03806, Q2M6F1, Q47048
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 20, 2016
This is version 85 of the entry and version 1 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.