Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P94284 (TRXB_BORBU)

Last modified February 9, 2010. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
    Thioredoxin reductase
      Short name=TRXR
    EC=1.8.1.9
Gene names
Name: trxB
Ordered Locus Names: BB_0515
OrganismBorrelia burgdorferi (Lyme disease spirochete) [Complete proteome] [HAMAP]
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete 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

thioredoxin-disulfide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Thioredoxin reductase
PRO_0000166720

Regions

Nucleotide binding55 – 628FAD By similarity
Nucleotide binding298 – 30710FAD By similarity

Amino acid modifications

Disulfide bond156 ↔ 159Redox-active By similarity

Experimental info

Sequence conflict3031L → P in AAB41020. Ref.1
Sequence conflict315 – 32612FIASV…GNFLK → LLHLLS in AAB41020. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P94284-1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: E0F5AC6ACFFFFF3B

FASTA32635,673
        10         20         30         40         50         60 
MLEFETIDIN LTKKKNLSQK EVDFIEDVII VGSGPAGLTA GIYSVMSNYK AAILEGPEPG 

        70         80         90        100        110        120 
GQLTTTTEVY NYPGFKNGIS GRNLMLNMRE QVVNLGAKTF PETVFSIKRK GNIFYLYTEN 

       130        140        150        160        170        180 
YIYKSKAVII AVGSKPKKLE TLKNSGLFWN KGISVCAICD GHLFKGKRVA VIGGGNTALS 

       190        200        210        220        230        240 
ESIYLSKLVD KVYLIVRKNN LRAIAMLRDS VAKLPNIEIL YNSEAIEVDG KSSVSSVKIF 

       250        260        270        280        290        300 
NKKDNVVYEL EVSAVFMAVG YKPNTEFLKG FLDLDEEGFI VTKDVVKTSV DGVFSCGDVS 

       310        320 
NKLYAQAITA AAEGFIASVE LGNFLK 

« Hide

References

« Hide 'large scale' references
[1]"Phenylalanyl-tRNA synthetase genes (alpha and beta subunits) and thioredoxin reductase gene of Borrelia burgdorferi."
Barbour A.G., Hinnebusch J.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[2]"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi."
Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. expand/collapse author list , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C.
Nature 390:580-586(1997) [PubMed: 9403685] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82978 Genomic DNA. Translation: AAB41020.1.
AE000783 Genomic DNA. Translation: AAC66890.1.
PIRB70164.
RefSeqNP_212649.1.

3D structure databases

SMRP94284. Positions 25-326.
ModBaseSearch...

Genome annotation databases

GeneID1195361.
GenomeReviewsGene locus BB_0515 in contig AE000783_GR.
KEGGbbu:BB0515.
NMPDRfig|224326.1.peg.899.
TIGRBB_0515.

Phylogenomic databases

HOGENOMHBG669726.
OMACAICDGH.

Enzyme and pathway databases

BioCycBBUR224326:BB_0515-MONOMER.
BRENDA1.8.1.9. 142596.

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.
TIGRFAMsTIGR01292. TRX_reduct. 1 hit.
PROSITEPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRXB_BORBU
AccessionPrimary (citable) accession number: P94284
Secondary accession number(s): O51467
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 15, 1998
Last modified: February 9, 2010
This is version 76 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)

Relevant documents

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