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Reviewed, UniProtKB/Swiss-Prot P39916 (TRXB_COXBU)

Last modified November 24, 2009. Version 76. 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: CBU_1193
OrganismCoxiella burnetii [Complete proteome] [HAMAP]
Taxonomic identifier777 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length320 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

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 – 320320Thioredoxin reductase
PRO_0000166728

Regions

Nucleotide binding36 – 438FAD By similarity
Nucleotide binding287 – 29610FAD By similarity

Amino acid modifications

Disulfide bond136 ↔ 139Redox-active By similarity

Experimental info

Sequence conflict211A → D in CAA53288. Ref.1
Sequence conflict251A → V in CAA53288. Ref.1
Sequence conflict511D → A in CAA53288. Ref.1
Sequence conflict64 – 663QLM → KLL in CAA53288. Ref.1
Sequence conflict74 – 774ERLD → GGALN in CAA53288. Ref.1
Sequence conflict87 – 882EA → KP in CAA53288. Ref.1
Sequence conflict921Q → P in CAA53288. Ref.1
Sequence conflict981K → Q in CAA53288. Ref.1
Sequence conflict1271A → P in CAA53288. Ref.1
Sequence conflict1461G → A in CAA53288. Ref.1
Sequence conflict1581A → S in CAA53288. Ref.1
Sequence conflict284 – 2929AAGDVTDHV → PAVVVRGQL in CAA53288. Ref.1
Sequence conflict296 – 2983AIT → TIA in CAA53288. Ref.1
Sequence conflict3061A → P in CAA53288. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P39916-1 [UniParc].

Last modified May 9, 2003. Version 2.
Checksum: 750851B6FDDEB5E3

FASTA32034,620
        10         20         30         40         50         60 
MNKPQHHSLI ILGSGPAGYT AAIYAARANL KPIMITGMEQ GGQLMTTTDV DNWPGEAPGL 

        70         80         90        100        110        120 
QGPQLMERMQ KHAERLDTQF IFDHINEADL NQRPFLLKGD NATYSCDALI IATGASARYL 

       130        140        150        160        170        180 
GLPSEKAYMG KGVSACATCD GFFYRGKKVA VVGGGNTAVE EALYLSHIAS HVTLIHRRDK 

       190        200        210        220        230        240 
LRAEKMLSAQ LIKKVEEGKV AIVWSHVIEE VLGDDQGVTG VHLKHVKEEK TQDLTIDGLF 

       250        260        270        280        290        300 
IAIGHDPNTK IFKEQLEMDE AGYLRAKSGL QGNATATNIP GVFAAGDVTD HVYRQAITAA 

       310        320 
GMGCMAALDA ERYLDSLNQA 

« Hide

References

« Hide 'large scale' references
[1]Oswald W.
Thesis (1994), Justus Liebig University / Frankfurt, Germany
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Nine Mile phase I / Bratislava.
[2]"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."
Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. expand/collapse author list , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.
Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nine Mile phase I / RSA 493.

Cross-references

Sequence databases

X75627 Genomic DNA. Translation: CAA53288.1.
AE016828 Genomic DNA. Translation: AAO90702.1.
PIRS43131.
RefSeqNP_820188.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1209097.
GenomeReviewsGene locus CBU_1193 in contig AE016828_GR.
KEGGcbu:CBU_1193.
NMPDRfig|227377.1.peg.1132.
TIGRCBU_1193.

Phylogenomic databases

HOGENOMP39916.
OMAHCKLLIL

Enzyme and pathway databases

BioCycCBUR227377:CBU_1193-MON.
BRENDA1.8.1.9. 256353.

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_COXBU
AccessionPrimary (citable) accession number: P39916
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 9, 2003
Last modified: November 24, 2009
This is version 76 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

Coxiella burnetii

Coxiella burnetii (strain RSA 493): 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