Thioredoxin-2 - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0AGG4 (THIO2_ECOLI)

Last modified June 16, 2009. Version 31. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	139 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.

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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 protein binding Inferred from physical interaction. Source: IntAct protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro protein-disulfide reductase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
murD	P14900	1	EBI-549392,EBI-554780

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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

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Sequences

Sequence

Length

Mass (Da)

Tools

P0AGG4-1 [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

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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.

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Cross-references

Sequence databases
	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	AP_003168.1. NP_417077.1.
3D structure databases
HSSP	HSSP built from PDB template 1DBY based on UniProtKB P23400.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0AGG4. 23 interactions.
Genome annotation databases
GeneID	947062.
GenomeReviews	Gene locus JW2566 in contig AP009048_GR. Gene locus b2582 in contig U00096_GR.
KEGG	ecj:JW2566. eco:b2582.
Organism-specific databases
EchoBASE	EB1833.
EcoGene	EG11887. trxC.
CMR	Search...
Phylogenomic databases
HOGENOM	P0AGG4.
OMA	P0AGG4. MIFKQGH.
Enzyme and pathway databases
BioCyc	EcoCyc:RED-THIOREDOXIN2-MON.
Family and domain databases
InterPro	IPR005746. Thioredoxin. IPR017936. Thioredoxin-like. IPR006662. Thioredoxin-like_subdom. IPR015467. Thioredoxin_core. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHER	PTHR10438. Trx. 1 hit.
Pfam	PF00085. Thioredoxin. 1 hit. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
TIGRFAMs	TIGR01068. thioredoxin. 1 hit.
PROSITE	PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

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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:	June 16, 2009
This is version 31 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)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents