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Protein

Aminopyrimidine aminohydrolase

Gene

tenA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway. Thus, catalyzes the conversion of 4-amino-5-aminomethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP). To a lesser extent, is also able to catalyze the hydrolytic cleavage of thiamine; however, this thiaminase activity is unlikely to be physiologically relevant. Therefore, is involved in the regeneration of the thiamine pyrimidine from thiamine degraded products present in the environment, rather than in thiamine degradation.1 Publication

Caution

Was originally described as a regulatory protein involved in the regulation of the production of extracellular enzymes.1 PublicationCurated

Catalytic activityi

4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + ammonia.1 Publication
Thiamine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole.1 Publication

Kineticsi

kcat is 22.0 min(-1) for the hydrolysis of 4-amino-5-aminomethyl-2-methylpyrimidine. Catalyzes the hydrolysis of aminopyrimidine 100 times faster than the hydrolysis of thiamine.1 Publication
  1. KM=11.8 µM for 4-amino-5-aminomethyl-2-methylpyrimidine1 Publication

    Pathwayi: thiamine diphosphate biosynthesis

    This protein is involved in the pathway thiamine diphosphate biosynthesis, which is part of Cofactor biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei44Substrate2 Publications1
    Sitei47Increases nucleophilicity of active site Cys1 Publication1
    Active sitei135Nucleophile1 Publication1
    Binding sitei139Substrate2 Publications1
    Binding sitei163Substrate2 Publications1
    Active sitei205Proton donor1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase
    Biological processThiamine biosynthesis

    Enzyme and pathway databases

    BioCyciBSUB:BSU11650-MONOMER
    MetaCyc:BSU11650-MONOMER
    BRENDAi3.5.99.2 658
    UniPathwayiUPA00060

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopyrimidine aminohydrolase1 Publication (EC:3.5.99.21 Publication)
    Alternative name(s):
    4-amino-5-aminomethyl-2-methylpyrimidine hydrolase1 Publication
    Thiaminase II1 Publication
    Gene namesi
    Name:tenA1 Publication
    Ordered Locus Names:BSU11650
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Pathology & Biotechi

    Disruption phenotypei

    Inactivation of this gene causes a delay in sporulation, but does not affect cell growth and the production of extracellular enzymes (PubMed:1898926). The deletion mutant does not require a hydroxypyrimidine source as it is able to biosynthesize it using ThiA; the tenA/thiA double mutant, however, is hydroxypyrimidine-requiring and is unable to salvage the pyrimidine from formylaminopyrimidine, aminopyrimidine, or base-degraded thiamine (PubMed:17618314).2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi44D → A: 6300-fold reduction in catalytic efficiency. 1 Publication1
    Mutagenesisi47Y → F: About 2-fold decrease in substrate affinity and 30-fold reduction in catalytic activity. 1 Publication1
    Mutagenesisi112Y → F: About 2-fold decrease in substrate affinity and 70-fold reduction in catalytic activity. 1 Publication1
    Mutagenesisi135C → A: Loss of catalytic activity. 1 Publication1
    Mutagenesisi205E → A: 2000-fold reduction in catalytic efficiency. 1 Publication1

    Chemistry databases

    DrugBankiDB02022 4-Amino-5-Hydroxymethyl-2-Methylpyrimidine

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001920461 – 236Aminopyrimidine aminohydrolaseAdd BLAST236

    Proteomic databases

    PaxDbiP25052
    PRIDEiP25052

    Expressioni

    Inductioni

    Strongly repressed by thiamine.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    IntActiP25052, 1 interactor
    MINTiP25052
    STRINGi224308.Bsubs1_010100006441

    Structurei

    Secondary structure

    1236
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 10Combined sources8
    Helixi12 – 19Combined sources8
    Helixi22 – 29Combined sources8
    Helixi34 – 61Combined sources28
    Helixi65 – 93Combined sources29
    Helixi97 – 101Combined sources5
    Helixi107 – 120Combined sources14
    Turni121 – 123Combined sources3
    Helixi125 – 146Combined sources22
    Helixi154 – 163Combined sources10
    Helixi166 – 184Combined sources19
    Helixi188 – 213Combined sources26
    Helixi221 – 225Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TO9X-ray2.40A/B1-236[»]
    1TYHX-ray2.54A/B/D/E2-236[»]
    1YAFX-ray2.60A/B/C/D1-236[»]
    1YAKX-ray2.50A/B/C/D1-236[»]
    2QCXX-ray2.20A/B1-236[»]
    ProteinModelPortaliP25052
    SMRiP25052
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25052

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TenA family.Curated

    Phylogenomic databases

    eggNOGiENOG4105ETU Bacteria
    COG0819 LUCA
    HOGENOMiHOG000225158
    InParanoidiP25052
    KOiK03707
    OMAiCISHPFV
    PhylomeDBiP25052

    Family and domain databases

    Gene3Di1.20.910.10, 1 hit
    InterProiView protein in InterPro
    IPR016084 Haem_Oase-like_multi-hlx
    IPR004305 Thiaminase-2/PQQC
    IPR027574 Thiaminase_II
    PfamiView protein in Pfam
    PF03070 TENA_THI-4, 1 hit
    SUPFAMiSSF48613 SSF48613, 1 hit
    TIGRFAMsiTIGR04306 salvage_TenA, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P25052-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKFSEECRSA AAEWWEGSFV HPFVQGIGDG TLPIDRFKYY VLQDSYYLTH
    60 70 80 90 100
    FAKVQSFGAA YAKDLYTTGR MASHAQGTYE AEMALHREFA ELLEISEEER
    110 120 130 140 150
    KAFKPSPTAY SYTSHMYRSV LSGNFAEILA ALLPCYWLYY EVGEKLLHCD
    160 170 180 190 200
    PGHPIYQKWI GTYGGDWFRQ QVEEQINRFD ELAENSTEEV RAKMKENFVI
    210 220 230
    SSYYEYQFWG MAYRKEGWSD SAIKEVEECG ASRHNG
    Length:236
    Mass (Da):27,417
    Last modified:May 1, 1992 - v1
    Checksum:i6815CFC95BDB07D6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M73546 Genomic DNA Translation: AAA22848.1
    AL009126 Genomic DNA Translation: CAB13022.1
    PIRiA39184 XMBSTA
    RefSeqiNP_389047.1, NC_000964.3
    WP_003232909.1, NZ_JNCM01000035.1

    Genome annotation databases

    EnsemblBacteriaiCAB13022; CAB13022; BSU11650
    GeneIDi939807
    KEGGibsu:BSU11650
    PATRICifig|224308.179.peg.1254

    Entry informationi

    Entry nameiTENA_BACSU
    AccessioniPrimary (citable) accession number: P25052
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: May 23, 2018
    This is version 121 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
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    Main funding by: National Institutes of Health