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Reviewed, UniProtKB/Swiss-Prot P75531 (TRXB_MYCPN)

Last modified February 9, 2010. Version 74. 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: MPN_240
ORF Names: MP591
OrganismMycoplasma pneumoniae [Complete proteome] [HAMAP]
Taxonomic identifier2104 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length315 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 – 315315Thioredoxin reductase
PRO_0000166738

Regions

Nucleotide binding45 – 528FAD By similarity
Nucleotide binding288 – 29710FAD By similarity

Amino acid modifications

Disulfide bond145 ↔ 148Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P75531-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 7155E4AF8D2A2EE7

FASTA31534,532
        10         20         30         40         50         60 
MLKVKSDFLT KDQVIYDVAI VGAGPAGIAA GIYGKRANLN LAIIEGSTPG GKVVKTNIVE 

        70         80         90        100        110        120 
NYPGYKSITG PDLGLEMYNH LIDLEPTFFY ANLIKLDKAA DTFILYLDDK TVVFAKTVIY 

       130        140        150        160        170        180 
ATGMLERKLG VAKEDHFYGK GISYCAICDG SLYKDQVVGV VGGGNSAIQE ALYLASMAKT 

       190        200        210        220        230        240 
VHLIHRREGF RADETALNKL RNLPNVVFHL NYTVKELLGN NTLNGIVLQN TLDHSTKQID 

       250        260        270        280        290        300 
LNCVFPYIGF ESITKPVEHL NLKLDPQGFL ITNEQMETSL KGLFAAGDCR SKHFRQIGTA 

       310 
INDGIIAVLT IRDVL 

« Hide

References

« Hide 'large scale' references
[1]"The thioredoxin reductase system of mycoplasmas."
Ben-Menachem G., Himmelreich R., Herrmann R., Aharonowitz Y., Rottem S.
Microbiology 143:1933-1940(1997) [PubMed: 9202470] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29342 / M129.
[2]"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
Nucleic Acids Res. 24:4420-4449(1996) [PubMed: 8948633] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29342 / M129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51988 Genomic DNA. Translation: AAC45451.1.
U00089 Genomic DNA. Translation: AAB96239.1.
PIRS73917.
RefSeqNP_109928.1.

3D structure databases

SMRP75531. Positions 16-313.
ModBaseSearch...

Genome annotation databases

GeneID877259.
GenomeReviewsGene locus MPN_240 in contig U00089_GR.
KEGGmpn:MPN240.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG669726.
OMASYTIENY.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-543.
MPNE272634:MPN240-MONOMER.
BRENDA1.8.1.9. 39500.

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_MYCPN
AccessionPrimary (citable) accession number: P75531
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: February 9, 2010
This is version 74 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

Mycoplasma pneumoniae

Mycoplasma pneumoniae (strain M129): 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