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Protein

Bifunctional thioredoxin reductase/thioredoxin

Gene

trxB/A

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi41 – 48FADBy similarity8
Nucleotide bindingi285 – 294FADBy similarity10

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional thioredoxin reductase/thioredoxin
Including the following 2 domains:
Thioredoxin reductase (EC:1.8.1.9)
Short name:
TRXR
Thioredoxin
Gene namesi
Name:trxB/A
Synonyms:trx
Ordered Locus Names:ML2703
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML2703.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001667581 – 458Bifunctional thioredoxin reductase/thioredoxinAdd BLAST458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi142 ↔ 145Redox-activePROSITE-ProRule annotation
Disulfide bondi379 ↔ 382Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi272631.ML2703.

Structurei

3D structure databases

ProteinModelPortaliP46843.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini341 – 455ThioredoxinPROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 321Thioredoxin reductaseAdd BLAST321
Regioni322 – 347LinkerAdd BLAST26

Sequence similaritiesi

In the N-terminal section; belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105C3M. Bacteria.
COG0492. LUCA.
COG0526. LUCA.
HOGENOMiHOG000072912.
KOiK00384.
K03671.
OMAiGQLEMNN.
OrthoDBiPOG091H02HU.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
TIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46843-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTTPSAHET IHEVIVIGSG PAGYTAALYA ARAQLTPLVF EGTSFGGALM
60 70 80 90 100
TTTEVENYPG FRNGITGPEL MDDMREQALR FGAELRTEDV ESVSLRGPIK
110 120 130 140 150
SVVTAEGQTY QARAVILAMG TSVRYLQIPG EQELLGRGVS ACATCDGSFF
160 170 180 190 200
RGQDIAVIGG GDSAMEEALF LTRFARSVTL VHRRDEFRAS KIMLGRARNN
210 220 230 240 250
DKIKFITNHT VVAVNGYTTV TGLRLRNTTT GEETTLVVTG VFVAIGHEPR
260 270 280 290 300
SSLVSDVVDI DPDGYVLVKG RTTSTSMDGV FAAGDLVDRT YRQAITAAGS
310 320 330 340 350
GCAAAIDAER WLAEHAGSKA NETTEETGDV DSTDTTDWST AMTDAKNAGV
360 370 380 390 400
TIEVTDASFF ADVLSSNKPV LVDFWATWCG PCKMVAPVLE EIASEQRNQL
410 420 430 440 450
TVAKLDVDTN PEMAREFQVV SIPTMILFQG GQPVKRIVGA KGKAALLRDL

SDVVPNLN
Length:458
Mass (Da):49,046
Last modified:November 1, 1995 - v1
Checksum:i84D367AB31899987
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39923 Genomic DNA. Translation: AAB53131.1.
X87899 Genomic DNA. Translation: CAA61150.1.
AL583926 Genomic DNA. Translation: CAC32235.1.
PIRiS77662.
RefSeqiNP_302724.1. NC_002677.1.
WP_010909042.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC32235; CAC32235; CAC32235.
GeneIDi910819.
KEGGimle:ML2703.
PATRICi18060585. VBIMycLep78757_5206.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39923 Genomic DNA. Translation: AAB53131.1.
X87899 Genomic DNA. Translation: CAA61150.1.
AL583926 Genomic DNA. Translation: CAC32235.1.
PIRiS77662.
RefSeqiNP_302724.1. NC_002677.1.
WP_010909042.1. NC_002677.1.

3D structure databases

ProteinModelPortaliP46843.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML2703.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC32235; CAC32235; CAC32235.
GeneIDi910819.
KEGGimle:ML2703.
PATRICi18060585. VBIMycLep78757_5206.

Organism-specific databases

LepromaiML2703.

Phylogenomic databases

eggNOGiENOG4105C3M. Bacteria.
COG0492. LUCA.
COG0526. LUCA.
HOGENOMiHOG000072912.
KOiK00384.
K03671.
OMAiGQLEMNN.
OrthoDBiPOG091H02HU.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
TIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRXB_MYCLE
AccessioniPrimary (citable) accession number: P46843
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 5, 2016
This is version 131 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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.