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Reviewed, UniProtKB/Swiss-Prot Q9ZD97 (TRXB_RICPR)

Last modified February 9, 2010. Version 66. 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

Names and origin

Protein namesRecommended name:
    Thioredoxin reductase
      Short name=TRXR
    EC=1.8.1.9
Gene names
Name: trxB
Ordered Locus Names: RP445
OrganismRickettsia prowazekii [Complete proteome] [HAMAP]
Taxonomic identifier782 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length310 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 – 310310Thioredoxin reductase
PRO_0000166743

Regions

Nucleotide binding34 – 418FAD By similarity
Nucleotide binding281 – 29010FAD By similarity

Amino acid modifications

Disulfide bond135 ↔ 138Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZD97-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 573CA975C750957D

FASTA31033,582
        10         20         30         40         50         60 
MKITTKVLII GSGPAGLSAA IYTARSALKP ILINGMQPGG QLTMTTDVEN YPGFAETIQG 

        70         80         90        100        110        120 
PWLMEQMSMQ AKNVGTEIIS DYVERVDLSK RPFKIFTGTG NEYEADSIII CTGAESKWLG 

       130        140        150        160        170        180 
IASEQEFRGF GVSSCAICDG FFFKNQEIVV VGGGNSALEE ALYLTNHANK VTVVHRRNSF 

       190        200        210        220        230        240 
RAEKILQDRL FKNPKISVIW DHIIDEIVGS NKPKAVTGVK IQNVYTNEIN LVNCSGVFIA 

       250        260        270        280        290        300 
IGHAPNTALF KGQIAIDDDN YIVTQSGSTR TNVEGVFAAG DVQDKIYRQA VTAAASGCMA 

       310 
ALEVAKFLNK 

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed: 9823893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235271 Genomic DNA. Translation: CAA14902.1.
PIRD71703.
RefSeqNP_220826.1.

3D structure databases

SMRQ9ZD97. Positions 4-310.
ModBaseSearch...

Genome annotation databases

GeneID883344.
KEGGrpr:RP445.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG669726.
OMAHCKLLIL.

Enzyme and pathway databases

BioCycRPRO272947:RP445-MONOMER.
BRENDA1.8.1.9. 141977.

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_RICPR
AccessionPrimary (citable) accession number: Q9ZD97
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: February 9, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

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