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Reviewed, UniProtKB/Swiss-Prot P52214 (TRXB_MYCTU)

Last modified June 16, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

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

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Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

Sequence similarities

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

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Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

removal of superoxide radicals

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

thioredoxin-disulfide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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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...

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Sequences

Sequence LengthMass (Da)Tools
P52214-1 [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

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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: 9634230] [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: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X95798 Genomic DNA. Translation: CAA65070.1.
BX842584 Genomic DNA. Translation: CAA16226.1.
AE000516 Genomic DNA. Translation: AAK48397.1.
PIRA70851.
RefSeqNP_218430.1.
NP_338583.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2A87X-ray3.00A/B1-335[»]
ModBaseSearch...

Genome annotation databases

GeneID886232.
926658.
GenomeReviewsGene locus MT4032 in contig AE000516_GR.
Gene locus Rv3913 in contig AL123456_GR.
KEGGmtc:MT4032.
mtu:Rv3913.
TIGRMT4032.

Organism-specific databases

TubercuListRv3913.

Phylogenomic databases

HOGENOMP52214.
OMAP52214. PSCGPCH.

Enzyme and pathway databases

BRENDA1.8.1.9. 809.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
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.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01292. TRX_reduct. 1 hit.
PROSITEPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameTRXB_MYCTU
AccessionPrimary (citable) accession number: P52214
Secondary accession number(s): O53592
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1999
Last modified: June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents