trxA

Functionⁱ

Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	27	Deprotonates C-terminal active site Cys	1
Active siteⁱ	33	Nucleophile	1
Siteⁱ	34	Contributes to redox potential value	1
Siteⁱ	35	Contributes to redox potential value	1
Active siteⁱ	36	Nucleophile	1

GO - Molecular functionⁱ

DNA polymerase processivity factor activity
Source: FlyBase
Inferred from direct assayⁱ
- "Hydrophobic Residue in Escherichia coli Thioredoxin Critical for the Processivity of T7 DNA Polymerase."
  Lee S.J., Tran N.Q., Lee J., Richardson C.C.
  Biochemistry 57:5807-5817(2018) [PubMed] [Europe PMC] [Abstract]
oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
  Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
  Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
protein-disulfide reductase (NAD(P)) activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
  Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
  Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
protein-disulfide reductase activity
Source: EcoCyc
Inferred from direct assayⁱ
- "Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli."
  Mossner E., Huber-Wunderlich M., Rietsch A., Beckwith J., Glockshuber R., Aslund F.
  J Biol Chem 274:25254-25259(1999) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Electron transport, Host-virus interaction, Transport

Biological process

Electron transport, Host-virus interaction, Transport

Enzyme and pathway databases

BioCycⁱ	EcoCyc:RED-THIOREDOXIN-MONOMER MetaCyc:RED-THIOREDOXIN-MONOMER

BioCycⁱ

EcoCyc:RED-THIOREDOXIN-MONOMER
MetaCyc:RED-THIOREDOXIN-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Thioredoxin 1 Short name: Trx-1
Gene namesⁱ	Name:trxA Synonyms:fipA, tsnC Ordered Locus Names:b3781, JW5856
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000120096	2 – 109	Thioredoxin 1Add BLAST		108

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Disulfide bondⁱ	33 ↔ 36	Redox-activePROSITE-ProRule annotation1 Publication
Modified residueⁱ	70	N6-acetyllysine1 Publication		1

Keywords - PTMⁱ

Acetylation, Disulfide bond

Proteomic databases

jPOSTⁱ	P0AA25
PaxDbⁱ	P0AA25
PRIDEⁱ	P0AA25

2D gel databases

SWISS-2DPAGEⁱ	P0AA25

SWISS-2DPAGEⁱ

P0AA25

PTM databases

CarbonylDBⁱ	P0AA25
iPTMnetⁱ	P0AA25

Interactionⁱ

Subunit structureⁱ

Monomer.

Interacts with bacteriophage T3 DNA polymerase.

1 Publication

Binary interactionsⁱ

Hide details

P0AA25

With	#Exp.	IntAct
trxB [P0A9P4]	2	EBI-368542,EBI-1029826
5 [P00581] from Escherichia phage T7.	2	EBI-368542,EBI-8664634
At2g44920 [O22160] from Arabidopsis thaliana.	2	EBI-368542,EBI-2895776
FKBP13 [Q9SCY2] from Arabidopsis thaliana.	2	EBI-368542,EBI-2895757
PPD6 [Q9LXX5] from Arabidopsis thaliana.	2	EBI-368542,EBI-2895738
PRXQ [Q9LU86] from Arabidopsis thaliana.	2	EBI-368542,EBI-540311
PSBO1 [P23321] from Arabidopsis thaliana.	2	EBI-368542,EBI-449414
PSBO2 [Q9S841] from Arabidopsis thaliana.	2	EBI-368542,EBI-449424
TL17 [P81760] from Arabidopsis thaliana.	2	EBI-368542,EBI-449573
TL29 [P82281] from Arabidopsis thaliana.	2	EBI-368542,EBI-2895799
VDE1 [Q39249] from Arabidopsis thaliana.	2	EBI-368542,EBI-2895666

Protein-protein interaction databases

BioGRIDⁱ	4263316, 300 interactors 852588, 8 interactors
Database of interacting proteins More...DIPⁱ	DIP-31856N
IntActⁱ	P0AA25, 99 interactors
STRINGⁱ	511145.b3781

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	5 – 8	Combined sources	4
Turnⁱ	10 – 12	Combined sources	3
Helixⁱ	13 – 16	Combined sources	4
Turnⁱ	17 – 19	Combined sources	3
Beta strandⁱ	22 – 29	Combined sources	8
Helixⁱ	34 – 49	Combined sources	16
Turnⁱ	50 – 53	Combined sources	4
Beta strandⁱ	55 – 60	Combined sources	6
Turnⁱ	61 – 63	Combined sources	3
Helixⁱ	65 – 70	Combined sources	6
Beta strandⁱ	75 – 83	Combined sources	9
Beta strandⁱ	86 – 93	Combined sources	8
Helixⁱ	97 – 105	Combined sources	9

Show more details

3D structure databases

BMRBⁱ	P0AA25
SASBDBⁱ	P0AA25
SMRⁱ	P0AA25
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0AA25

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	2 – 109	ThioredoxinPROSITE-ProRule annotationAdd BLAST		108

Sequence similaritiesⁱ

Belongs to the thioredoxin family.Curated

Keywords - Domainⁱ

Redox-active center

Phylogenomic databases

eggNOGⁱ	COG3118, Bacteria
HOGENOMⁱ	CLU_090389_10_2_6
InParanoidⁱ	P0AA25
PhylomeDBⁱ	P0AA25

Family and domain databases

InterProⁱ	View protein in InterPro IPR005746, Thioredoxin IPR036249, Thioredoxin-like_sf IPR017937, Thioredoxin_CS IPR013766, Thioredoxin_domain
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00085, Thioredoxin, 1 hit
PIRSFⁱ	PIRSF000077, Thioredoxin, 1 hit
SUPFAMⁱ	SSF52833, SSF52833, 1 hit
TIGRFAMsⁱ	TIGR01068, thioredoxin, 1 hit
PROSITEⁱ	View protein in PROSITE PS00194, THIOREDOXIN_1, 1 hit PS51352, THIOREDOXIN_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P0AA25-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY 
        60         70         80         90        100
QGKLTVAKLN IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL 

KEFLDANLA

Length:109

Mass (Da):11,807

Last modified:January 23, 2007 - v2

Checksum:ⁱEF5933EA29668EE9

GO

Sequence cautionⁱ

The sequence AAA24534 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

The sequence AAA67582 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	72 – 73	GI → IG AA sequence (PubMed:4883076).Curated		2
Sequence conflictⁱ	88	A → AS in AAA24696 (PubMed:1379743).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
PIRⁱ	A91519, TXEC
NCBI Reference Sequences More...RefSeqⁱ	NP_418228.2, NC_000913.3 WP_001280776.1, NZ_STEB01000021.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76786; AAC76786; b3781 BAE77517; BAE77517; BAE77517
GeneIDⁱ	64173577 948289
KEGGⁱ	ecj:JW5856 eco:b3781
PATRICⁱ	fig\|511145.12.peg.3896

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P0AA25	Thioredoxin 1	)	ECO57		109	UniRef100_P0AA27
Thioredoxin 1		ECOL6		109
Thioredoxin 1	)	SALTI		109
Thioredoxin 1	)	SALTY		109
Thioredoxin 1		SHIFL		109
+428

Protein	Similar proteins		Species	Score	Length	Source
P0AA25	Thioredoxin 1	)	ECO57		109	UniRef90_P0AA27
Thioredoxin 1		ECOL6		109
Thioredoxin 1	)	SALTI		109
Thioredoxin 1	)	SALTY		109
Thioredoxin 1		SHIFL		109
+428

Protein	Similar proteins		Species	Score	Length	Source
P0AA25	Thioredoxin 1	)	ECO57		109	UniRef50_P0AA27
Thioredoxin 1		ECOL6		109
Thioredoxin 1	)	SALTI		109
Thioredoxin 1	)	SALTY		109
Thioredoxin 1		SHIFL		109
+440

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
PIRⁱ	A91519, TXEC
RefSeqⁱ	NP_418228.2, NC_000913.3 WP_001280776.1, NZ_STEB01000021.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	2-109	[»]
	1M7T	NMR	-	A	32-108	[»]
	1OAZ	X-ray	2.78	A/B	2-109	[»]
	1SKR	X-ray	2.40	B	2-109	[»]
	1SKS	X-ray	2.30	B	2-109	[»]
	1SKW	X-ray	2.30	B	2-109	[»]
	1SL0	X-ray	3.20	B/D	2-109	[»]
	1SL1	X-ray	2.20	B	2-109	[»]
	1SL2	X-ray	2.30	B	2-109	[»]
	1SRX	X-ray	2.80	A	2-109	[»]
	1T7P	X-ray	2.20	B	2-109	[»]
	1T8E	X-ray	2.54	B	2-109	[»]
	1THO	X-ray	2.30	A	2-109	[»]
	1TK0	X-ray	2.30	B	2-109	[»]
	1TK5	X-ray	2.20	B	2-109	[»]
	1TK8	X-ray	2.50	B	2-109	[»]
	1TKD	X-ray	2.49	B	2-109	[»]
	1TXX	X-ray	2.20	A	2-109	[»]
	1X9M	X-ray	2.10	B	2-109	[»]
	1X9S	X-ray	2.70	B	2-109	[»]
	1X9W	X-ray	2.30	B	2-109	[»]
	1XOA	NMR	-	A	2-109	[»]
	1XOB	NMR	-	A	2-109	[»]
	1ZCP	X-ray	2.30	A/B/C/D	2-109	[»]
	1ZYQ	X-ray	2.70	B	2-109	[»]
	1ZZY	X-ray	2.50	A/B	2-109	[»]
	2AJQ	X-ray	2.60	B/I	2-109	[»]
	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	2-109	[»]
	2FD3	X-ray	2.45	A/B	2-109	[»]
	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	[»]
	4HU7	X-ray	1.40	A/B	2-109	[»]
	4HU9	X-ray	1.55	A	2-109	[»]
	4HUA	X-ray	1.10	A	2-109	[»]
	4X43	X-ray	1.65	A/B/C	2-109	[»]
	5HR0	X-ray	1.31	A/B	1-109	[»]
	5HR1	X-ray	2.14	A/B/C/D/E/F/G	1-107	[»]
	5HR2	X-ray	1.20	A	1-109	[»]
	5HR3	X-ray	1.10	A/B	1-109	[»]
	5XOC	X-ray	2.40	B	2-109	[»]
	6GD1	X-ray	2.01	A/B	1-109	[»]
	6GDG	electron microscopy	4.11	A	2-109	[»]
	6H7J	X-ray	2.80	E/F	2-109	[»]
	6H7L	X-ray	2.70	E/F	2-109	[»]
	6H7M	X-ray	2.76	E/F	2-109	[»]
	6H7N	X-ray	2.50	E/F	2-109	[»]
6H7O	X-ray	2.80	E/F	2-109	[»]
6IBL	X-ray	2.70	A/B	2-109	[»]
6LUR	X-ray	2.00	A/B/C/D/E/F/G/H	1-109	[»]
6N7W	electron microscopy	4.50	I	1-109	[»]
6P7E	X-ray	3.00	E/F/G/H	1-109	[»]
6Y4Y	X-ray	1.75	A/B/C/D	1-109	[»]
6Y4Z	X-ray	1.90	A/B/C/D	1-109	[»]
6YEV	X-ray	2.94	E/F/G	1-109	[»]
BMRBⁱ	P0AA25
SASBDBⁱ	P0AA25
SMRⁱ	P0AA25
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	4263316, 300 interactors 852588, 8 interactors
DIPⁱ	DIP-31856N
IntActⁱ	P0AA25, 99 interactors
STRINGⁱ	511145.b3781

PTM databases

CarbonylDBⁱ	P0AA25
iPTMnetⁱ	P0AA25

2D gel databases

SWISS-2DPAGEⁱ	P0AA25

SWISS-2DPAGEⁱ

P0AA25

Proteomic databases

jPOSTⁱ	P0AA25
PaxDbⁱ	P0AA25
PRIDEⁱ	P0AA25

Genome annotation databases

EnsemblBacteriaⁱ	AAC76786; AAC76786; b3781 BAE77517; BAE77517; BAE77517
GeneIDⁱ	64173577 948289
KEGGⁱ	ecj:JW5856 eco:b3781
PATRICⁱ	fig\|511145.12.peg.3896

Organism-specific databases

EchoBASEⁱ	EB1024

EchoBASEⁱ

EB1024

Phylogenomic databases

eggNOGⁱ	COG3118, Bacteria
HOGENOMⁱ	CLU_090389_10_2_6
InParanoidⁱ	P0AA25
PhylomeDBⁱ	P0AA25

Enzyme and pathway databases

BioCycⁱ	EcoCyc:RED-THIOREDOXIN-MONOMER MetaCyc:RED-THIOREDOXIN-MONOMER

BioCycⁱ

EcoCyc:RED-THIOREDOXIN-MONOMER
MetaCyc:RED-THIOREDOXIN-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P0AA25
Protein Ontology More...PROⁱ	PR:P0AA25

Family and domain databases

InterProⁱ	View protein in InterPro IPR005746, Thioredoxin IPR036249, Thioredoxin-like_sf IPR017937, Thioredoxin_CS IPR013766, Thioredoxin_domain
Pfamⁱ	View protein in Pfam PF00085, Thioredoxin, 1 hit
PIRSFⁱ	PIRSF000077, Thioredoxin, 1 hit
SUPFAMⁱ	SSF52833, SSF52833, 1 hit
TIGRFAMsⁱ	TIGR01068, thioredoxin, 1 hit
PROSITEⁱ	View protein in PROSITE PS00194, THIOREDOXIN_1, 1 hit PS51352, THIOREDOXIN_2, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	THIO_ECOLI
Accessionⁱ	P0AA25Primary (citable) accession number: P0AA25 Secondary accession number(s): P00274 , P76750, Q2M889, Q47674, Q8XAT2
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	January 23, 2007
	Last modified:	September 29, 2021
	This is version 153 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0AA25 (THIO_ECOLI)

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Thioredoxin 1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

Other locations

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P0AA25

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ