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P39916

- TRXB_COXBU

UniProt

P39916 - TRXB_COXBU

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
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (09 May 2003)
      Previous versions | rss
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    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

    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-SubCell

    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

    MNKPQHHSLI ILGSGPAGYT AAIYAARANL KPIMITGMEQ GGQLMTTTDV    50
    DNWPGEAPGL QGPQLMERMQ KHAERLDTQF IFDHINEADL NQRPFLLKGD 100
    NATYSCDALI IATGASARYL GLPSEKAYMG KGVSACATCD GFFYRGKKVA 150
    VVGGGNTAVE EALYLSHIAS HVTLIHRRDK LRAEKMLSAQ LIKKVEEGKV 200
    AIVWSHVIEE VLGDDQGVTG VHLKHVKEEK TQDLTIDGLF IAIGHDPNTK 250
    IFKEQLEMDE AGYLRAKSGL QGNATATNIP GVFAAGDVTD HVYRQAITAA 300
    GMGCMAALDA ERYLDSLNQA 320
    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

    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 1, 2014
    This is version 101 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