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Protein

Glutathione S-transferase YfcF

Gene

yfcF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Enzyme regulationi

GSH transferase activity is inhibited by S-hexyl glutathione.1 Publication

Kineticsi

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

  1. KM=0.24 mM for glutathione1 Publication
  2. KM=1.1 mM for 1-chloro-2,4-dinitrobenzene1 Publication

pH dependencei

Activity decreases as pH is lowered from neutral to acidic.1 Publication

GO - Molecular functioni

  1. glutathione transferase activity Source: EcoCyc
  2. peroxidase activity Source: UniProtKB-KW

GO - Biological processi

  1. response to hydrogen peroxide Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase, Transferase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase YfcF (EC:2.5.1.18)
Gene namesi
Name:yfcF
Ordered Locus Names:b2301, JW2298
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG14109. yfcF.

Pathology & Biotechi

Disruption phenotypei

Deletion of yfcF decreases the resistance of the bacteria to hydrogen peroxide.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101S → A: Nearly no effect on GSH transferase activity. 1 Publication
Mutagenesisi16 – 161S → G: 2% of wild-type GSH transferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 214214Glutathione S-transferase YfcFPRO_0000186015Add
BLAST

Proteomic databases

PaxDbiP77544.

Expressioni

Gene expression databases

GenevestigatoriP77544.

Interactioni

Protein-protein interaction databases

IntActiP77544. 3 interactions.
STRINGi511145.b2301.

Structurei

Secondary structure

1
214
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116Combined sources
Helixi17 – 2913Combined sources
Beta strandi34 – 385Combined sources
Beta strandi61 – 644Combined sources
Beta strandi67 – 715Combined sources
Helixi72 – 8211Combined sources
Turni85 – 873Combined sources
Helixi96 – 11116Combined sources
Helixi114 – 1196Combined sources
Helixi123 – 1264Combined sources
Helixi136 – 15217Combined sources
Turni153 – 1553Combined sources
Helixi166 – 17914Combined sources
Turni180 – 1823Combined sources
Helixi187 – 19711Combined sources
Helixi200 – 21011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BBYX-ray1.85A1-214[»]
ProteinModelPortaliP77544.
SMRiP77544. Positions 3-211.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77544.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 8782GST N-terminalAdd
BLAST
Domaini95 – 214120GST C-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the GST superfamily.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000255229.
InParanoidiP77544.
OMAiFSPYVMS.
OrthoDBiEOG6R5C65.
PhylomeDBiP77544.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77544-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKPAITLWS DAHFFSPYVL SAWVALQEKG LSFHIKTIDL DSGEHLQPTW
60 70 80 90 100
QGYGQTRRVP LLQIDDFELS ESSAIAEYLE DRFAPPTWER IYPLDLENRA
110 120 130 140 150
RARQIQAWLR SDLMPIREER PTDVVFAGAK KAPLTAEGKA SAEKLFAMAE
160 170 180 190 200
HLLVLGQPNL FGEWCIADTD LALMINRLVL HGDEVPERLV DYATFQWQRA
210
SVQRFIALSA KQSG
Length:214
Mass (Da):24,326
Last modified:February 1, 1997 - v1
Checksum:i6B2308D403DA3077
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75361.1.
AP009048 Genomic DNA. Translation: BAA16138.1.
PIRiC65002.
RefSeqiNP_416804.1. NC_000913.3.
YP_490543.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75361; AAC75361; b2301.
BAA16138; BAA16138; BAA16138.
GeneIDi12931522.
946749.
KEGGiecj:Y75_p2267.
eco:b2301.
PATRICi32119973. VBIEscCol129921_2396.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75361.1.
AP009048 Genomic DNA. Translation: BAA16138.1.
PIRiC65002.
RefSeqiNP_416804.1. NC_000913.3.
YP_490543.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BBYX-ray1.85A1-214[»]
ProteinModelPortaliP77544.
SMRiP77544. Positions 3-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP77544. 3 interactions.
STRINGi511145.b2301.

Proteomic databases

PaxDbiP77544.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75361; AAC75361; b2301.
BAA16138; BAA16138; BAA16138.
GeneIDi12931522.
946749.
KEGGiecj:Y75_p2267.
eco:b2301.
PATRICi32119973. VBIEscCol129921_2396.

Organism-specific databases

EchoBASEiEB3862.
EcoGeneiEG14109. yfcF.

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000255229.
InParanoidiP77544.
OMAiFSPYVMS.
OrthoDBiEOG6R5C65.
PhylomeDBiP77544.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP77544.
PROiP77544.

Gene expression databases

GenevestigatoriP77544.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiYFCF_ECOLI
AccessioniPrimary (citable) accession number: P77544
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 7, 2015
This is version 100 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

External Data

Dasty 3

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 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.