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P77544 (YFCF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase YfcF

EC=2.5.1.18
Gene names
Name:yfcF
Ordered Locus Names:b2301, JW2298
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exhibits glutathione (GSH) S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. Ref.4

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.4

Enzyme regulation

GSH transferase activity is inhibited by S-hexyl glutathione. Ref.4

Disruption phenotype

Deletion of yfcF decreases the resistance of the bacteria to hydrogen peroxide. Ref.4

Sequence similarities

Belongs to the GST superfamily.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

kcat is 0.11 sec(-1) for the GSH transferase reaction with CDNB as substrate.

KM=0.24 mM for glutathione Ref.4

KM=1.1 mM for 1-chloro-2,4-dinitrobenzene

pH dependence:

Activity decreases as pH is lowered from neutral to acidic.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 214214Glutathione S-transferase YfcF
PRO_0000186015

Regions

Domain6 – 8782GST N-terminal
Domain95 – 214120GST C-terminal

Experimental info

Mutagenesis101S → A: Nearly no effect on GSH transferase activity. Ref.4
Mutagenesis161S → G: 2% of wild-type GSH transferase activity. Ref.4

Secondary structure

.............................. 214
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P77544 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 6B2308D403DA3077

FASTA21424,326
        10         20         30         40         50         60 
MSKPAITLWS DAHFFSPYVL SAWVALQEKG LSFHIKTIDL DSGEHLQPTW QGYGQTRRVP 

        70         80         90        100        110        120 
LLQIDDFELS ESSAIAEYLE DRFAPPTWER IYPLDLENRA RARQIQAWLR SDLMPIREER 

       130        140        150        160        170        180 
PTDVVFAGAK KAPLTAEGKA SAEKLFAMAE HLLVLGQPNL FGEWCIADTD LALMINRLVL 

       190        200        210 
HGDEVPERLV DYATFQWQRA SVQRFIALSA KQSG 

« Hide

References

« Hide 'large scale' references
[1]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"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.
[4]"Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress."
Kanai T., Takahashi K., Inoue H.
J. Biochem. 140:703-711(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEFENSE AGAINST OXIDATIVE STRESS, GSH TRANSFERASE ACTIVITY, PEROXIDASE ACTIVITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-10 AND SER-16.
Strain: K12.
[5]"Crystal structure of glutathione S-transferase (NP_416804.1) from Escherichia coli K12 at 1.85 A resolution."
Joint center for structural genomics (JCSG)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
Strain: K12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC75361.1.
AP009048 Genomic DNA. Translation: BAA16138.1.
PIRC65002.
RefSeqNP_416804.1. NC_000913.3.
YP_490543.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BBYX-ray1.85A1-214[»]
ProteinModelPortalP77544.
SMRP77544. Positions 3-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP77544. 3 interactions.
STRING511145.b2301.

Proteomic databases

PaxDbP77544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75361; AAC75361; b2301.
BAA16138; BAA16138; BAA16138.
GeneID12931522.
946749.
KEGGecj:Y75_p2267.
eco:b2301.
PATRIC32119973. VBIEscCol129921_2396.

Organism-specific databases

EchoBASEEB3862.
EcoGeneEG14109. yfcF.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000255229.
OMAWSIADTD.
OrthoDBEOG6R5C65.
PhylomeDBP77544.

Enzyme and pathway databases

BioCycEcoCyc:G7193-MONOMER.
ECOL316407:JW2298-MONOMER.
MetaCyc:G7193-MONOMER.

Gene expression databases

GenevestigatorP77544.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP77544.
PROP77544.

Entry information

Entry nameYFCF_ECOLI
AccessionPrimary (citable) accession number: P77544
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 14, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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