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Protein

Thioredoxin reductase

Gene

trxB

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 429FADBy similarity
Nucleotide bindingi279 – 28810FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase (EC:1.8.1.9)
Short name:
TRXR
Gene namesi
Name:trxB
Ordered Locus Names:SCO3890
ORF Names:SCH24.12c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 322321Thioredoxin reductasePRO_0000166753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi136 ↔ 139Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP52215.

Expressioni

Inductioni

Expressed from 2 promoters, 1 of which (trxBp1) is under control of SigR, and further transiently induced (about 50-fold) by the thiol-oxidizing agent diamide. Part of the trxB-trxA operon.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi100226.SCO3890.

Structurei

3D structure databases

ProteinModelPortaliP52215.
SMRiP52215. Positions 4-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105C3M. Bacteria.
COG0492. LUCA.
HOGENOMiHOG000072912.
InParanoidiP52215.
KOiK00384.
OrthoDBiEOG65XN2W.
PhylomeDBiP52215.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52215-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDVRNVIII GSGPAGYTAA LYTARASLKP LVFEGAVTAG GALMNTTEVE
60 70 80 90 100
NFPGFQDGIM GPELMDNMRA QAERFGAELI PDDVVAVDLS GEIKTVTDTA
110 120 130 140 150
GTVHRAKAVI VTTGSQHRKL GLPNEDALSG RGVSWCATCD GFFFKDQDIA
160 170 180 190 200
VIGGGDTAME EATFLSRFAK SVTIVHRRDT LRASKAMQER AFADPKISFV
210 220 230 240 250
WDSEVAEVQG DQKLAGLKLR NVKTGELSDL PVTGLFIAIG HDPRTELFKG
260 270 280 290 300
QLDLDPEGYL KVDAPSTRTN LTGVFGAGDV VDHTYRQAIT AAGTGCSAAV
310 320
DAEPFLAALS DEDKAEPEKT AV
Length:322
Mass (Da):34,156
Last modified:January 23, 2007 - v3
Checksum:i1B337B1742E3C457
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261A → R in CAA63075 (PubMed:9795152).Curated
Sequence conflicti26 – 261A → R in CAA07451 (PubMed:9795152).Curated
Sequence conflicti73 – 742ER → DG in CAA63075 (PubMed:9795152).Curated
Sequence conflicti73 – 742ER → DG in CAA07451 (PubMed:9795152).Curated
Sequence conflicti155 – 1551Missing in CAA63075 (PubMed:9795152).Curated
Sequence conflicti234 – 2341G → A in CAA63075 (PubMed:9795152).Curated
Sequence conflicti258 – 2581Missing in CAA63075 (PubMed:9795152).Curated
Sequence conflicti300 – 3001V → L in CAB42713 (PubMed:12000953).Curated
Sequence conflicti304 – 3041P → R in CAB42713 (PubMed:12000953).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92105 Genomic DNA. Translation: CAA63076.1.
X92104 Genomic DNA. Translation: CAA63075.1.
AJ007313 Genomic DNA. Translation: CAA07451.1.
AL939118 Genomic DNA. Translation: CAB42713.1.
PIRiT36577.
T42062.
RefSeqiNP_628076.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB42713; CAB42713; CAB42713.
GeneIDi1099326.
KEGGisco:SCO3890.
PATRICi23737564. VBIStrCoe124346_3963.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92105 Genomic DNA. Translation: CAA63076.1.
X92104 Genomic DNA. Translation: CAA63075.1.
AJ007313 Genomic DNA. Translation: CAA07451.1.
AL939118 Genomic DNA. Translation: CAB42713.1.
PIRiT36577.
T42062.
RefSeqiNP_628076.1. NC_003888.3.

3D structure databases

ProteinModelPortaliP52215.
SMRiP52215. Positions 4-307.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO3890.

Proteomic databases

PRIDEiP52215.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB42713; CAB42713; CAB42713.
GeneIDi1099326.
KEGGisco:SCO3890.
PATRICi23737564. VBIStrCoe124346_3963.

Phylogenomic databases

eggNOGiENOG4105C3M. Bacteria.
COG0492. LUCA.
HOGENOMiHOG000072912.
InParanoidiP52215.
KOiK00384.
OrthoDBiEOG65XN2W.
PhylomeDBiP52215.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene organization in the trxA/B-oriC region of the Streptomyces coelicolor chromosome and comparison with other eubacteria."
    Gal-Mor O., Borovok I., Av-Gay Y., Cohen G., Aharonowitz Y.
    Gene 217:83-90(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.
  2. Aharonowitz Y.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.
  4. "sigmaR, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2)."
    Paget M.S., Kang J.G., Roe J.H., Buttner M.J.
    EMBO J. 17:5776-5782(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiTRXB_STRCO
AccessioniPrimary (citable) accession number: P52215
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.