Disulfide-bond oxidoreductase YfcG - Escherichia coli (strain K12)

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P77526 (YFCG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	yfcG
Ordered Locus Names:	b2302, JW2299

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4 Ref.6
Subunit structure	Homodimer Probable. Ref.6
Disruption phenotype	Deletion of yfcG decreases the resistance of the bacteria to hydrogen peroxide. Ref.4
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 (Ref.6). 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- (Ref.6).
Sequence similarities	Belongs to the GST superfamily. Nu-class GSH transferase family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.
Biophysicochemical properties	Kinetic parameters: 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. K_M=1.6 mM for glutathione (when assaying the disulfide-bond reductase activity with 2-hydroxyethyl disulfide) Ref.6

Ontologies

Keywords
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to oxidative stress Inferred from mutant phenotype Ref.4. Source: EcoCyc
Molecular_function	disulfide oxidoreductase activity Inferred from direct assay Ref.6. Source: EcoCyc peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 215

215

Disulfide-bond oxidoreductase YfcG

PRO_0000186016

Regions

Domain

1 – 87

GST N-terminal

Domain

90 – 215

126

GST C-terminal

Region

71 – 72

Glutathione 1 binding

Sites

Binding site

Glutathione 1

Binding site

Glutathione 1

Binding site

Glutathione 1; via amide nitrogen and carbonyl oxygen

Binding site

132

Glutathione 2

Experimental info

Mutagenesis

T → A: No effect on GSH transferase activity. Ref.4

Mutagenesis

N → A: Loss of GSH transferase activity. Ref.4

Mutagenesis

K → A: 10-fold reduction in GSH transferase activity. Ref.4

Mutagenesis

166

C → A: No effect on disulfide-bond reductase activity. Ref.6

Secondary structure

215

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P77526 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 058CEBAC879A3050
Show »

FASTA

215

24,516

        10         20         30         40         50         60 
MIDLYFAPTP NGHKITLFLE EAELDYRLIK VDLGKGGQFR PEFLRISPNN KIPAIVDHSP 

        70         80         90        100        110        120 
ADGGEPLSLF ESGAILLYLA EKTGLFLSHE TRERAATLQW LFWQVGGLGP MLGQNHHFNH 

       130        140        150        160        170        180 
AAPQTIPYAI ERYQVETQRL YHVLNKRLEN SPWLGGENYS IADIACWPWV NAWTRQRIDL 

       190        200        210 
AMYPAVKNWH ERIRSRPATG QALLKAQLGD ERSDS

« Hide

References

	« Hide 'large scale' referencesShow '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. 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 277:1453-1474(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, 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC75362.1.
AP009048 Genomic DNA. Translation: BAA16139.1.

PIR

D65002.

RefSeq

NP_416805.1. NC_000913.2.
YP_490544.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GX0	X-ray	2.30	A	1-215	[»]

ProteinModelPortal

P77526.

SMR

P77526. Positions 1-204.

ModBase

Search...

Protein-protein interaction databases

IntAct

P77526. 2 interactions.

STRING

511145.b2302.

Proteomic databases

PaxDb

P77526.

PRIDE

P77526.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75362; AAC75362; b2302.
BAA16139; BAA16139; BAA16139.

GeneID

12931523.
946763.

KEGG

ecj:Y75_p2268.
eco:b2302.

PATRIC

32119975. VBIEscCol129921_2397.

Organism-specific databases

EchoBASE

EB3863.

EcoGene

EG14110. yfcG.

Phylogenomic databases

eggNOG

COG0625.

HOGENOM

HOG000125752.

K00799.

OMA

NISAGDQ.

ProtClustDB

PRK13972.

Enzyme and pathway databases

BioCyc

EcoCyc:G7194-MONOMER.
ECOL316407:JW2299-MONOMER.
MetaCyc:G7194-MONOMER.

Gene expression databases

Genevestigator

P77526.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF00043. GST_C. 1 hit.
[Graphical view]

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P77526.

Entry information

Entry name

YFCG_ECOLI

Accession

Primary (citable) accession number: P77526

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents