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P77526

- YFCG_ECOLI

UniProt

P77526 - YFCG_ECOLI

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Protein

Disulfide-bond oxidoreductase YfcG

Gene

yfcG

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

Functioni

Exhibits a very robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H2O2, tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the nucleophilic substrate. Is involved in defense against oxidative stress, probably via its peroxidase activity.2 Publications

Kineticsi

kcat is 180 sec(-1) for the disulfide-bond reductase reaction toward 2-hydroxyethyl disulfide. kcat is 0.27 sec(-1) for the hydroperoxidase reaction with cumene hydroperoxide. kcat is 0.1 sec(-1) for the GSH transferase reaction with chloro-2,4-dinitrobenzene (CDNB) as substrate.

  1. KM=1.6 mM for glutathione (when assaying the disulfide-bond reductase activity with 2-hydroxyethyl disulfide)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111Glutathione 1
Binding sitei38 – 381Glutathione 1
Binding sitei52 – 521Glutathione 1; via amide nitrogen and carbonyl oxygen
Binding sitei132 – 1321Glutathione 2

GO - Molecular functioni

  1. disulfide oxidoreductase activity Source: EcoCyc
  2. peroxidase activity Source: UniProtKB-KW

GO - Biological processi

  1. response to oxidative stress Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciEcoCyc:G7194-MONOMER.
ECOL316407:JW2299-MONOMER.
MetaCyc:G7194-MONOMER.
RETL1328306-WGS:GSTH-836-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Disulfide-bond oxidoreductase YfcG (EC:1.8.4.-)
Alternative name(s):
GSH-dependent disulfide-bond oxidoreductase YfcG
GST N1-1
GST-like protein YfcG
Organic hydroperoxidase (EC:1.11.1.-)
Gene namesi
Name:yfcG
Ordered Locus Names:b2302, JW2299
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG14110. yfcG.

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91T → A: No effect on GSH transferase activity. 1 Publication
Mutagenesisi11 – 111N → A: Loss of GSH transferase activity. 1 Publication
Mutagenesisi14 – 141K → A: 10-fold reduction in GSH transferase activity. 1 Publication
Mutagenesisi166 – 1661C → A: No effect on disulfide-bond reductase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Disulfide-bond oxidoreductase YfcGPRO_0000186016Add
BLAST

Proteomic databases

PaxDbiP77526.
PRIDEiP77526.

Expressioni

Gene expression databases

GenevestigatoriP77526.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP77526. 2 interactions.
STRINGi511145.b2302.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi10 – 2213Combined sources
Beta strandi26 – 305Combined sources
Turni33 – 364Combined sources
Helixi37 – 393Combined sources
Helixi41 – 444Combined sources
Beta strandi54 – 596Combined sources
Beta strandi67 – 715Combined sources
Helixi72 – 8312Combined sources
Helixi91 – 10616Combined sources
Helixi108 – 12013Combined sources
Helixi127 – 15024Combined sources
Beta strandi156 – 1583Combined sources
Helixi161 – 17010Combined sources
Helixi171 – 1766Combined sources
Helixi180 – 1823Combined sources
Helixi184 – 19411Combined sources
Helixi197 – 2037Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GX0X-ray2.30A1-215[»]
ProteinModelPortaliP77526.
SMRiP77526. Positions 1-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77526.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8787GST N-terminalAdd
BLAST
Domaini90 – 215126GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni71 – 722Glutathione 1 binding

Sequence similaritiesi

Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125752.
InParanoidiP77526.
KOiK00799.
OMAiTYPWVVS.
OrthoDBiEOG6677PW.
PhylomeDBiP77526.

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.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF13417. 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.

P77526-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIDLYFAPTP NGHKITLFLE EAELDYRLIK VDLGKGGQFR PEFLRISPNN
60 70 80 90 100
KIPAIVDHSP ADGGEPLSLF ESGAILLYLA EKTGLFLSHE TRERAATLQW
110 120 130 140 150
LFWQVGGLGP MLGQNHHFNH AAPQTIPYAI ERYQVETQRL YHVLNKRLEN
160 170 180 190 200
SPWLGGENYS IADIACWPWV NAWTRQRIDL AMYPAVKNWH ERIRSRPATG
210
QALLKAQLGD ERSDS
Length:215
Mass (Da):24,516
Last modified:February 1, 1997 - v1
Checksum:i058CEBAC879A3050
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75362.1.
AP009048 Genomic DNA. Translation: BAA16139.1.
PIRiD65002.
RefSeqiNP_416805.1. NC_000913.3.
YP_490544.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75362; AAC75362; b2302.
BAA16139; BAA16139; BAA16139.
GeneIDi12931523.
946763.
KEGGiecj:Y75_p2268.
eco:b2302.
PATRICi32119975. VBIEscCol129921_2397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75362.1 .
AP009048 Genomic DNA. Translation: BAA16139.1 .
PIRi D65002.
RefSeqi NP_416805.1. NC_000913.3.
YP_490544.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GX0 X-ray 2.30 A 1-215 [» ]
ProteinModelPortali P77526.
SMRi P77526. Positions 1-204.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P77526. 2 interactions.
STRINGi 511145.b2302.

Proteomic databases

PaxDbi P77526.
PRIDEi P77526.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75362 ; AAC75362 ; b2302 .
BAA16139 ; BAA16139 ; BAA16139 .
GeneIDi 12931523.
946763.
KEGGi ecj:Y75_p2268.
eco:b2302.
PATRICi 32119975. VBIEscCol129921_2397.

Organism-specific databases

EchoBASEi EB3863.
EcoGenei EG14110. yfcG.

Phylogenomic databases

eggNOGi COG0625.
HOGENOMi HOG000125752.
InParanoidi P77526.
KOi K00799.
OMAi TYPWVVS.
OrthoDBi EOG6677PW.
PhylomeDBi P77526.

Enzyme and pathway databases

BioCyci EcoCyc:G7194-MONOMER.
ECOL316407:JW2299-MONOMER.
MetaCyc:G7194-MONOMER.
RETL1328306-WGS:GSTH-836-MONOMER.

Miscellaneous databases

EvolutionaryTracei P77526.
PROi P77526.

Gene expression databases

Genevestigatori P77526.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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, DISRUPTION PHENOTYPE, MUTAGENESIS OF THR-9; ASN-11 AND LYS-14.
    Strain: K12.
  5. "Structure and function of YghU, a nu-class glutathione transferase related to YfcG from Escherichia coli."
    Stourman N.V., Branch M.C., Schaab M.R., Harp J.M., Ladner J.E., Armstrong R.N.
    Biochemistry 50:1274-1281(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FAMILY NAME.
    Strain: K12.
  6. "Analysis of the structure and function of YfcG from Escherichia coli reveals an efficient and unique disulfide bond reductase."
    Wadington M.C., Ladner J.E., Stourman N.V., Harp J.M., Armstrong R.N.
    Biochemistry 48:6559-6561(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE DISULFIDE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, SUBUNIT, MUTAGENESIS OF CYS-166.
    Strain: K12.

Entry informationi

Entry nameiYFCG_ECOLI
AccessioniPrimary (citable) accession number: P77526
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 26, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reductase activity of YfcG is unique in that no sulfhydryl groups in the protein appear to be covalently involved in the redox chemistry.1 Publication
Glutathionylspermidine (GspSH) binds YfcG about 10 times more tightly than GSH. Moreover, GSSG binds 100 times more tightly than GSH and 10 times more tightly than the GSH analog, GSO3- (PubMed:19537707).1 Publication

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