Reviewed, UniProtKB/Swiss-Prot P68688 (GLRX1_ECOLI)

Names and origin

Protein names

Recommended name:
    Glutaredoxin-1
      Short name=Grx1

Gene names

Name:	grxA
Synonyms:	grx
Ordered Locus Names:	b0849, JW0833

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	85 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase.
Subunit structure	Monomer.
Sequence similarities	Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain.

Ontologies

Keywords
Biological process	Deoxyribonucleotide synthesis Electron transport Transport
Domain	Redox-active center
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro deoxyribonucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
sll1621	P73728	1	EBI-863137,EBI-862771	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 85

85

Glutaredoxin-1

PRO_0000141581

Regions

Domain

1 – 85

85

Glutaredoxin

Amino acid modifications

Disulfide bond

11 ↔ 14

Redox-active

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

85

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

13 – 28

16

Beta strand

32 – 36

5

Helix

38 – 41

4

Helix

46 – 51

6

Beta strand

61 – 64

4

Beta strand

67 – 72

6

Helix

73 – 84

12

Sequences

	Sequence		Length	Mass (Da)
	P68688-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 33C185A47021EF42	FASTA	85	9,685
	10 20 30 40 50 60 MQTVIFGRSG CPYCVRAKDL AEKLSNERDD FQYQYVDIRA EGITKEDLQQ KAGKPVETVP 70 80 QIFVDQQHIG GYTDFAAWVK ENLDA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol." Hoeoeg J.-O., Joernvall H., Holmgren A., Carlquist M., Persson M. Eur. J. Biochem. 136:223-232(1983) [PubMed: 6352262] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: K12.
[2]	"Cloning and expression of the glutaredoxin (grx) gene of Escherichia coli." Hoeoeg J.-O., von Bahr-Lindstroem H., Joernvall H., Holmgren A. Gene 43:13-21(1986) [PubMed: 3530878] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	Chatterjee P.K., Sternberg N.L. Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"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.
[6]	"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.
[7]	"Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin. Sequence-specific assignments and secondary structure determination of the oxidized form." Sodano P., Chary K.V.R., Bjoernberg O., Holmgren A., Kren B., Fuchs J.A., Wuethrich K. Eur. J. Biochem. 200:369-377(1991) [PubMed: 1889405] [Abstract] Cited for: STRUCTURE BY NMR.
[8]	"Sequence-specific 1H NMR assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin." Sodano P., Xia T.-H., Bushweller J.H., Bjoernberg O., Holmgren A., Billeter M., Wuethrich K. J. Mol. Biol. 221:1311-1324(1991) [PubMed: 1942053] [Abstract] Cited for: STRUCTURE BY NMR.
[9]	"NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins." Xia T.-H., Bushweller J.H., Sodano P., Billeter M., Bjoernberg O., Holmgren A., Wuethrich K. Protein Sci. 1:310-321(1992) [PubMed: 1304339] [Abstract] Cited for: STRUCTURE BY NMR.
[10]	"Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements." Kelley J.J. III, Caputo M., Eaton S.F., Laue T.M., Bushweller J.H. Biochemistry 36:5029-5044(1997) [PubMed: 9125525] [Abstract] Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M13449 Genomic DNA. Translation: AAA23936.1.
U18655 Genomic DNA. Translation: AAC43449.1.
U00096 Genomic DNA. Translation: AAC73936.1.
AP009048 Genomic DNA. Translation: BAA35552.1.

PIR

GDEC. A00283.

RefSeq

AP_001480.1.
NP_415370.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EGO	NMR	-	A	1-85	[»]
1EGR	NMR	-	A	1-85	[»]
1GRX	NMR	-	A	1-85	[»]
1QFN	NMR	-	A	1-85	[»]
1UPY	model	-	G	1-85	[»]
1UPZ	model	-	G	1-85	[»]
1UQ0	model	-	G	1-85	[»]
1UQ1	model	-	G	1-85	[»]
1UQ2	model	-	G	1-85	[»]
1UQ3	model	-	G	1-85	[»]
1UQ6	model	-	G	1-85	[»]
1UQ7	model	-	G	1-85	[»]
1UQH	model	-	G	1-85	[»]
1UQN	model	-	G	1-85	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P68688. 10 interactions.

2-D gel databases

ECO2DBASE

B011.0. 6TH EDITION.

Genome annotation databases

GeneID

945479.

GenomeReviews

Gene locus JW0833 in contig AP009048_GR.
Gene locus b0849 in contig U00096_GR.

KEGG

ecj:JW0833.
eco:b0849.

Organism-specific databases

EchoBASE

EB0412.

EcoGene

EG10417. grxA.

CMR

Search...

Phylogenomic databases

HOGENOM

P68688.

OMA

P68688. KYVDIHA.

Enzyme and pathway databases

BioCyc

EcoCyc:RED-GLUTAREDOXIN.
MetaCyc:RED-GLUTAREDOXIN.

Family and domain databases

InterPro

IPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR014025. Glutaredoxin_sub.
IPR011902. GRXA.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF00462. Glutaredoxin. 1 hit.
[Graphical view]

PRINTS

PR00160. GLUTAREDOXIN.

TIGRFAMs

TIGR02183. GRXA. 1 hit.

PROSITE

PS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLRX1_ECOLI

Accession

Primary (citable) accession number: P68688
Secondary accession number(s): P00277

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 49 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)