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Protein

Thioredoxin

Gene

trxA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 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.By similarity

GO - Molecular functioni

  • disulfide oxidoreductase activity Source: MTBBASE
  • electron carrier activity Source: MTBBASE
  • glutathione disulfide oxidoreductase activity Source: MTBBASE
  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: GO_Central
  • protein disulfide oxidoreductase activity Source: MTBBASE
  • S-nitrosoglutathione reductase activity Source: MTBBASE

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-1222538. Tolerance by Mtb to nitric oxide produced by macrophages.
R-HSA-1222541. Cell redox homeostasis.
R-MTU-936721. Cysteine synthesis from O-acetylserine.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin
Short name:
Trx
Alternative name(s):
MPT46
Gene namesi
Name:trxA
Synonyms:trx, trxC
Ordered Locus Names:Rv3914
ORF Names:MTV028.05
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3914.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • extracellular region Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 116115ThioredoxinPRO_0000120117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi37 ↔ 40Redox-activePROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP9WG67.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv3914.

Structurei

Secondary structure

1
116
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53Combined sources
Beta strandi9 – 113Combined sources
Turni14 – 163Combined sources
Helixi17 – 204Combined sources
Turni21 – 233Combined sources
Beta strandi28 – 336Combined sources
Helixi38 – 5316Combined sources
Turni54 – 574Combined sources
Beta strandi59 – 646Combined sources
Turni65 – 673Combined sources
Helixi69 – 746Combined sources
Beta strandi79 – 879Combined sources
Beta strandi90 – 978Combined sources
Helixi101 – 1077Combined sources
Turni109 – 1113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I1UX-ray1.30A1-116[»]
2L4QNMR-A1-116[»]
2L59NMR-A1-116[»]
3O6TX-ray2.40A/B/C/D1-116[»]
ProteinModelPortaliP9WG67.
SMRiP9WG67. Positions 7-114.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 113112ThioredoxinPROSITE-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.
KOiK03671.
OMAiMPKQKIL.
PhylomeDBiP9WG67.

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.

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

P9WG67-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDSEKSATI KVTDASFATD VLSSNKPVLV DFWATWCGPC KMVAPVLEEI
60 70 80 90 100
ATERATDLTV AKLDVDTNPE TARNFQVVSI PTLILFKDGQ PVKRIVGAKG
110
KAALLRELSD VVPNLN
Length:116
Mass (Da):12,544
Last modified:April 16, 2014 - v1
Checksum:i3B7B9AC90B44B571
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95798 Genomic DNA. Translation: CAA65071.1.
AL123456 Genomic DNA. Translation: CCP46743.1.
PIRiB70851.
RefSeqiNP_218431.1. NC_000962.3.
WP_003400164.1. NZ_KK339374.1.

Genome annotation databases

EnsemblBacteriaiCCP46743; CCP46743; Rv3914.
GeneIDi886241.
KEGGimtu:Rv3914.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95798 Genomic DNA. Translation: CAA65071.1.
AL123456 Genomic DNA. Translation: CCP46743.1.
PIRiB70851.
RefSeqiNP_218431.1. NC_000962.3.
WP_003400164.1. NZ_KK339374.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I1UX-ray1.30A1-116[»]
2L4QNMR-A1-116[»]
2L59NMR-A1-116[»]
3O6TX-ray2.40A/B/C/D1-116[»]
ProteinModelPortaliP9WG67.
SMRiP9WG67. Positions 7-114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3914.

Proteomic databases

PaxDbiP9WG67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46743; CCP46743; Rv3914.
GeneIDi886241.
KEGGimtu:Rv3914.

Organism-specific databases

TubercuListiRv3914.

Phylogenomic databases

eggNOGiENOG4105K63. Bacteria.
COG0526. LUCA.
KOiK03671.
OMAiMPKQKIL.
PhylomeDBiP9WG67.

Enzyme and pathway databases

ReactomeiR-HSA-1222538. Tolerance by Mtb to nitric oxide produced by macrophages.
R-HSA-1222541. Cell redox homeostasis.
R-MTU-936721. Cysteine synthesis from O-acetylserine.

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

« Hide 'large scale' publications
  1. "Sequence analysis and functional characterization of thioredoxin and thioredoxin reductase of Mycobacterium tuberculosis."
    Wieles B., Phillip W., Drijfhout J.W., Offringa R., Ottenhoff T.H.M.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  3. "Identification and functional characterization of thioredoxin of Mycobacterium tuberculosis."
    Wieles B., Nagai S., Wiker H.G., Harboe M., Ottenhoff T.H.M.
    Infect. Immun. 63:4946-4948(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), DISULFIDE BOND.

Entry informationi

Entry nameiTHIO_MYCTU
AccessioniPrimary (citable) accession number: P9WG67
Secondary accession number(s): L0TDX8, P0A616, P52229
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: April 13, 2016
This is version 19 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.