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P45741 (THI1_PANTH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiaminase-1

EC=2.5.1.2
Alternative name(s):
Thiaminase I
Thiamine pyridinylase
OrganismPaenibacillus thiaminolyticus (Bacillus thiaminolyticus)
Taxonomic identifier49283 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subunit structure

Monomer.

Subcellular location

Secreted.

Induction

Inhibited by organomercurials and iodoacetate.

Mass spectrometry

Molecular mass is 42127±1 Da from positions 31 - 409. Determined by ESI. Ref.1

Molecular mass is 42198±1 Da from positions 30 - 409. Determined by ESI. Ref.1

Molecular mass is 42255±1 Da from positions 29 - 409. Determined by ESI. Ref.1

Ontologies

Keywords
   Biological processThiamine catabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionTransferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processthiamine catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionthiamine pyridinylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929
Chain30 – 409380Thiaminase-1
PRO_0000022489

Sites

Active site1431Nucleophile
Active site2711Proton acceptor

Natural variations

Natural variant301Missing in part of the chains.
Natural variant311Missing in part of the chains.

Experimental info

Mutagenesis1431C → S: Loss of activity.
Mutagenesis2711E → Q: Loss of activity.

Secondary structure

................................................................ 409
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45741 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 9A5BD988C5C9182A

FASTA40945,214
        10         20         30         40         50         60 
MSKVKGFIYK PLMVMLALLL VVVSPAGAGA AHSDASSDIT LKVAIYPYVP DPARFQAAVL 

        70         80         90        100        110        120 
DQWQRQEPGV KLEFTDWDSY SADPPDDLDV FVLDSIFLSH FVDAGYLLPF GSQDIDQAED 

       130        140        150        160        170        180 
VLPFALQGAK RNGEVYGLPQ ILCTNLLFYR KGDLKIGQVD NIYELYKKIG TSHSEQIPPP 

       190        200        210        220        230        240 
QNKGLLINMA GGTTKASMYL EALIDVTGQY TEYDLLPPLD PLNDKVIRGL RLLINMAGEK 

       250        260        270        280        290        300 
PSQYVPEDGD AYVRASWFAQ GSGRAFIGYS ESMMRMGDYA EQVRFKPISS SAGQDIPLFY 

       310        320        330        340        350        360 
SDVVSVNSKT AHPELAKKLA NVMASADTVE QALRPQADGQ YPQYLLPARH QVYEALMQDY 

       370        380        390        400 
PIYSELAQIV NKPSNRVFRL GPEVRTWLKD AKQVLPEALG LTDVSSLAS 

« Hide

References

[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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17168 Genomic DNA. Translation: AAC44156.1.
PIRT47118.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2THIX-ray2.50A/B31-409[»]
3THIX-ray2.00A39-409[»]
4THIX-ray2.00A39-400[»]
ProteinModelPortalP45741.
SMRP45741. Positions 39-400.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16819.

Family and domain databases

InterProIPR006059. Solute-bd_1_bac.
[Graphical view]
PfamPF01547. SBP_bac_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP45741.

Entry information

Entry nameTHI1_PANTH
AccessionPrimary (citable) accession number: P45741
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references