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P45741

- THI1_PANTH

UniProt

P45741 - THI1_PANTH

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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

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-KW
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 – 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 – 445Combined sources
Helixi52 – 6615Combined sources
Beta strandi70 – 745Combined sources
Turni79 – 813Combined sources
Beta strandi90 – 945Combined sources
Helixi95 – 973Combined sources
Helixi98 – 1036Combined sources
Helixi112 – 1143Combined sources
Helixi118 – 1203Combined sources
Helixi123 – 1286Combined sources
Beta strandi138 – 1436Combined sources
Beta strandi145 – 1506Combined sources
Helixi154 – 1574Combined sources
Helixi162 – 1698Combined sources
Beta strandi181 – 1877Combined sources
Helixi192 – 20716Combined sources
Beta strandi219 – 2213Combined sources
Helixi224 – 23714Combined sources
Helixi239 – 2435Combined sources
Helixi253 – 2608Combined sources
Beta strandi262 – 2698Combined sources
Helixi272 – 2765Combined sources
Helixi277 – 2815Combined sources
Beta strandi283 – 2864Combined sources
Beta strandi289 – 2935Combined sources
Beta strandi298 – 30710Combined sources
Helixi313 – 32412Combined sources
Helixi326 – 3338Combined sources
Beta strandi346 – 3494Combined sources
Helixi350 – 3567Combined sources
Turni357 – 3593Combined sources
Helixi362 – 3709Combined sources
Helixi384 – 3918Combined sources
Turni392 – 3943Combined sources
Helixi395 – 3995Combined sources

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

        10         20         30         40         50
MSKVKGFIYK PLMVMLALLL VVVSPAGAGA AHSDASSDIT LKVAIYPYVP
60 70 80 90 100
DPARFQAAVL DQWQRQEPGV KLEFTDWDSY SADPPDDLDV FVLDSIFLSH
110 120 130 140 150
FVDAGYLLPF GSQDIDQAED VLPFALQGAK RNGEVYGLPQ ILCTNLLFYR
160 170 180 190 200
KGDLKIGQVD NIYELYKKIG TSHSEQIPPP QNKGLLINMA GGTTKASMYL
210 220 230 240 250
EALIDVTGQY TEYDLLPPLD PLNDKVIRGL RLLINMAGEK PSQYVPEDGD
260 270 280 290 300
AYVRASWFAQ GSGRAFIGYS ESMMRMGDYA EQVRFKPISS SAGQDIPLFY
310 320 330 340 350
SDVVSVNSKT AHPELAKKLA NVMASADTVE QALRPQADGQ YPQYLLPARH
360 370 380 390 400
QVYEALMQDY PIYSELAQIV NKPSNRVFRL GPEVRTWLKD AKQVLPEALG

LTDVSSLAS
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 29, 2014
This is version 74 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