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Protein

Thioredoxin reductase

Gene

trxB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 518FADBy similarity
Nucleotide bindingi288 – 29710FADBy similarity

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: MTBBASE
  • NADPH binding Source: MTBBASE
  • protein disulfide oxidoreductase activity Source: MTBBASE
  • thioredoxin-disulfide reductase activity Source: MTBBASE

GO - Biological processi

  • cell redox homeostasis Source: MTBBASE
  • growth Source: MTBBASE
  • removal of superoxide radicals Source: InterPro
  • response to hypoxia Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiR-HSA-1222541. Cell redox homeostasis.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase (EC:1.8.1.9)
Short name:
TR
Short name:
TRXR
Gene namesi
Name:trxB
Synonyms:trxB2
Ordered Locus Names:Rv3913
ORF Names:MTV028.04
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3913.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2390811.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 335334Thioredoxin reductasePRO_0000166741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources
Disulfide bondi145 ↔ 148Redox-activeBy similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP9WHH1.

Expressioni

Inductioni

Expressed following oxidative stress under control of SigH.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi83332.Rv3913.

Chemistry

BindingDBiP9WHH1.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 206Combined sources
Helixi23 – 3513Combined sources
Beta strandi41 – 433Combined sources
Helixi51 – 533Combined sources
Helixi70 – 8314Combined sources
Beta strandi87 – 893Combined sources
Beta strandi93 – 975Combined sources
Beta strandi99 – 1079Combined sources
Beta strandi112 – 1209Combined sources
Beta strandi124 – 1263Combined sources
Helixi133 – 1364Combined sources
Turni139 – 1413Combined sources
Beta strandi142 – 1443Combined sources
Helixi146 – 1494Combined sources
Helixi150 – 1534Combined sources
Beta strandi157 – 1615Combined sources
Helixi165 – 17410Combined sources
Turni175 – 1773Combined sources
Beta strandi179 – 1846Combined sources
Beta strandi186 – 1894Combined sources
Helixi196 – 2027Combined sources
Beta strandi206 – 2094Combined sources
Beta strandi211 – 2188Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi225 – 2317Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi250 – 2523Combined sources
Turni255 – 2573Combined sources
Beta strandi275 – 2773Combined sources
Beta strandi283 – 2853Combined sources
Helixi287 – 2893Combined sources
Helixi297 – 32024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A87X-ray3.00A/B1-335[»]
ProteinModelPortaliP9WHH1.
SMRiP9WHH1. Positions 10-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105C3M. Bacteria.
COG0492. LUCA.
KOiK00384.
OMAiGQLEMNN.
PhylomeDBiP9WHH1.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P9WHH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAPPVHDRA HHPVRDVIVI GSGPAGYTAA LYAARAQLAP LVFEGTSFGG
60 70 80 90 100
ALMTTTDVEN YPGFRNGITG PELMDEMREQ ALRFGADLRM EDVESVSLHG
110 120 130 140 150
PLKSVVTADG QTHRARAVIL AMGAAARYLQ VPGEQELLGR GVSSCATCDG
160 170 180 190 200
FFFRDQDIAV IGGGDSAMEE ATFLTRFARS VTLVHRRDEF RASKIMLDRA
210 220 230 240 250
RNNDKIRFLT NHTVVAVDGD TTVTGLRVRD TNTGAETTLP VTGVFVAIGH
260 270 280 290 300
EPRSGLVREA IDVDPDGYVL VQGRTTSTSL PGVFAAGDLV DRTYRQAVTA
310 320 330
AGSGCAAAID AERWLAEHAA TGEADSTDAL IGAQR
Length:335
Mass (Da):35,643
Last modified:April 16, 2014 - v1
Checksum:i3D0DD581E6C187E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251A → R in CAA65070 (Ref. 1) Curated
Sequence conflicti215 – 2151V → C in CAA65070 (Ref. 1) Curated
Sequence conflicti228 – 2281V → Y in CAA65070 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95798 Genomic DNA. Translation: CAA65070.1.
AL123456 Genomic DNA. Translation: CCP46742.1.
PIRiA70851.
RefSeqiNP_218430.1. NC_000962.3.
WP_003900782.1. NZ_KK339374.1.

Genome annotation databases

EnsemblBacteriaiCCP46742; CCP46742; Rv3913.
GeneIDi886232.
KEGGimtu:Rv3913.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95798 Genomic DNA. Translation: CAA65070.1.
AL123456 Genomic DNA. Translation: CCP46742.1.
PIRiA70851.
RefSeqiNP_218430.1. NC_000962.3.
WP_003900782.1. NZ_KK339374.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A87X-ray3.00A/B1-335[»]
ProteinModelPortaliP9WHH1.
SMRiP9WHH1. Positions 10-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3913.

Chemistry

BindingDBiP9WHH1.
ChEMBLiCHEMBL2390811.

Proteomic databases

PaxDbiP9WHH1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46742; CCP46742; Rv3913.
GeneIDi886232.
KEGGimtu:Rv3913.

Organism-specific databases

TubercuListiRv3913.

Phylogenomic databases

eggNOGiENOG4105C3M. Bacteria.
COG0492. LUCA.
KOiK00384.
OMAiGQLEMNN.
PhylomeDBiP9WHH1.

Enzyme and pathway databases

ReactomeiR-HSA-1222541. Cell redox homeostasis.

Miscellaneous databases

PROiP9WHH1.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRXB_MYCTU
AccessioniPrimary (citable) accession number: P9WHH1
Secondary accession number(s): L0TFM3, O53592, P52214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: June 8, 2016
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.
Was identified as a high-confidence drug target.

Keywords - Technical termi

3D-structure, Complete proteome, 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.