Skip Header

Contribute Send feedback
Read comments (?) or add your own

P52214 (TRXB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thioredoxin reductase
Short name=TR
Short name=TRXR
EC=1.8.1.9
Gene names
Name:trxB
Ordered Locus Names:Rv3913, MT4032
ORF Names:MTV028.04
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond.

Was identified as a high-confidence drug target.

Sequence similarities

Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335Thioredoxin reductase
PRO_0000166741

Regions

Nucleotide binding44 – 518FAD By similarity
Nucleotide binding288 – 29710FAD By similarity

Amino acid modifications

Disulfide bond145 ↔ 148Redox-active By similarity

Experimental info

Sequence conflict1251A → R in CAA65070. Ref.1
Sequence conflict2151V → C in CAA65070. Ref.1
Sequence conflict2281V → Y in CAA65070. Ref.1

Secondary structure

1 ................................................................ 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52214 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 3D0DD581E6C187E2

FASTA33535,643
        10         20         30         40         50         60 
MTAPPVHDRA HHPVRDVIVI GSGPAGYTAA LYAARAQLAP LVFEGTSFGG ALMTTTDVEN 

        70         80         90        100        110        120 
YPGFRNGITG PELMDEMREQ ALRFGADLRM EDVESVSLHG PLKSVVTADG QTHRARAVIL 

       130        140        150        160        170        180 
AMGAAARYLQ VPGEQELLGR GVSSCATCDG FFFRDQDIAV IGGGDSAMEE ATFLTRFARS 

       190        200        210        220        230        240 
VTLVHRRDEF RASKIMLDRA RNNDKIRFLT NHTVVAVDGD TTVTGLRVRD TNTGAETTLP 

       250        260        270        280        290        300 
VTGVFVAIGH EPRSGLVREA IDVDPDGYVL VQGRTTSTSL PGVFAAGDLV DRTYRQAVTA 

       310        320        330 
AGSGCAAAID AERWLAEHAA TGEADSTDAL IGAQR

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis and funtional 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]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[3]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[4]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X95798 Genomic DNA. Translation: CAA65070.1.
BX842584 Genomic DNA. Translation: CAA16226.1.
AE000516 Genomic DNA. Translation: AAK48397.1.
AL123456 Genomic DNA. Translation: CCP46742.1.
PIRA70851.
RefSeqNP_218430.1. NC_000962.3.
NP_338583.1. NC_002755.2.
YP_006517414.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A87X-ray3.00A/B1-335[»]
ProteinModelPortalP52214.
SMRP52214. Positions 10-322.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv3913.

Proteomic databases

PRIDEP52214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK48397; AAK48397; MT4032.
GeneID13317541.
886232.
926658.
KEGGmtc:MT4032.
mtu:Rv3913.
mtv:RVBD_3913.
PATRIC18130625. VBIMycTub22151_4400.

Organism-specific databases

TubercuListRv3913.

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHOG000072912.
KOK00384.
OMAVMGAFIA.
ProtClustDBCLSK792809.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00469. PNDRDTASEII.
TIGRFAMsTIGR01292. TRX_reduct. 1 hit.
PROSITEPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52214.

Entry information

Entry nameTRXB_MYCTU
AccessionPrimary (citable) accession number: P52214
Secondary accession number(s): L0TFM3, O53592
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1999
Last modified: May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents