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P80880 (TRXB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thioredoxin reductase
Short name=TRXR
EC=1.8.1.9
Alternative name(s):
General stress protein 35
Short name=GSP35
Gene names
Name:trxB
Synonyms:yvcH
Ordered Locus Names:BSU34790
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Induction

By heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation.

Miscellaneous

The active site is a redox-active disulfide bond By similarity.

Sequence similarities

Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 316315Thioredoxin reductase
PRO_0000166719

Regions

Nucleotide binding36 – 438FAD By similarity
Nucleotide binding278 – 28710FAD By similarity

Amino acid modifications

Disulfide bond135 ↔ 138Redox-active By similarity

Experimental info

Sequence conflict21S → A AA sequence Ref.3
Sequence conflict71Y → E AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P80880 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9A14AC9E75A3F0AC

FASTA31634,519
        10         20         30         40         50         60 
MSEEKIYDVI IIGAGPAGMT AAVYTSRANL STLMIERGIP GGQMANTEDV ENYPGFESIL 

        70         80         90        100        110        120 
GPELSNKMFE HAKKFGAEYA YGDIKEVIDG KEYKVVKAGS KEYKARAVII AAGAEYKKIG 

       130        140        150        160        170        180 
VPGEKELGGR GVSYCAVCDG AFFKGKELVV VGGGDSAVEE GVYLTRFASK VTIVHRRDKL 

       190        200        210        220        230        240 
RAQSILQARA FDNEKVDFLW NKTVKEIHEE NGKVGNVTLV DTVTGEESEF KTDGVFIYIG 

       250        260        270        280        290        300 
MLPLSKPFEN LGITNEEGYI ETNDRMETKV EGIFAAGDIR EKSLRQIVTA TGDGSIAAQS 

       310 
VQHYVEELQE TLKTLK

« Hide

References

« Hide 'large scale' references
[1]Denizot F.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-24.
Strain: 168 / IS58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z94043 Genomic DNA. Translation: CAB08055.1.
AL009126 Genomic DNA. Translation: CAB15484.1.
PIRA69727.
RefSeqNP_391359.1. NC_000964.3.

3D structure databases

ProteinModelPortalP80880.
SMRP80880. Positions 1-308.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU34790.

Proteomic databases

PaxDbP80880.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15484; CAB15484; BSU34790.
GeneID936549.
KEGGbsu:BSU34790.
PATRIC18978964. VBIBacSub10457_3644.

Organism-specific databases

GenoListBSU34790. [Micado]

Phylogenomic databases

eggNOGCOG0492.
HOGENOMHOG000072911.
KOK00384.
OMAIYNAKPL.
ProtClustDBCLSK2752520.

Enzyme and pathway databases

BioCycBSUB:BSU34790-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_BACSU
AccessionPrimary (citable) accession number: P80880
Secondary accession number(s): O06971
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents