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P39916 (TRXB_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length320 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
Reference proteome
Gene Ontology (GO)
   Biological_processremoval of superoxide radicals

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

thioredoxin-disulfide reductase activity

Inferred from electronic annotation. Source: UniProtKB-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 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RSA 493 / Nine Mile phase I.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75627 Genomic DNA. Translation: CAA53288.1.
AE016828 Genomic DNA. Translation: AAO90702.1.
PIRS43131.
RefSeqNP_820188.1. NC_002971.3.

3D structure databases

ProteinModelPortalP39916.
SMRP39916. Positions 5-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_1193.

Proteomic databases

PRIDEP39916.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO90702; AAO90702; CBU_1193.
GeneID1209097.
KEGGcbu:CBU_1193.
PATRIC17931129. VBICoxBur82552_1190.

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHOG000072912.
KOK00384.
OMAHINEVDF.
OrthoDBEOG65XN2W.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-1181-MONOMER.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
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: May 14, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names