Glutathione reductase - Escherichia coli (strain K12)

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P06715 (GSHR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 135. 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:
Glutathione reductase
Short name=GR
Short name=GRase
EC=1.8.1.7

Gene names

Name:	gor
Ordered Locus Names:	b3500, JW3467

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.

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 Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay. Source: UniProtKB
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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...

Sequences

Sequence

Length

Mass (Da)

Tools

P06715 [UniParc].

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

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

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_417957.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P06715.

SMR

P06715. Positions 2-450.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06715. 5 interactions.

2D gel databases

SWISS-2DPAGE

P06715.

ECO2DBASE

F045.6. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004575; EBESCP00000004575; EBESCG00000003735.
EBESCT00000017933; EBESCP00000017224; EBESCG00000016989.

GeneID

948014.

GenomeReviews

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

KEGG

ecj:JW3467.
eco:b3500.

PATRIC

32122450. VBIEscCol129921_3602.

Organism-specific databases

EchoBASE

EB0407.

EcoGene

EG10412. gor.

Phylogenomic databases

eggNOG

COG1249.

GeneTree

EBGT00050000009315.

HOGENOM

HBG515043.

OMA

VTSHRQP.

PhylomeDB

P06715.

ProtClustDB

PRK06116.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P06715.

Family and domain databases

InterPro

IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.

K00383.

Pfam

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

PRINTS

PR00368. FADPNR.

SUPFAM

SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.

TIGRFAMs

TIGR01421. Gluta_reduc_1. 1 hit.

PROSITE

PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00336. Nitrofurazone.

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:	January 25, 2012
This is version 135 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

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel 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