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Reviewed, UniProtKB/Swiss-Prot Q9ZL18 (TRXB_HELPJ)

Last modified June 16, 2009. Version 67. 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: jhp_0764
OrganismHelicobacter pylori J99 (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

electron carrier activity

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 – 311311Thioredoxin reductase
PRO_0000166734

Regions

Nucleotide binding31 – 399FAD By similarity
Nucleotide binding281 – 29010FAD By similarity

Amino acid modifications

Disulfide bond133 ↔ 136Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZL18-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 4F35C5407E56EC2E

FASTA31133,433
        10         20         30         40         50         60 
MIDCAIIGGG PAGLSAGLYA TRGGVKNAVL FEKGMPGGQI TGSSEIENYP GVKEVVSGLD 

        70         80         90        100        110        120 
FMQPWQEQCF RFGLKHEMTA IQRVSKKGSH FVILAEDGKT FEAKSVIIAT GGSPKRTGIK 

       130        140        150        160        170        180 
GESEYWGKGV STCATCDGFF YKNKEVAVLG GGDTAVEEAI YLANICKKVY LIHRRDGFRC 

       190        200        210        220        230        240 
APITLEHAKN NSKIEFLTPY VVEEIKGDAS GVSSLSIKNT ATNEKRELVV PGLFIFVGYD 

       250        260        270        280        290        300 
VNNAVLKQED NSMLCECDEY GSIVVDFSMK TNVQGLFAAG DIRIFAPKQV VCAASDGATA 

       310 
ALSVISYLEH H 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed: 9923682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE001439 Genomic DNA. Translation: AAD06343.1.
PIRD71890.
RefSeqNP_223482.1.

3D structure databases

HSSPHSSP built from PDB template 1VDC based on UniProtKB Q39243.
ModBaseSearch...

Genome annotation databases

GeneID890127.
GenomeReviewsGene locus jhp_0764 in contig AE001439_GR.
KEGGhpj:jhp0764.
NMPDRfig|85963.1.peg.760.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9ZL18.
OMAQ9ZL18. FVGYDVN.

Enzyme and pathway databases

BioCycHPYL85963:JHP0764-MON.
BRENDA1.8.1.9. 295085.

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...

Entry information

Entry nameTRXB_HELPJ
AccessionPrimary (citable) accession number: Q9ZL18
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 67 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

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