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Reviewed, UniProtKB/Swiss-Prot O84101 (TRXB_CHLTR)

Last modified June 16, 2009. Version 64. 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: CT_099
OrganismChlamydia trachomatis [Complete proteome] [HAMAP]
Taxonomic identifier813 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia

Protein attributes

Sequence length312 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 – 312312Thioredoxin reductase
PRO_0000166726

Regions

Nucleotide binding33 – 4311FAD By similarity
Nucleotide binding283 – 29210FAD By similarity

Amino acid modifications

Disulfide bond138 ↔ 141Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O84101-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 729D0D22F8FA0A39

FASTA31233,508
        10         20         30         40         50         60 
MTHAKLVIIG SGPAGYTAAI YASRALLTPV LFEGFFSGIA GGQLMTTTEV ENFPGFPEGV 

        70         80         90        100        110        120 
LGHQLMDLMK TQAQRFGTQV LSKDITAVDF SVRPFVLKSG KETFTCDACI IATGASAKRL 

       130        140        150        160        170        180 
SIPGAGDNEF WQKGVTACAV CDGASPIFRD KDLFVVGGGD SALEEAMFLT RYGKRVFVVH 

       190        200        210        220        230        240 
RRDTLRASKV MVNKAQANEK IFFLWNSEIV KISGDTLVRS IDIYNNVDET TTTMEAAGVF 

       250        260        270        280        290        300 
FAIGHQPNTA FLGGQVALDE NGYIITEKGS SRTSVPGVFA AGDVQDKYYR QAITSAGSGC 

       310 
MAALDAERFL EN 

« Hide

References

[1]"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
Science 282:754-759(1998) [PubMed: 9784136] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.

Cross-references

Sequence databases

AE001273 Genomic DNA. Translation: AAC67690.1. Different initiation.
PIRB71556.
RefSeqNP_219602.1.

3D structure databases

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

2-D gel databases

PHCI-2DPAGEO84101.

Genome annotation databases

GeneID884181.
GenomeReviewsGene locus CT_099 in contig AE001273_GR.
KEGGctr:CT099.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO84101.

Enzyme and pathway databases

BioCycCTRA315277:CT099-MON.
BRENDA1.8.1.9. 108.

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_CHLTR
AccessionPrimary (citable) accession number: O84101
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: June 16, 2009
This is version 64 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