Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P45741

- THI1_PANTH

UniProt

P45741 - THI1_PANTH

Protein

Thiaminase-1

Gene
N/A
Organism
Paenibacillus thiaminolyticus (Bacillus thiaminolyticus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Degrades thiamine by replacing its thiazole moiety with a wide range of nucleophiles.

    Catalytic activityi

    Thiamine + pyridine = 1-((4-amino-2-methylpyrimidin-5-yl)methyl)pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei143 – 1431Nucleophile
    Active sitei271 – 2711Proton acceptor

    GO - Molecular functioni

    1. thiamine pyridinylase activity Source: UniProtKB-EC
    2. transporter activity Source: InterPro

    GO - Biological processi

    1. thiamine catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Thiamine catabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16819.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thiaminase-1 (EC:2.5.1.2)
    Alternative name(s):
    Thiaminase I
    Thiamine pyridinylase
    OrganismiPaenibacillus thiaminolyticus (Bacillus thiaminolyticus)
    Taxonomic identifieri49283 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi143 – 1431C → S: Loss of activity.
    Mutagenesisi271 – 2711E → Q: Loss of activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Add
    BLAST
    Chaini30 – 409380Thiaminase-1PRO_0000022489Add
    BLAST

    Expressioni

    Inductioni

    Inhibited by organomercurials and iodoacetate.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    409
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 445
    Helixi52 – 6615
    Beta strandi70 – 745
    Turni79 – 813
    Beta strandi90 – 945
    Helixi95 – 973
    Helixi98 – 1036
    Helixi112 – 1143
    Helixi118 – 1203
    Helixi123 – 1286
    Beta strandi138 – 1436
    Beta strandi145 – 1506
    Helixi154 – 1574
    Helixi162 – 1698
    Beta strandi181 – 1877
    Helixi192 – 20716
    Beta strandi219 – 2213
    Helixi224 – 23714
    Helixi239 – 2435
    Helixi253 – 2608
    Beta strandi262 – 2698
    Helixi272 – 2765
    Helixi277 – 2815
    Beta strandi283 – 2864
    Beta strandi289 – 2935
    Beta strandi298 – 30710
    Helixi313 – 32412
    Helixi326 – 3338
    Beta strandi346 – 3494
    Helixi350 – 3567
    Turni357 – 3593
    Helixi362 – 3709
    Helixi384 – 3918
    Turni392 – 3943
    Helixi395 – 3995

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2THIX-ray2.50A/B31-409[»]
    3THIX-ray2.00A39-409[»]
    4THIX-ray2.00A39-400[»]
    ProteinModelPortaliP45741.
    SMRiP45741. Positions 39-400.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45741.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR006059. Solute-bd_1_bac.
    [Graphical view]
    PfamiPF01547. SBP_bac_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P45741-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKVKGFIYK PLMVMLALLL VVVSPAGAGA AHSDASSDIT LKVAIYPYVP    50
    DPARFQAAVL DQWQRQEPGV KLEFTDWDSY SADPPDDLDV FVLDSIFLSH 100
    FVDAGYLLPF GSQDIDQAED VLPFALQGAK RNGEVYGLPQ ILCTNLLFYR 150
    KGDLKIGQVD NIYELYKKIG TSHSEQIPPP QNKGLLINMA GGTTKASMYL 200
    EALIDVTGQY TEYDLLPPLD PLNDKVIRGL RLLINMAGEK PSQYVPEDGD 250
    AYVRASWFAQ GSGRAFIGYS ESMMRMGDYA EQVRFKPISS SAGQDIPLFY 300
    SDVVSVNSKT AHPELAKKLA NVMASADTVE QALRPQADGQ YPQYLLPARH 350
    QVYEALMQDY PIYSELAQIV NKPSNRVFRL GPEVRTWLKD AKQVLPEALG 400
    LTDVSSLAS 409
    Length:409
    Mass (Da):45,214
    Last modified:November 1, 1995 - v1
    Checksum:i9A5BD988C5C9182A
    GO

    Mass spectrometryi

    Molecular mass is 42127±1 Da from positions 31 - 409. Determined by ESI. 1 Publication
    Molecular mass is 42198±1 Da from positions 30 - 409. Determined by ESI. 1 Publication
    Molecular mass is 42255±1 Da from positions 29 - 409. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301Missing in part of the chains.
    Natural varianti31 – 311Missing in part of the chains.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17168 Genomic DNA. Translation: AAC44156.1.
    PIRiT47118.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17168 Genomic DNA. Translation: AAC44156.1 .
    PIRi T47118.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2THI X-ray 2.50 A/B 31-409 [» ]
    3THI X-ray 2.00 A 39-409 [» ]
    4THI X-ray 2.00 A 39-400 [» ]
    ProteinModelPortali P45741.
    SMRi P45741. Positions 39-400.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16819.

    Miscellaneous databases

    EvolutionaryTracei P45741.

    Family and domain databases

    InterProi IPR006059. Solute-bd_1_bac.
    [Graphical view ]
    Pfami PF01547. SBP_bac_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mechanistic studies on thiaminase I. Overexpression and identification of the active site nucleophile."
      Costello C.A., Kelleher N.L., Abe M., McLafferty F.W., Begley T.P.
      J. Biol. Chem. 271:3445-3452(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-50, MASS SPECTROMETRY.
    2. "Crystal structure of thiaminase-I from Bacillus thiaminolyticus at 2.0-A resolution."
      Campobasso N., Costello C.A., Kinsland C., Begley T.P., Ealick S.E.
      Biochemistry 37:15981-15989(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiTHI1_PANTH
    AccessioniPrimary (citable) accession number: P45741
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3