P77544 (YFCF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase YfcF
EC=2.5.1.18

Gene names

Name:	yfcF
Ordered Locus Names:	b2301, JW2298

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	214 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Molecular function	Oxidoreductase Peroxidase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to hydrogen peroxide Inferred from mutant phenotype Ref.4. Source: EcoCyc
Molecular_function	glutathione transferase activity Inferred from direct assay Ref.4. 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 – 214

214

Glutathione S-transferase YfcF

PRO_0000186015

Regions

Domain

6 – 87

82

GST N-terminal

Domain

95 – 214

120

GST C-terminal

Experimental info

Mutagenesis

10

1

S → A: Nearly no effect on GSH transferase activity. Ref.4

Mutagenesis

16

1

S → G: 2% of wild-type GSH transferase activity. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

214

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Helix

17 – 29

13

Beta strand

34 – 38

5

Beta strand

61 – 64

4

Beta strand

67 – 71

5

Helix

72 – 82

11

Turn

85 – 87

3

Helix

96 – 111

16

Helix

114 – 119

6

Helix

123 – 126

4

Helix

136 – 152

17

Turn

153 – 155

3

Helix

166 – 179

14

Turn

180 – 182

3

Helix

187 – 197

11

Helix

200 – 210

11

Sequences

	Sequence		Length	Mass (Da)
	P77544 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 6B2308D403DA3077	FASTA	214	24,326
	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

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. , 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 277:1453-1474(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, 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.

PIR

C65002.

RefSeq

NP_416804.1. NC_000913.2.
YP_490543.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BBY	X-ray	1.85	A	1-214	[»]

ProteinModelPortal

P77544.

SMR

P77544. Positions 3-211.

ModBase

Search...

Protein-protein interaction databases

IntAct

P77544. 3 interactions.

STRING

511145.b2301.

Proteomic databases

PaxDb

P77544.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75361; AAC75361; b2301.
BAA16138; BAA16138; BAA16138.

GeneID

12931522.
946749.

KEGG

ecj:Y75_p2267.
eco:b2301.

PATRIC

32119973. VBIEscCol129921_2396.

Organism-specific databases

EchoBASE

EB3862.

EcoGene

EG14109. yfcF.

Phylogenomic databases

eggNOG

COG0625.

HOGENOM

HOG000255229.

OMA

FSPYVMS.

ProtClustDB

PRK15113.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P77544.

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.
IPR012336. Thioredoxin-like_fold.
[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

P77544.

Entry information

Entry name

YFCF_ECOLI

Accession

Primary (citable) accession number: P77544

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program