P0AC59 (GLRX2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutaredoxin-2
Short name=Grx2

Gene names

Name:	grxB
Ordered Locus Names:	b1064, JW1051

Organism

Escherichia coli (strain K12)

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	Involved in reducing some disulfides in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide reductase.
Sequence similarities	Belongs to the glutaredoxin family. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Domain	Redox-active center
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro 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 disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 215

215

Glutaredoxin-2

PRO_0000141585

Regions

Domain

1 – 77

77

GST N-terminal

Amino acid modifications

Disulfide bond

9 ↔ 12

Redox-active By similarity

Experimental info

Sequence conflict

13

1

L → I AA sequence Ref.5

Secondary structure

1

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215

Helix Strand Turn

Details...

Beta strand

2 – 5

4

Helix

10 – 22

13

Beta strand

27 – 30

4

Helix

37 – 43

7

Beta strand

44 – 46

3

Beta strand

50 – 53

4

Turn

54 – 56

3

Beta strand

57 – 60

4

Helix

62 – 72

11

Helix

84 – 107

24

Helix

111 – 113

3

Helix

116 – 123

8

Turn

124 – 129

6

Helix

132 – 157

26

Beta strand

159 – 162

4

Helix

170 – 183

14

Helix

192 – 205

14

Helix

211 – 213

3

Sequences

	Sequence		Length	Mass (Da)
	P0AC59 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: A8AAAB2548D824FE	FASTA	215	24,350
	10 20 30 40 50 60 MKLYIYDHCP YCLKARMIFG LKNIPVELHV LLNDDAETPT RMVGQKQVPI LQKDDSRYMP 70 80 90 100 110 120 ESMDIVHYVD KLDGKPLLTG KRSPAIEEWL RKVNGYANKL LLPRFAKSAF DEFSTPAARK 130 140 150 160 170 180 YFVDKKEASA GNFADLLAHS DGLIKNISDD LRALDKLIVK PNAVNGELSE DDIQLFPLLR 190 200 210 NLTLVAGINW PSRVADYRDN MAKQTQINLL SSMAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli." Vlamis-Gardikas A., Aaslund F., Spyrou G., Bergman T., Holmgren A. J. Biol. Chem. 272:11236-11243(1997) [PubMed: 9111025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: K12.
[2]	"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.
[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]	"Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant." Aaslund F., Ehn B., Miranda-Vizuete A., Pueyo C., Holmgren A. Proc. Natl. Acad. Sci. U.S.A. 91:9813-9817(1994) [PubMed: 7937896] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-18, CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X92076 Genomic DNA. Translation: CAA63058.1.
U00096 Genomic DNA. Translation: AAC74148.1.
AP009048 Genomic DNA. Translation: BAA35872.1.

PIR

E64849.

RefSeq

NP_415582.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G7O	NMR	-	A	1-215	[»]

ProteinModelPortal

P0AC59.

SMR

P0AC59. Positions 1-215.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48247N.

IntAct

P0AC59. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004135; EBESCP00000004135; EBESCG00000003375.
EBESCT00000015718; EBESCP00000015009; EBESCG00000014778.

GeneID

946926.

GenomeReviews

Gene locus JW1051 in contig AP009048_GR.
Gene locus b1064 in contig U00096_GR.

KEGG

ecj:JW1051.
eco:b1064.

PATRIC

32117367. VBIEscCol129921_1106.

Organism-specific databases

EchoBASE

EB2551.

EcoGene

EG12688. grxB.

Phylogenomic databases

eggNOG

COG2999.

GeneTree

EBGT00050000009127.

HOGENOM

HBG625601.

OMA

MPESLDI.

ProtClustDB

PRK10387.

Enzyme and pathway databases

BioCyc

EcoCyc:GRXB-MONOMER.

Gene expression databases

Genevestigator

P0AC59.

Family and domain databases

InterPro

IPR011767. GLR_AS.
IPR007494. Glutaredoxin2_C.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR011901. GRXB.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

KO

K03675.

PANTHER

PTHR11260:SF65. PTHR11260:SF65. 1 hit.

Pfam

PF04399. Glutaredoxin2_C. 1 hit.
[Graphical view]

SUPFAM

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

TIGRFAMs

TIGR02182. GRXB. 1 hit.

PROSITE

PS00195. GLUTAREDOXIN_1. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GLRX2_ECOLI

Accession

Primary (citable) accession number: P0AC59
Secondary accession number(s): P39811, P75928, P77043

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program