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UniProtKB/Swiss-Prot entry P46843


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TRXB_MYCLE
Primary accession number P46843
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 77)
Name and origin of the protein
Protein name Bifunctional thioredoxin reductase/thioredoxin
Synonyms None
Includes Thioredoxin reductase
     (TRXR)
     (EC 1.8.1.9)
Thioredoxin
Gene name
Name: trxB/A
Synonyms: trx
OrderedLocusNames: ML2703
From
Mycobacterium leprae [TaxID: 1769] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8969512 [NCBI, ExPASy, EBI, Israel, Japan]
Fsihi H., de Rossi E., Salazar L., Cantoni R., Labo M., Riccardi G., Takiff H.E., Eiglmeier K., Bergh S., Cole S.T.;
"Gene arrangement and organization in an approximately 76 kb fragment encompassing the oriC region of the chromosome of Mycobacterium leprae.";
Microbiology 142:3147-3161(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7476189 [NCBI, ExPASy, EBI, Israel, Japan]
Wieles B., van Soolingen D., Holmgren A., Offringa R., Ottenhoff T., Thole J.;
"Unique gene organization of thioredoxin and thioredoxin reductase in Mycobacterium leprae.";
Mol. Microbiol. 16:921-929(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TN;
DOI=10.1038/35059006; PubMed=11234002 [NCBI, ExPASy, EBI, Israel, Japan]
Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G.;
"Massive gene decay in the leprosy bacillus.";
Nature 409:1007-1011(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L39923; AAB53131.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X87899; CAA61150.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL583926; CAC32235.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S77662; S77662.
RefSeq NP_302724.1; -.
3D structure databases
HSSP P80579; 1QUW. [HSSP ENTRY / PDB]
SMR P46843; 7-318, 351-456.
ModBase P46843.
Enzyme and pathway databases
BioCyc MLEP272631:ML2703-MON; -.
Organism-specific databases
Leproma ML2703; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0015035; Molecular function: protein disulfide oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0004791; Molecular function: thioredoxin-disulfide reductase activity (inferred from electronic annotation from InterPro).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006662; Biological process: glycerol ether metabolic process (inferred from electronic annotation from InterPro).
GO:0019430; Biological process: removal of superoxide radicals (inferred from electronic annotation from InterPro).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000759; Adrndx_reductase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR016040; NAD(P)-bd.
IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
IPR005982; Thioredox_reduct.
IPR005746; Thioredoxin.
IPR006662; Thioredoxin-like.
IPR013766; Thioredoxin_dom.
IPR015467; Trx.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR10438; Trx; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF00085; Thioredoxin; 1.
Pfam graphical view of domain structure.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.
PR00421; THIOREDOXIN.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01068; thioredoxin; 1.
TIGR01292; TRX_reduct; 1.
PROSITE PS00573; PYRIDINE_REDOX_2; 1.
PS00194; THIOREDOXIN_1; 1.
PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P46843.
Genome annotation databases
GeneID 910819; -.
GenomeReviews AL450380_GR; ML2703.
KEGG mle:ML2703; -.
NMPDR fig|272631.1.peg.1596; -.
Phylogenomic databases
HOGENOM P46843; -.
Genome annotation databases
CMR P46843; ML2703.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Electron transport; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   458  458     Bifunctional thioredoxin reductase/thioredoxin. PRO_0000166758
DOMAIN   341   455  115     Thioredoxin. 
NP_BIND   41    48  8     FAD (By similarity). 
NP_BIND   285   294  10     FAD (By similarity). 
REGION   1   321  321     Thioredoxin reductase. 
REGION   322   347  26     Linker. 
DISULFID   142   145        Redox-active (By similarity). 
DISULFID   379   382        Redox-active (By similarity). 
Sequence information
Length: 458 AA [This is the length of the unprocessed precursor] Molecular weight: 49046 Da [This is the MW of the unprocessed precursor] CRC64: 84D367AB31899987 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNTTPSAHET IHEVIVIGSG PAGYTAALYA ARAQLTPLVF EGTSFGGALM TTTEVENYPG 

        70         80         90        100        110        120 
FRNGITGPEL MDDMREQALR FGAELRTEDV ESVSLRGPIK SVVTAEGQTY QARAVILAMG 

       130        140        150        160        170        180 
TSVRYLQIPG EQELLGRGVS ACATCDGSFF RGQDIAVIGG GDSAMEEALF LTRFARSVTL 

       190        200        210        220        230        240 
VHRRDEFRAS KIMLGRARNN DKIKFITNHT VVAVNGYTTV TGLRLRNTTT GEETTLVVTG 

       250        260        270        280        290        300 
VFVAIGHEPR SSLVSDVVDI DPDGYVLVKG RTTSTSMDGV FAAGDLVDRT YRQAITAAGS 

       310        320        330        340        350        360 
GCAAAIDAER WLAEHAGSKA NETTEETGDV DSTDTTDWST AMTDAKNAGV TIEVTDASFF 

       370        380        390        400        410        420 
ADVLSSNKPV LVDFWATWCG PCKMVAPVLE EIASEQRNQL TVAKLDVDTN PEMAREFQVV 

       430        440        450 
SIPTMILFQG GQPVKRIVGA KGKAALLRDL SDVVPNLN 

P46843 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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