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UniProtKB/Swiss-Prot entry O84101

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

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Entry information
Entry name TRXB_CHLTR
Primary accession number O84101
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 60)
Name and origin of the protein
Protein name Thioredoxin reductase
Synonyms TRXR
EC 1.8.1.9
Gene name
Name: trxB
OrderedLocusNames: CT_099
From
Chlamydia trachomatis [TaxID: 813] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=D/UW-3/Cx;
DOI=10.1126/science.282.5389.754; PubMed=9784136 [NCBI, ExPASy, EBI, Israel, Japan]
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis.";
Science 282:754-759(1998).
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
AE001273; AAC67690.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B71556; B71556.
RefSeq NP_219602.1; -.
3D structure databases
HSSP Q39243; 1VDC. [HSSP ENTRY / PDB]
ModBase O84101.
Enzyme and pathway databases
BioCyc CTRA315277:CT099-MON; -.
2D gel databases
PHCI-2DPAGE O84101; -.
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.
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.
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 884181; -.
GenomeReviews AE001273_GR; CT_099.
KEGG ctr:CT099; -.
Phylogenomic databases
HOGENOM O84101; -.
Genome annotation databases
CMR O84101; CT_099.
Other
ProtoNet O84101.
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   312  312     Thioredoxin reductase. PRO_0000166726
NP_BIND   33    43  11     FAD (By similarity). 
NP_BIND   283   292  10     FAD (By similarity). 
DISULFID   138   141        Redox-active (By similarity). 
Sequence information
Length: 312 AA [This is the length of the unprocessed precursor] Molecular weight: 33508 Da [This is the MW of the unprocessed precursor] CRC64: 729D0D22F8FA0A39 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTHAKLVIIG SGPAGYTAAI YASRALLTPV LFEGFFSGIA GGQLMTTTEV ENFPGFPEGV 

        70         80         90        100        110        120 
LGHQLMDLMK TQAQRFGTQV LSKDITAVDF SVRPFVLKSG KETFTCDACI IATGASAKRL 

       130        140        150        160        170        180 
SIPGAGDNEF WQKGVTACAV CDGASPIFRD KDLFVVGGGD SALEEAMFLT RYGKRVFVVH 

       190        200        210        220        230        240 
RRDTLRASKV MVNKAQANEK IFFLWNSEIV KISGDTLVRS IDIYNNVDET TTTMEAAGVF 

       250        260        270        280        290        300 
FAIGHQPNTA FLGGQVALDE NGYIITEKGS SRTSVPGVFA AGDVQDKYYR QAITSAGSGC 

       310 
MAALDAERFL EN
O84101 in FASTA format

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