Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-threonine 3-dehydrogenase, mitochondrial

Gene

Tdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD+-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate, mediating L-threonine catabolism.1 Publication

Catalytic activityi

L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH.1 Publication

Kineticsi

  1. KM=72.4 mM for L-threonine1 Publication
  2. KM=1.67 mM for NAD+1 Publication

    Pathwayi: L-threonine degradation via oxydo-reductase pathway

    This protein is involved in step 1 of the subpathway that synthesizes glycine from L-threonine.1 Publication
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. L-threonine 3-dehydrogenase, mitochondrial (Tdh)
    2. 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial (Gcat)
    This subpathway is part of the pathway L-threonine degradation via oxydo-reductase pathway, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycine from L-threonine, the pathway L-threonine degradation via oxydo-reductase pathway and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei195Proton donor/acceptor1 Publication1
    Binding sitei195NADCombined sources1 Publication1
    Binding sitei199NADCombined sources1 Publication1
    Binding sitei225NAD; via amide nitrogenCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi62 – 67NAD bindingCombined sources1 Publication6
    Nucleotide bindingi88 – 90NAD bindingCombined sources1 Publication3
    Nucleotide bindingi106 – 107NAD bindingCombined sources1 Publication2

    GO - Molecular functioni

    • coenzyme binding Source: InterPro
    • identical protein binding Source: UniProtKB
    • L-threonine 3-dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    • L-threonine catabolic process to glycine Source: UniProtKB-UniPathway
    • threonine catabolic process Source: UniProtKB

    Keywordsi

    Molecular functionOxidoreductase
    LigandNAD

    Enzyme and pathway databases

    BRENDAi1.1.1.103. 3474.
    UniPathwayiUPA00046; UER00505.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-threonine 3-dehydrogenase, mitochondrialCurated (EC:1.1.1.1031 Publication)
    Gene namesi
    Name:TdhImported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 14

    Organism-specific databases

    MGIiMGI:1926231. Tdh.

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi133S → A: Decreased L-threonine 3-dehydrogenase activity. 1 Publication1
    Mutagenesisi180R → K: Decreased L-threonine 3-dehydrogenase activity. No effect on protein NAD(+)-binding. No gross effect on protein folding. No effect on protein stability. 1 Publication1
    Mutagenesisi237T → A: Decreased L-threonine 3-dehydrogenase activity. 1 Publication1
    Mutagenesisi333M → A: Decreased L-threonine 3-dehydrogenase activity. 1 Publication1
    Mutagenesisi333M → E: Decreased L-threonine 3-dehydrogenase activity. Decreased affinity for L-threonine. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_0000298784? – 373L-threonine 3-dehydrogenase, mitochondrial
    Transit peptidei1 – ?MitochondrionSequence analysis

    Proteomic databases

    PaxDbiQ8K3F7.
    PeptideAtlasiQ8K3F7.
    PRIDEiQ8K3F7.

    PTM databases

    iPTMnetiQ8K3F7.
    PhosphoSitePlusiQ8K3F7.

    Expressioni

    Gene expression databases

    BgeeiENSMUSG00000021953.
    CleanExiMM_TDH.
    ExpressionAtlasiQ8K3F7. baseline and differential.
    GenevisibleiQ8K3F7. MM.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    GO - Molecular functioni

    • identical protein binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi208451. 2 interactors.
    STRINGi10090.ENSMUSP00000022522.

    Structurei

    Secondary structure

    1373
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi58 – 61Combined sources4
    Turni62 – 64Combined sources3
    Helixi66 – 79Combined sources14
    Helixi81 – 83Combined sources3
    Beta strandi84 – 88Combined sources5
    Helixi94 – 97Combined sources4
    Beta strandi102 – 104Combined sources3
    Helixi110 – 119Combined sources10
    Beta strandi124 – 127Combined sources4
    Helixi133 – 138Combined sources6
    Helixi146 – 160Combined sources15
    Beta strandi164 – 166Combined sources3
    Helixi171 – 173Combined sources3
    Beta strandi181 – 183Combined sources3
    Beta strandi185 – 187Combined sources3
    Helixi194 – 212Combined sources19
    Beta strandi217 – 222Combined sources6
    Beta strandi224 – 226Combined sources3
    Helixi236 – 238Combined sources3
    Helixi239 – 248Combined sources10
    Beta strandi252 – 257Combined sources6
    Beta strandi263 – 267Combined sources5
    Helixi268 – 280Combined sources13
    Helixi283 – 285Combined sources3
    Beta strandi289 – 292Combined sources4
    Beta strandi295 – 298Combined sources4
    Helixi300 – 308Combined sources9
    Beta strandi315 – 318Combined sources4
    Helixi322 – 330Combined sources9
    Helixi338 – 344Combined sources7
    Helixi352 – 362Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4YR9X-ray2.80A/B/C/D/E/F47-373[»]
    4YRAX-ray2.65A/B/C/D/E/F/G/H/I/J/K/L47-373[»]
    4YRBX-ray3.25A/B/C/D/E/F47-373[»]
    ProteinModelPortaliQ8K3F7.
    SMRiQ8K3F7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG2774. Eukaryota.
    COG0451. LUCA.
    GeneTreeiENSGT00390000014037.
    HOGENOMiHOG000034276.
    HOVERGENiHBG062086.
    InParanoidiQ8K3F7.
    KOiK15789.
    OMAiHWHASPR.
    OrthoDBiEOG091G09SG.
    PhylomeDBiQ8K3F7.
    TreeFamiTF314544.

    Family and domain databases

    InterProiView protein in InterPro
    IPR001509. Epimerase_deHydtase.
    IPR016040. NAD(P)-bd_dom.
    PfamiView protein in Pfam
    PF01370. Epimerase. 1 hit.
    SUPFAMiSSF51735. SSF51735. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8K3F7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLFLGMLKQV VNGTAQSKAS SCRKLVLPLK FLGTSQHRIP ADANFHSTSI
    60 70 80 90 100
    SEAEPPRVLI TGGLGQLGVG LANLLRKRFG KDNVILSDIR KPPAHVFHSG
    110 120 130 140 150
    PFVYANILDY KSLREIVVNH RISWLFHYSA LLSAVGEANV SLARDVNITG
    160 170 180 190 200
    LHNVLDVAAE YNVRLFVPST IGAFGPTSPR NPAPDLCIQR PRTIYGVSKV
    210 220 230 240 250
    HTELMGEYYY YRYGLDFRCL RYPGIISADS QPGGGTTDYA VQIFHAAAKN
    260 270 280 290 300
    GTFECNLEAG TRLPMMYISD CLRATLEVME APAERLSMRT YNISAMSFTP
    310 320 330 340 350
    EELAQALRKH APDFQITYCV DPLRQAIAES WPMILDDSNA RKDWGWKHDF
    360 370
    DLPELVATML NFHGVSTRVA QVN
    Length:373
    Mass (Da):41,462
    Last modified:October 1, 2002 - v1
    Checksum:i6A416A079A7EC381
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti82D → N in AAH58860 (PubMed:15489334).Curated1
    Sequence conflicti214G → V in AAF61395 (PubMed:12097150).Curated1
    Sequence conflicti232P → R in AAF61395 (PubMed:12097150).Curated1
    Sequence conflicti318Y → H in AAH58860 (PubMed:15489334).Curated1
    Sequence conflicti361N → S in AAF61395 (PubMed:12097150).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF134346 mRNA. Translation: AAF61395.2.
    AY116662 mRNA. Translation: AAM51557.1.
    AK077571 mRNA. Translation: BAC36870.1.
    BC058860 mRNA. Translation: AAH58860.1.
    CCDSiCCDS27202.1.
    RefSeqiNP_067455.5. NM_021480.5.
    UniGeneiMm.354229.

    Genome annotation databases

    EnsembliENSMUST00000022522; ENSMUSP00000022522; ENSMUSG00000021953.
    GeneIDi58865.
    KEGGimmu:58865.
    UCSCiuc007uhs.1. mouse.

    Similar proteinsi

    Entry informationi

    Entry nameiTDH_MOUSE
    AccessioniPrimary (citable) accession number: Q8K3F7
    Secondary accession number(s): Q6PD91, Q9JLU3
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: October 1, 2002
    Last modified: August 30, 2017
    This is version 106 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families