Reviewed, UniProtKB/Swiss-Prot P0AC64 (GLRX3_ECO57)

Names and origin

Protein names

Recommended name:
    Glutaredoxin-3
      Short name=Grx3

Gene names

Name:	grxC
Ordered Locus Names:	Z5037, ECs4488

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	83 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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 By similarity.
Subunit structure	Monomer Probable.
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	Complete proteome
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 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 83	82	Glutaredoxin-3		PRO_0000141589
Regions
	Domain	2 – 83	82	Glutaredoxin
Amino acid modifications
	Disulfide bond	12 ↔ 15		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AC64-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5B19A85BB0C9FBEF	FASTA	83	9,137
	10 20 30 40 50 60 MANVEIYTKE TCPYCHRAKA LLSSKGVSFQ ELPIDGNAAK REEMIKRSGR TTVPQIFIDA 70 80 QHIGGCDDLY ALDARGGLDP LLK

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG58757.1. BA000007 Genomic DNA. Translation: BAB37911.1.
PIR	A86037. H91189.
RefSeq	NP_290193.1. NP_312515.1.
3D structure databases
SMR	P0AC64. Positions 2-83.
ModBase	Search...
Genome annotation databases
GeneID	915569. 960937.
GenomeReviews	Gene locus Z5037 in contig AE005174_GR. Gene locus ECs4488 in contig BA000007_GR.
KEGG	ece:Z5037. ecs:ECs4488.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0AC64.
OMA	P0AC64. CDELHAL.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS4488-MON.
Family and domain databases
InterPro	IPR011767. GLR_AS. IPR002109. Glutaredoxin. IPR014025. Glutaredoxin_sub. IPR011900. GRX_bact. 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	TIGR02181. GRX_bact. 1 hit.
PROSITE	PS00195. GLUTAREDOXIN_1. 1 hit. PS51354. GLUTAREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLRX3_ECO57

Accession

Primary (citable) accession number: P0AC64
Secondary accession number(s): P37687

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 24 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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