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P39916

- TRXB_COXBU

UniProt

P39916 - TRXB_COXBU

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Protein

Thioredoxin reductase

Gene

trxB

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

Binds 1 FAD per subunit.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 438FADBy similarity
Nucleotide bindingi287 – 29610FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. thioredoxin-disulfide reductase activity Source: UniProtKB-EC

GO - Biological processi

  1. removal of superoxide radicals Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciCBUR227377:GJ7S-1181-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase (EC:1.8.1.9)
Short name:
TRXR
Gene namesi
Name:trxB
Ordered Locus Names:CBU_1193
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
ProteomesiUP000002671: Chromosome

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320Thioredoxin reductasePRO_0000166728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi136 ↔ 139Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP39916.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi227377.CBU_1193.

Structurei

3D structure databases

ProteinModelPortaliP39916.
SMRiP39916. Positions 5-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0492.
HOGENOMiHOG000072912.
KOiK00384.
OMAiHINEVDF.
OrthoDBiEOG65XN2W.

Family and domain databases

InterProiIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
PR00469. PNDRDTASEII.
TIGRFAMsiTIGR01292. TRX_reduct. 1 hit.
PROSITEiPS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39916-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKPQHHSLI ILGSGPAGYT AAIYAARANL KPIMITGMEQ GGQLMTTTDV
60 70 80 90 100
DNWPGEAPGL QGPQLMERMQ KHAERLDTQF IFDHINEADL NQRPFLLKGD
110 120 130 140 150
NATYSCDALI IATGASARYL GLPSEKAYMG KGVSACATCD GFFYRGKKVA
160 170 180 190 200
VVGGGNTAVE EALYLSHIAS HVTLIHRRDK LRAEKMLSAQ LIKKVEEGKV
210 220 230 240 250
AIVWSHVIEE VLGDDQGVTG VHLKHVKEEK TQDLTIDGLF IAIGHDPNTK
260 270 280 290 300
IFKEQLEMDE AGYLRAKSGL QGNATATNIP GVFAAGDVTD HVYRQAITAA
310 320
GMGCMAALDA ERYLDSLNQA
Length:320
Mass (Da):34,620
Last modified:May 9, 2003 - v2
Checksum:i750851B6FDDEB5E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211A → D in CAA53288. 1 PublicationCurated
Sequence conflicti25 – 251A → V in CAA53288. 1 PublicationCurated
Sequence conflicti51 – 511D → A in CAA53288. 1 PublicationCurated
Sequence conflicti64 – 663QLM → KLL in CAA53288. 1 PublicationCurated
Sequence conflicti74 – 774ERLD → GGALN in CAA53288. 1 PublicationCurated
Sequence conflicti87 – 882EA → KP in CAA53288. 1 PublicationCurated
Sequence conflicti92 – 921Q → P in CAA53288. 1 PublicationCurated
Sequence conflicti98 – 981K → Q in CAA53288. 1 PublicationCurated
Sequence conflicti127 – 1271A → P in CAA53288. 1 PublicationCurated
Sequence conflicti146 – 1461G → A in CAA53288. 1 PublicationCurated
Sequence conflicti158 – 1581A → S in CAA53288. 1 PublicationCurated
Sequence conflicti284 – 2929AAGDVTDHV → PAVVVRGQL in CAA53288. 1 PublicationCurated
Sequence conflicti296 – 2983AIT → TIA in CAA53288. 1 PublicationCurated
Sequence conflicti306 – 3061A → P in CAA53288. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75627 Genomic DNA. Translation: CAA53288.1.
AE016828 Genomic DNA. Translation: AAO90702.1.
PIRiS43131.
RefSeqiNP_820188.1. NC_002971.3.

Genome annotation databases

EnsemblBacteriaiAAO90702; AAO90702; CBU_1193.
GeneIDi1209097.
KEGGicbu:CBU_1193.
PATRICi17931129. VBICoxBur82552_1190.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75627 Genomic DNA. Translation: CAA53288.1 .
AE016828 Genomic DNA. Translation: AAO90702.1 .
PIRi S43131.
RefSeqi NP_820188.1. NC_002971.3.

3D structure databases

ProteinModelPortali P39916.
SMRi P39916. Positions 5-317.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 227377.CBU_1193.

Proteomic databases

PRIDEi P39916.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO90702 ; AAO90702 ; CBU_1193 .
GeneIDi 1209097.
KEGGi cbu:CBU_1193.
PATRICi 17931129. VBICoxBur82552_1190.

Phylogenomic databases

eggNOGi COG0492.
HOGENOMi HOG000072912.
KOi K00384.
OMAi HINEVDF.
OrthoDBi EOG65XN2W.

Enzyme and pathway databases

BioCyci CBUR227377:GJ7S-1181-MONOMER.

Family and domain databases

InterProi IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR008255. Pyr_nucl-diS_OxRdtase_2_AS.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR005982. Thioredox_Rdtase.
[Graphical view ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
PR00469. PNDRDTASEII.
TIGRFAMsi TIGR01292. TRX_reduct. 1 hit.
PROSITEi PS00573. PYRIDINE_REDOX_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Oswald W.
    Thesis (1994), Justus Liebig University / Frankfurt, Germany
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Nine Mile phase I / Bratislava.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RSA 493 / Nine Mile phase I.

Entry informationi

Entry nameiTRXB_COXBU
AccessioniPrimary (citable) accession number: P39916
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 9, 2003
Last modified: October 29, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3