P0AA25 (THIO_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin-1
Short name=Trx-1

Gene names

Name:	trxA
Synonyms:	fipA, tsnC
Ordered Locus Names:	b3781, JW5856

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	109 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Subunit structure	Monomer. Interacts with bacteriophage T3 DNA polymerase.
Sequence similarities	Belongs to the thioredoxin family. Contains 1 thioredoxin domain.
Sequence caution	The sequence AAA24534.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAA67582.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Electron transport Host-virus interaction Transport
Domain	Redox-active center
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from mutant phenotype PubMed 9188456. Source: EcoCyc electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activity Inferred from direct assay PubMed 10464247. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
At2g44920	O22160	2	EBI-368542,EBI-2895776	From a different organism.
At5g53490	P81760	2	EBI-368542,EBI-449573	From a different organism.
FKBP13	Q9SCY2	2	EBI-368542,EBI-2895757	From a different organism.
PPD6	Q9LXX5	2	EBI-368542,EBI-2895738	From a different organism.
PRXQ	Q9LU86	2	EBI-368542,EBI-540311	From a different organism.
PSBO1	P23321	2	EBI-368542,EBI-449414	From a different organism.
PSBO2	Q9S841	2	EBI-368542,EBI-449424	From a different organism.
TL29	P82281	2	EBI-368542,EBI-2895799	From a different organism.
VDE1	Q39249	2	EBI-368542,EBI-2895666	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 109

108

Thioredoxin-1

PRO_0000120096

Regions

Domain

2 – 109

108

Thioredoxin

Sites

Active site

33

1

Nucleophile

Active site

36

1

Nucleophile

Site

27

1

Deprotonates C-terminal active site Cys

Site

34

1

Contributes to redox potential value

Site

35

1

Contributes to redox potential value

Amino acid modifications

Modified residue

70

1

N6-acetyllysine Ref.10

Disulfide bond

33 ↔ 36

Redox-active Ref.15

Experimental info

Sequence conflict

72 – 73

2

GI → IG AA sequence Ref.8

Sequence conflict

88

1

A → AS in AAA24696. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

109

Helix Strand Turn

Details...

Beta strand

5 – 7

3

Turn

10 – 12

3

Helix

13 – 16

4

Turn

17 – 19

3

Beta strand

21 – 29

9

Helix

34 – 49

16

Turn

50 – 53

4

Beta strand

54 – 60

7

Turn

61 – 63

3

Helix

67 – 70

4

Beta strand

75 – 83

9

Beta strand

86 – 93

8

Helix

97 – 108

12

Sequences

	Sequence		Length	Mass (Da)
	P0AA25 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: EF5933EA29668EE9	FASTA	109	11,807
	10 20 30 40 50 60 MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY QGKLTVAKLN 70 80 90 100 IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL KEFLDANLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the thioredoxin gene from Escherichia coli." Hoeoeg J.-O., von Bahr-Lindstroem H., Josephson S., Wallace B.J., Kushner S.R., Joernvall H., Holmgren A. Biosci. Rep. 4:917-923(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genetic and physical analysis of the thioredoxin (trxA) gene of Escherichia coli K-12." Wallace B.J., Kushner S.R. Gene 32:399-408(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning and nucleotide sequence of the trxA gene of Escherichia coli K-12." Lim C.-J., Geraghty D., Fuchs J.A. J. Bacteriol. 163:311-316(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Physical analysis of the thioredoxin gene from Escherichia coli K-12." Wallace B.J., Zownir O., Kushner S.R. (In) Holmgren A. (eds.); Thioredoxin and glutaredoxin systems, structure and function, pp.11-19, Raven Press, New York (1986) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R. Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Thioredoxin. 6. The amino acid sequence of the protein from Escherichia coli B." Holmgren A. Eur. J. Biochem. 6:475-484(1968) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-109. Strain: B.
[9]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[10]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[11]	"Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8-A resolution." Holmgren A., Soederberg B.-O., Eklund H., Braenden C.-I. Proc. Natl. Acad. Sci. U.S.A. 72:2305-2309(1975) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[12]	"Structure of oxidized thioredoxin to 4 with 5-A resolution." Soederberg B.-O., Holmgren A., Braenden C.-I. J. Mol. Biol. 90:143-152(1974) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
[13]	"Crystal structure of thioredoxin from Escherichia coli at 1.68-A resolution." Katti S.K., le Master D.M., Eklund H. J. Mol. Biol. 212:167-184(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS).
[14]	"Crystal structure analysis of a mutant Escherichia coli thioredoxin in which lysine 36 is replaced by glutamic acid." Nikkola M., Gleason F.K., Fuchs J.A., Eklund H. Biochemistry 32:5093-5098(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-37.
[15]	"The CXXC motif: crystal structure of an active-site variant of Escherichia coli thioredoxin." Schultz L.W., Chivers P.T., Raines R.T. Acta Crystallogr. D 55:1533-1538(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), DISULFIDE BOND.
[16]	"Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase." Lennon B.W., Williams C.H. Jr., Ludwig M.L. Science 289:1190-1194(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TRXB.
[17]	"Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy." Dyson H.J., Gippert G.P., Case D.A., Holmgren A., Wright P.E. Biochemistry 29:4129-4136(1990) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[18]	"High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin." Jeng M.F., Campbell A.P., Begley T., Holmgren A., Case D.A., Wright P.E., Dyson H.J. Structure 2:853-868(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M26133 Genomic DNA. Translation: AAA24693.1.
K02845 Genomic DNA. Translation: AAA24534.1. Different initiation.
M10424 Genomic DNA. Translation: AAA24533.1.
M54881 Genomic DNA. Translation: AAA24696.1.
M12779 Genomic DNA. Translation: AAA24694.1.
M87049 Genomic DNA. Translation: AAA67582.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76786.2.
AP009048 Genomic DNA. Translation: BAE77517.1.

PIR

TXEC. A91519.

RefSeq

NP_418228.2. NC_000913.2.
YP_491658.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F6M	X-ray	2.95	C/D/G/H	2-109	[»]
1KEB	X-ray	1.80	A/B	2-108	[»]
1M7T	NMR	-	A	68-108	[»]
1OAZ	X-ray	2.77	A/B	1-109	[»]
1SKR	X-ray	2.40	B	2-108	[»]
1SKS	X-ray	2.30	B	2-108	[»]
1SKW	X-ray	2.30	B	2-108	[»]
1SL0	X-ray	3.20	B/D	2-108	[»]
1SL1	X-ray	2.20	B	2-108	[»]
1SL2	X-ray	2.30	B	2-108	[»]
1SRX	X-ray	2.80	A	2-109	[»]
1T7P	X-ray	2.20	B	2-108	[»]
1T8E	X-ray	2.54	B	2-108	[»]
1THO	X-ray	2.30	A	2-108	[»]
1TK0	X-ray	2.30	B	2-108	[»]
1TK5	X-ray	2.20	B	2-108	[»]
1TK8	X-ray	2.50	B	2-108	[»]
1TKD	X-ray	2.49	B	2-108	[»]
1TXX	X-ray	2.20	A	2-109	[»]
1X9M	X-ray	2.10	B	2-108	[»]
1X9S	X-ray	2.70	B	2-108	[»]
1X9W	X-ray	2.30	B	2-108	[»]
1XOA	NMR	-	A	2-109	[»]
1XOB	NMR	-	A	2-109	[»]
1ZCP	X-ray	2.30	A/B/C/D	2-108	[»]
1ZYQ	X-ray	2.70	B	2-108	[»]
1ZZY	X-ray	2.50	A/B	2-109	[»]
2AJQ	X-ray	2.60	B/I	2-108	[»]
2BTO	X-ray	2.50	T	2-109	[»]
2EIO	X-ray	2.60	A/B/C/D	2-109	[»]
2EIQ	X-ray	1.90	A/B	2-109	[»]
2EIR	X-ray	2.50	A/B/C/D	2-109	[»]
2FCH	X-ray	2.60	A/B/C/D/E/F/G	2-108	[»]
2FD3	X-ray	2.45	A/B	2-108	[»]
2H6X	X-ray	2.60	A/B	2-109	[»]
2H6Y	X-ray	2.40	A/B	2-109	[»]
2H6Z	X-ray	2.25	A/B	2-109	[»]
2H70	X-ray	2.70	A/B	2-109	[»]
2H71	X-ray	2.20	A/B	2-109	[»]
2H72	X-ray	2.25	A/B	2-109	[»]
2H73	X-ray	2.45	A/B	2-109	[»]
2H74	X-ray	2.40	A/B	4-109	[»]
2H75	X-ray	2.20	A/B	2-109	[»]
2H76	X-ray	2.25	A/B	2-109	[»]
2O8V	X-ray	3.00	B	2-109	[»]
2TIR	X-ray	2.00	A	2-109	[»]
2TRX	X-ray	1.68	A/B	2-109	[»]
3DYR	X-ray	2.00	A/B	2-109	[»]

ProteinModelPortal

P0AA25.

SMR

P0AA25. Positions 2-109.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31856N.

IntAct

P0AA25. 91 interactions.

STRING

511145.b3781.

2D gel databases

SWISS-2DPAGE

P0AA25.

Proteomic databases

PaxDb

P0AA25.

PRIDE

P0AA25.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76786; AAC76786; b3781.
BAE77517; BAE77517; BAE77517.

GeneID

12934322.
948289.

KEGG

ecj:Y75_p3394.
eco:b3781.

PATRIC

32123053. VBIEscCol129921_3896.

Organism-specific databases

EchoBASE

EB1024.

EcoGene

EG11031. trxA.

Phylogenomic databases

eggNOG

COG0526.

HOGENOM

HOG000292977.

KO

K03671.

OMA

SDKIVYL.

ProtClustDB

PRK09381.

Enzyme and pathway databases

BioCyc

EcoCyc:RED-THIOREDOXIN-MONOMER.
ECOL316407:JW5856-MONOMER.
MetaCyc:RED-THIOREDOXIN-MONOMER.

Gene expression databases

Genevestigator

P0AA25.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]

PANTHER

PTHR10438. PTHR10438. 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...

Other

EvolutionaryTrace

P0AA25.

Entry information

Entry name

THIO_ECOLI

Accession

Primary (citable) accession number: P0AA25
Secondary accession number(s): P00274 , P76750, Q2M889, Q47674, Q8XAT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program