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UniProtKB/Swiss-Prot entry O32823


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

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Entry information
Entry name TRXB_LISMO
Primary accession number O32823
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 61)
Name and origin of the protein
Protein name Thioredoxin reductase
Synonyms TRXR
EC 1.8.1.9
Gene name
Name: trxB
OrderedLocusNames: lmo2478
From
Listeria monocytogenes [TaxID: 1639] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=EGD / Serovar 1/2a;
Borovok I., Mislovati M., Cohen G., Aharonowitz Y.;
"Isolation, cloning and characterization of the Listeria monocytogenes thioredoxin reductase gene, trxB.";
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-679 / EGD-e / Serovar 1/2a;
DOI=10.1126/science.1063447; PubMed=11679669 [NCBI, ExPASy, EBI, Israel, Japan]
Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
"Comparative genomics of Listeria species.";
Science 294:849-852(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
AF009622; AAB63804.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591983; CAD00556.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR AF1384; AF1384.
RefSeq NP_466001.1; -.
3D structure databases
HSSP Q39243; 1VDC. [HSSP ENTRY / PDB]
ModBase O32823.
Enzyme and pathway databases
BioCyc LMON169963:LMO2478-MON; -.
Organism-specific databases
ListiList LMO02478; -.
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:0004791; Molecular function: thioredoxin-disulfide reductase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019430; Biological process: removal of superoxide radicals (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000759; Adrndx_reductase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
IPR003042; Rng_hydrolase.
IPR005982; Thioredox_reduct.
Graphical view of domain structure.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.
PR00420; RNGMNOXGNASE.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01292; TRX_reduct; 1.
PROSITE PS00573; PYRIDINE_REDOX_2; 1.
Genome annotation databases
GeneID 987338; -.
GenomeReviews AL591824_GR; lmo2478.
KEGG lmo:lmo2478; -.
Phylogenomic databases
HOGENOM O32823; -.
Genome annotation databases
CMR O32823; lmo2478.
Other
ProtoNet O32823.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   319  319     Thioredoxin reductase. PRO_0000166736
NP_BIND   37    44  8     FAD (By similarity). 
NP_BIND   279   288  10     FAD (By similarity). 
DISULFID   136   139        Redox-active (By similarity). 
Sequence information
Length: 319 AA [This is the length of the unprocessed precursor] Molecular weight: 34174 Da [This is the MW of the unprocessed precursor] CRC64: 8D42F36970611979 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASEEKIYDV IIIGAGPAGM TAALYTSRAD LDTLMIERGV PGGQMVNTAE VENYPGFDSI 

        70         80         90        100        110        120 
LGPDLSDKML SGAKQFGAEY AYGDIKEVVD GKEFKTVTAG SKTYKARAII IATGAEHRKL 

       130        140        150        160        170        180 
GAAGEEELSG RGVSYCAVCD GAFFKNRELI VVGGGDSAVE EGTYLTRYAD KVTIVHRRDK 

       190        200        210        220        230        240 
LRAQQILQDR AFKDEKVDFI WNSTVEEIVG DGKKVTGAKL VSTVDGSESI MPVDGVFIYV 

       250        260        270        280        290        300 
GLVPLTKAFL NLGITDDEGY IVTDEEMRTN LPGIFAAGDV RAKSLRQIVT ATGDGGLAGQ 

       310 
NAQKYVEELK ESLEAEAAK 

O32823 in FASTA format

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