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Protein

Aminopyrimidine aminohydrolase

Gene

tenA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei44 – 441Substrate2 Publications
    Sitei47 – 471Increases nucleophilicity of active site Cys1 Publication
    Active sitei135 – 1351Nucleophile1 Publication
    Binding sitei139 – 1391Substrate2 Publications
    Binding sitei163 – 1631Substrate2 Publications
    Active sitei205 – 2051Proton donor1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Thiamine biosynthesis

    Enzyme and pathway databases

    BioCyciBSUB:BSU11650-MONOMER.
    MetaCyc:BSU11650-MONOMER.
    RETL1328306-WGS:GSTH-251-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

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441D → A: 6300-fold reduction in catalytic efficiency. 1 Publication
    Mutagenesisi47 – 471Y → F: About 2-fold decrease in substrate affinity and 30-fold reduction in catalytic activity. 1 Publication
    Mutagenesisi112 – 1121Y → F: About 2-fold decrease in substrate affinity and 70-fold reduction in catalytic activity. 1 Publication
    Mutagenesisi135 – 1351C → A: Loss of catalytic activity. 1 Publication
    Mutagenesisi205 – 2051E → A: 2000-fold reduction in catalytic efficiency. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 236236Aminopyrimidine aminohydrolasePRO_0000192046Add
    BLAST

    Proteomic databases

    PaxDbiP25052.

    Expressioni

    Inductioni

    Strongly repressed by thiamine.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    IntActiP25052. 1 interaction.
    MINTiMINT-8367193.
    STRINGi224308.Bsubs1_010100006441.

    Structurei

    Secondary structure

    1
    236
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 108Combined sources
    Helixi12 – 198Combined sources
    Helixi22 – 298Combined sources
    Helixi34 – 6128Combined sources
    Helixi65 – 9329Combined sources
    Helixi97 – 1015Combined sources
    Helixi107 – 12014Combined sources
    Turni121 – 1233Combined sources
    Helixi125 – 14622Combined sources
    Helixi154 – 16310Combined sources
    Helixi166 – 18419Combined sources
    Helixi188 – 21326Combined sources
    Helixi221 – 2255Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-226.
    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.
    InterProiIPR016084. Haem_Oase-like_multi-hlx.
    IPR004305. Thiaminase-2/PQQC.
    IPR027574. Thiaminase_II.
    [Graphical view]
    PfamiPF03070. TENA_THI-4. 1 hit.
    [Graphical view]
    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.
    PATRICi18974047. VBIBacSub10457_1217.

    Cross-referencesi

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-226.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP25052. 1 interaction.
    MINTiMINT-8367193.
    STRINGi224308.Bsubs1_010100006441.

    Proteomic databases

    PaxDbiP25052.

    Protocols and materials databases

    DNASUi939807.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB13022; CAB13022; BSU11650.
    GeneIDi939807.
    KEGGibsu:BSU11650.
    PATRICi18974047. VBIBacSub10457_1217.

    Phylogenomic databases

    eggNOGiENOG4105ETU. Bacteria.
    COG0819. LUCA.
    HOGENOMiHOG000225158.
    InParanoidiP25052.
    KOiK03707.
    OMAiCISHPFV.
    PhylomeDBiP25052.

    Enzyme and pathway databases

    UniPathwayiUPA00060.
    BioCyciBSUB:BSU11650-MONOMER.
    MetaCyc:BSU11650-MONOMER.
    RETL1328306-WGS:GSTH-251-MONOMER.
    BRENDAi3.5.99.2. 658.

    Miscellaneous databases

    EvolutionaryTraceiP25052.

    Family and domain databases

    Gene3Di1.20.910.10. 1 hit.
    InterProiIPR016084. Haem_Oase-like_multi-hlx.
    IPR004305. Thiaminase-2/PQQC.
    IPR027574. Thiaminase_II.
    [Graphical view]
    PfamiPF03070. TENA_THI-4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48613. SSF48613. 1 hit.
    TIGRFAMsiTIGR04306. salvage_TenA. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiTENA_BACSU
    AccessioniPrimary (citable) accession number: P25052
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: September 7, 2016
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.