Glutathione reductase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P06715 (GSHR_ECOLI)

Last modified June 16, 2009. Version 109. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Glutathione reductase
      Short name=GRase
      Short name=GR
    EC=1.8.1.7

Gene names

Name:	gor
Ordered Locus Names:	b3500, JW3467

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Maintains high levels of reduced glutathione in the cytosol.
Catalytic activity	2 glutathione + NADP⁺ = glutathione disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay. Source: UniProtKB
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-909700,EBI-548960

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

Glutathione reductase

PRO_0000067975

Regions

Nucleotide binding

34 – 41

FAD

Sites

Active site

439

Proton acceptor

Amino acid modifications

Disulfide bond

42 ↔ 47

Redox-active Ref.6

Secondary structure

450

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P06715-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 3C8652AFE4E4ABF6
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FASTA

450

48,773

        10         20         30         40         50         60 
MTKHYDYIAI GGGSGGIASI NRAAMYGQKC ALIEAKELGG TCVNVGCVPK KVMWHAAQIR 

        70         80         90        100        110        120 
EAIHMYGPDY GFDTTINKFN WETLIASRTA YIDRIHTSYE NVLGKNNVDV IKGFARFVDA 

       130        140        150        160        170        180 
KTLEVNGETI TADHILIATG GRPSHPDIPG VEYGIDSDGF FALPALPERV AVVGAGYIAV 

       190        200        210        220        230        240 
ELAGVINGLG AKTHLFVRKH APLRSFDPMI SETLVEVMNA EGPQLHTNAI PKAVVKNTDG 

       250        260        270        280        290        300 
SLTLELEDGR SETVDCLIWA IGREPANDNI NLEAAGVKTN EKGYIVVDKY QNTNIEGIYA 

       310        320        330        340        350        360 
VGDNTGAVEL TPVAVAAGRR LSERLFNNKP DEHLDYSNIP TVVFSHPPIG TVGLTEPQAR 

       370        380        390        400        410        420 
EQYGDDQVKV YKSSFTAMYT AVTTHRQPCR MKLVCVGSEE KIVGIHGIGF GMDEMLQGFA 

       430        440        450 
VALKMGATKK DFDNTVAIHP TAAEEFVTMR

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases." Greer S., Perham R.N. Biochemistry 25:2736-2742(1986) [PubMed: 3521741] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed: 8041620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0-A resolution." Ermler U., Schulz G.E. Proteins 9:174-179(1991) [PubMed: 2006135] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[6]	"Structure of glutathione reductase from Escherichia coli at 1.86-A resolution: comparison with the enzyme from human erythrocytes." Mittl P.R.E., Schulz G.E. Protein Sci. 3:799-809(1994) [PubMed: 8061609] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), DISULFIDE BOND.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M13141 Genomic DNA. Translation: AAA23926.1.
U00039 Genomic DNA. Translation: AAB18476.1.
U00096 Genomic DNA. Translation: AAC76525.1.
AP009048 Genomic DNA. Translation: BAE77794.1.

PIR

RDECU. A24409.

RefSeq

AP_004293.1.
NP_417957.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GER	X-ray	1.86	A/B	1-450	[»]
1GES	X-ray	1.74	A/B	1-450	[»]
1GET	X-ray	2.00	A/B	1-450	[»]
1GEU	X-ray	2.20	A/B	1-450	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P06715. 3 interactions.

2-D gel databases

SWISS-2DPAGE

P06715.

ECO2DBASE

F045.6. 6TH EDITION.

Genome annotation databases

GeneID

948014.

GenomeReviews

Gene locus JW3467 in contig AP009048_GR.
Gene locus b3500 in contig U00096_GR.

KEGG

ecj:JW3467.
eco:b3500.

Organism-specific databases

EchoBASE

EB0407.

EcoGene

EG10412. gor.

CMR

Search...

Phylogenomic databases

HOGENOM

P06715.

OMA

P06715. HRQPCKM.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUTATHIONE-REDUCT-NADPH-MON.
MetaCyc:GLUTATHIONE-REDUCT-NADPH-MON.

Family and domain databases

InterPro

IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006322. Glut_reduct_1.
IPR000815. Hg_reductase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]

Gene3D

G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.
PR00945. HGRDTASE.

ProDom

PD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01421. gluta_reduc_1. 1 hit.

PROSITE

PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00336. Nitrofurazone.

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Entry information

Entry name

GSHR_ECOLI

Accession

Primary (citable) accession number: P06715
Secondary accession number(s): Q2M7G2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	June 16, 2009
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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 and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other Resources

Entry information

Relevant documents