Thioredoxin-2 - Escherichia coli (strain K12)

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P0AGG4 (THIO2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

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

Alternative name(s):
Protein-disulfide reductase

Gene names

Name:	trxC
Synonyms:	yfiG
Ordered Locus Names:	b2582, JW2566

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	139 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin.
Catalytic activity	Protein dithiol + NAD(P)⁺ = protein disulfide + NAD(P)H.
Subcellular location	Cytoplasm.
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 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 glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from mutant phenotype. Source: EcoCyc
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activity Inferred from mutant phenotype. Source: EcoCyc protein-disulfide reductase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from direct assay. Source: EcoCyc
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_0000120102

Regions

Domain

26 – 139

114

Thioredoxin

Zinc finger

5 – 18

Potential

Amino acid modifications

Disulfide bond

64 ↔ 67

Redox-active By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0AGG4 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 4C973F6FE55C8856
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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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression, and characterization of a novel Escherichia coli thioredoxin." Miranda-Vizuete A., Damdimopoulos A.E., Gustafsson J.-A., Spyrou G. J. Biol. Chem. 272:30841-30847(1997) [PubMed: 9388228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: K12 / TG1.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [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], SEQUENCE REVISION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia coli." Nashimoto H. (In) Nierhaus K.H. (eds.); The translational apparatus, pp.185-195, Plenum Press, New York (1993) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-104. Strain: K12.
[6]	Rudd K.E. Unpublished observations (NOV-1993) Cited for: IDENTIFICATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U85942 Genomic DNA. Translation: AAB88587.1. U00096 Genomic DNA. Translation: AAC75635.1. AP009048 Genomic DNA. Translation: BAA16469.2. D13169 Genomic DNA. No translation available.
PIR	E65036.
RefSeq	NP_417077.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0AGG4.
SMR	P0AGG4. Positions 36-139.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48115N.
IntAct	P0AGG4. 23 interactions.
MINT	MINT-1227521.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000001874; EBESCP00000001874; EBESCG00000001540. EBESCT00000016536; EBESCP00000015827; EBESCG00000015596.
GeneID	947062.
GenomeReviews	Gene locus JW2566 in contig AP009048_GR. Gene locus b2582 in contig U00096_GR.
KEGG	ecj:JW2566. eco:b2582.
PATRIC	32120565. VBIEscCol129921_2685.
Organism-specific databases
EchoBASE	EB1833.
EcoGene	EG11887. trxC.
Phylogenomic databases
eggNOG	COG0526.
GeneTree	EBGT00050000008978.
HOGENOM	HBG493509.
OMA	MIFKQGH.
PhylomeDB	P0AGG4.
ProtClustDB	PRK10996.
Enzyme and pathway databases
BioCyc	EcoCyc:RED-THIOREDOXIN2-MONOMER. MetaCyc:RED-THIOREDOXIN2-MONOMER.
Gene expression databases
Genevestigator	P0AGG4.
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_ECOLI

Accession

Primary (citable) accession number: P0AGG4
Secondary accession number(s): P33636

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 54 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

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

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents