P0AGG6 (THIO2_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin-2
Short name=Trx-2
EC=1.8.1.8

Alternative name(s):
Protein-disulfide reductase

Gene names

Name:	trxC
Ordered Locus Names:	Z3867, ECs3448

Organism

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

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	139 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin By similarity.
Catalytic activity	Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the thioredoxin family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Domain	Redox-active center Zinc-finger
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete 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 glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro protein-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 – 139	139	Thioredoxin-2		PRO_0000120103
Regions
	Domain	26 – 139	114	Thioredoxin
	Zinc finger	5 – 18	14	Potential
Amino acid modifications
	Disulfide bond	64 ↔ 67		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AGG6 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 4C973F6FE55C8856	FASTA	139	15,555
	10 20 30 40 50 60 MNTVCTHCQA INRIPDDRIE DAAKCGRCGH DLFDGEVINA TGETLDKLLK DDLPVVIDFW 70 80 90 100 110 120 APWCGPCRNF APIFEDVAQE RSGKVRFVKV NTEAERELSS RFGIRSIPTI MIFKNGQVVD 130 MLNGAVPKAP FDSWLNESL

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG57699.1. BA000007 Genomic DNA. Translation: BAB36871.1.
PIR	G85904. H91059.
RefSeq	NP_289141.1. NC_002655.2. NP_311475.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0AGG6.
SMR	P0AGG6. Positions 36-139.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1227488.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000025685; EBESCP00000024578; EBESCG00000024738. EBESCT00000056440; EBESCP00000054268; EBESCG00000055488.
GeneID	914878. 957981.
GenomeReviews	Gene locus Z3867 in contig AE005174_GR. Gene locus ECs3448 in contig BA000007_GR.
KEGG	ece:Z3867. ecs:ECs3448.
PATRIC	18356334. VBIEscCol44059_3362.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008978.
HOGENOM	HBG493509.
OMA	MIFKQGH.
ProtClustDB	PRK10996.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3448-MONOMER.
Family and domain databases
InterPro	IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K03672.
PANTHER	PTHR10438. Trx. 1 hit.
Pfam	PF00085. Thioredoxin. 1 hit. [Graphical view]
PIRSF	PIRSF000077. Thioredoxin. 1 hit.
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMs	TIGR01068. Thioredoxin. 1 hit.
PROSITE	PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THIO2_ECO57

Accession

Primary (citable) accession number: P0AGG6
Secondary accession number(s): P33636 , P76593, P77000, P77001

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program