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Reviewed, UniProtKB/Swiss-Prot Q9PKT7 (TRXB_CHLMU)

Last modified June 16, 2009. Version 61. 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: TC_0375
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [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_0000166724

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
Q9PKT7-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 53824B207C24158D

FASTA31233,556
        10         20         30         40         50         60 
MTHVKLAIIG SGPAGYTAAI YASRALLTPI LFEGFFSGIA GGQLMTTTEV ENFPGFPQGV 

        70         80         90        100        110        120 
LGHQLMENMK MQAQRFGTQV IAKDITSVDF SVRPFVLKSG EDTFTCDACI IATGASAKRL 

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

       190        200        210        220        230        240 
RRDTLRASKA MVNKAQANEK IVFLWNSEVV KILGDSLVRS IDIFNNVEKT TVTMEAAGVF 

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

       310 
MAALDAERFL EK 

« Hide

Cross-references

Sequence databases

AE002160 Genomic DNA. Translation: AAF39233.1.
PIRC81710.
RefSeqNP_296753.1.

3D structure databases

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

Genome annotation databases

GeneID1245727.
GenomeReviewsGene locus TC_0375 in contig AE002160_GR.
KEGGcmu:TC0375.
TIGRTC_0375.

Phylogenomic databases

HOGENOMQ9PKT7.
OMAQ9PKT7. PSCGPCH.

Enzyme and pathway databases

BioCycCMUR243161:TC_0375-MON.
BRENDA1.8.1.9. 256349.

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_CHLMU
AccessionPrimary (citable) accession number: Q9PKT7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 61 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