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Reviewed, UniProtKB/Swiss-Prot P51978 (TRXB_NEUCR)

Last modified June 16, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
    EC=1.8.1.9
Gene names
Name: cys-9
ORF Names: NCU08352
OrganismNeurospora crassa [Complete proteome]
Taxonomic identifier5141 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length334 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

electron carrier activity

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 – 334334Thioredoxin reductase
PRO_0000166764

Regions

Nucleotide binding32 – 4413FAD By similarity
Nucleotide binding287 – 29610FAD By similarity

Amino acid modifications

Disulfide bond140 ↔ 143Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P51978-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4D9EE9861E479EB4

FASTA33435,883
        10         20         30         40         50         60 
MHSKVVIIGS GPAAHTAAIY LARAELKPVL YEGFMANGIA AGGQLTTTTE IENFPGFPDG 

        70         80         90        100        110        120 
IMGQELMDKM KAQSERFGTQ IISETVAKVD LSARPFKYAT EWSPEEYHTA DSIILATGAS 

       130        140        150        160        170        180 
ARRLHLPGEE KYWQNGISAC AVCDGAVPIF RNKHLVVIGG GDSAAEEAMY LTKYGSHVTV 

       190        200        210        220        230        240 
LVRKDKLRAS SIMAHRLLNH EKVTVRFNTV GVEVKGDDKG LMSHLVVKDV TTGKEETLEA 

       250        260        270        280        290        300 
NGLFYAIGHD PATALVKGQL ETDADGYVVT KPGTTLTSVE GVFAAGDVQD KRYRQAITSA 

       310        320        330 
GTGCMAALDA EKFLSEHEET PAEHRDTSAV QGNL 

« Hide

References

« Hide 'large scale' references
[1]"Mutation of the cys-9 gene, which encodes thioredoxin reductase, affects the circadian conidiation rhythm in Neurospora crassa."
Onai K., Nakashima H.
Genetics 146:101-110(1997) [PubMed: 9136004] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ACR-2.
[2]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed: 12712197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases

D45049 Genomic DNA. Translation: BAA08090.1.
AABX02000029 Genomic DNA. Translation: EAA36019.1.
PIRT47256.
RefSeqXP_965255.1.

3D structure databases

HSSPHSSP built from PDB template 1VDC based on UniProtKB Q39243.
ModBaseSearch...

Genome annotation databases

GeneID3881395.
KEGGncr:NCU08352.
NMPDRfig|5141.1.peg.7331.

Enzyme and pathway databases

BioCycNCRA-XX3-01:NCRA-XX3-01-003211-MON.
BRENDA1.8.1.9. 266.

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.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01292. TRX_reduct. 1 hit.
PROSITEPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRXB_NEUCR
AccessionPrimary (citable) accession number: P51978
Secondary accession number(s): Q7RVM1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

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