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Protein

Thioredoxin

Gene

trxA

Organism
Alicyclobacillus acidocaldarius (Bacillus acidocaldarius)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin
Short name:
Trx
Gene namesi
Name:trxA
OrganismiAlicyclobacillus acidocaldarius (Bacillus acidocaldarius)
Taxonomic identifieri1388 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesAlicyclobacillaceaeAlicyclobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 105105ThioredoxinPRO_0000120072Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 32Redox-activePROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi1048834.TC41_0867.

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Turni7 – 93Combined sources
Helixi10 – 145Combined sources
Beta strandi15 – 184Combined sources
Beta strandi20 – 256Combined sources
Helixi30 – 4516Combined sources
Turni47 – 493Combined sources
Beta strandi51 – 566Combined sources
Turni57 – 593Combined sources
Helixi61 – 666Combined sources
Beta strandi71 – 799Combined sources
Beta strandi82 – 898Combined sources
Helixi93 – 997Combined sources
Turni100 – 1045Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NSWX-ray1.90A/B/C/D1-105[»]
1NW2X-ray1.90A/B/C/D/E/F/G/H1-105[»]
1QUWNMR-A1-105[»]
1RQMNMR-A1-105[»]
ProteinModelPortaliP80579.
SMRiP80579. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80579.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 105105ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105K63. Bacteria.
COG0526. LUCA.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80579-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ATMTLTDANF QQAIQGDKPV LVDFWAAWCG PCRMMAPVLE EFAEAHADKV
60 70 80 90 100
TVAKLNVDEN PETTSQFGIM SIPTLILFKG GRPVKQLIGY QPKEQLEAQL

ADVLQ
Length:105
Mass (Da):11,576
Last modified:October 1, 1996 - v1
Checksum:iE03F636DFB3C3745
GO

Mass spectrometryi

Molecular mass is 11577 Da from positions 1 - 105. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NSWX-ray1.90A/B/C/D1-105[»]
1NW2X-ray1.90A/B/C/D/E/F/G/H1-105[»]
1QUWNMR-A1-105[»]
1RQMNMR-A1-105[»]
ProteinModelPortaliP80579.
SMRiP80579. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1048834.TC41_0867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105K63. Bacteria.
COG0526. LUCA.

Miscellaneous databases

EvolutionaryTraceiP80579.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Thioredoxin from Bacillus acidocaldarius: characterization, high-level expression in Escherichia coli and molecular modelling."
    Bartolucci S., Guagliardi A., Pedone E., de Pascale D., Cannio R., Camardella L., Rossi M., Nicastro G., de Chiara C., Facci P., Mascetti G., Nicolini C.
    Biochem. J. 328:277-285(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, CHARACTERIZATION, DISULFIDE BOND, MASS SPECTROMETRY.
  2. "NMR solution structure of a novel thioredoxin from bacillus acidocaldarius possible determinants of protein stability."
    Nicastro G., De Chiara C., Pedone E., Tato M., Rossi M., Bartolucci S.
    Eur. J. Biochem. 267:403-413(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  3. "An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius."
    Bartolucci S., De Simone G., Galdiero S., Improta R., Menchise V., Pedone C., Pedone E., Saviano M.
    J. Bacteriol. 185:4285-4289(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiTHIO_ALIAC
AccessioniPrimary (citable) accession number: P80579
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 11, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.