SubmitCancel

Skip Header

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

P45741

- THI1_PANTH

UniProt

P45741 - THI1_PANTH

(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)

Protein
Thiaminase-1
Gene
N/A
Organism
Paenibacillus thiaminolyticus (Bacillus thiaminolyticus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

  1. thiamine catabolic process Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

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 – 2929
Add
BLAST
Chaini30 – 409380Thiaminase-1
PRO_0000022489Add
BLAST

Expressioni

Inductioni

Inhibited by organomercurials and iodoacetate.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

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.

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...

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 16, 2013
This is version 72 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

Similar proteinsi