ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q58931


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TRXB_METJA
Primary accession number Q58931
Secondary accession numbers None
Integrated into Swiss-Prot on January 16, 2004
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Putative thioredoxin reductase
Synonyms TRXR
EC 1.8.1.9
Gene name
OrderedLocusNames: MJ1536
From
Methanocaldococcus jannaschii (Methanococcus jannaschii) [TaxID: 2190] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=8688087 [NCBI, ExPASy, EBI, Israel, Japan]
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.";
Science 273:1058-1073(1996).
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
L77117; AAB99556.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G64491; G64491.
RefSeq NP_248544.1; -.
3D structure databases
HSSP P09625; 1CL0. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q58931.
Enzyme and pathway databases
BioCyc MJAN243232:MJ_1536-MON; -.
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 IPR013027; 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_reduct.
Graphical view of domain structure.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00469; PNDRDTASEII.
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.
ProtoNet Q58931.
Genome annotation databases
GeneID 1452444; -.
GenomeReviews L77117_GR; MJ1536.
KEGG mja:MJ1536; -.
NMPDR fig|243232.1.peg.1581; -.
TIGR MJ1536; -.
Phylogenomic databases
HOGENOM Q58931; -.
Other
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   301  301     Putative thioredoxin reductase. PRO_0000166759
NP_BIND   32    39  8     FAD (By similarity). 
NP_BIND   272   280  9     FAD (By similarity). 
DISULFID   130   133        Redox-active (By similarity). 
Sequence information
Length: 301 AA [This is the length of the unprocessed precursor] Molecular weight: 33035 Da [This is the MW of the unprocessed precursor] CRC64: B8319F2B33559AD8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIHDTIIIGA GPGGLTAGIY AMRGKLNALC IEKENAGGRI AEAGIVENYP GFEEIRGYEL 

        70         80         90        100        110        120 
AEKFKNHAEK FKLPIIYDEV IKIETKERPF KVITKNSEYL TKTIVIATGT KPKKLGLNED 

       130        140        150        160        170        180 
KFIGRGISYC TMCDAFFYLN KEVIVIGRDT PAIMSAINLK DIAKKVIVIT DKSELKAAES 

       190        200        210        220        230        240 
IMLDKLKEAN NVEIIYNAKP LEIVGEERAE GVKISVNGKE EIIKADGIFI SLGHVPNTEF 

       250        260        270        280        290        300 
LKDSGIELDK KGFIKTDENC RTNIDGIYAV GDVRGGVMQV AKAVGDGCVA MANIIKYLQK 


L 

Q58931 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!