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Protein

Thiaminase-1

Gene
N/A
Organism
Paenibacillus thiaminolyticus (Bacillus thiaminolyticus)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei143Nucleophile1
Active sitei271Proton acceptor1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Thiamine catabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16819.
BRENDAi2.5.1.2. 710.

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi143C → S: Loss of activity. 1
Mutagenesisi271E → Q: Loss of activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Add BLAST29
ChainiPRO_000002248930 – 409Thiaminase-1Add BLAST380

Expressioni

Inductioni

Inhibited by organomercurials and iodoacetate.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1409
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 44Combined sources5
Helixi52 – 66Combined sources15
Beta strandi70 – 74Combined sources5
Turni79 – 81Combined sources3
Beta strandi90 – 94Combined sources5
Helixi95 – 97Combined sources3
Helixi98 – 103Combined sources6
Helixi112 – 114Combined sources3
Helixi118 – 120Combined sources3
Helixi123 – 128Combined sources6
Beta strandi138 – 143Combined sources6
Beta strandi145 – 150Combined sources6
Helixi154 – 157Combined sources4
Helixi162 – 169Combined sources8
Beta strandi181 – 187Combined sources7
Helixi192 – 207Combined sources16
Beta strandi219 – 221Combined sources3
Helixi224 – 237Combined sources14
Helixi239 – 243Combined sources5
Helixi253 – 260Combined sources8
Beta strandi262 – 269Combined sources8
Helixi272 – 276Combined sources5
Helixi277 – 281Combined sources5
Beta strandi283 – 286Combined sources4
Beta strandi289 – 293Combined sources5
Beta strandi298 – 307Combined sources10
Helixi313 – 324Combined sources12
Helixi326 – 333Combined sources8
Beta strandi346 – 349Combined sources4
Helixi350 – 356Combined sources7
Turni357 – 359Combined sources3
Helixi362 – 370Combined sources9
Helixi384 – 391Combined sources8
Turni392 – 394Combined sources3
Helixi395 – 399Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2THIX-ray2.50A/B31-409[»]
3THIX-ray2.00A39-409[»]
4THIX-ray2.00A39-400[»]
ProteinModelPortaliP45741.
SMRiP45741.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45741.

Family & Domainsi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR006059. SBP_1_dom.
IPR030901. Thiaminase_BcmE.
[Graphical view]
PfamiPF01547. SBP_bac_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04541. thiaminase_BcmE. 1 hit.

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)DescriptionActionsGraphical viewLength
Natural varianti30Missing in part of the chains. 1
Natural varianti31Missing in part of the chains. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17168 Genomic DNA. Translation: AAC44156.1.
PIRiT47118.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17168 Genomic DNA. Translation: AAC44156.1.
PIRiT47118.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2THIX-ray2.50A/B31-409[»]
3THIX-ray2.00A39-409[»]
4THIX-ray2.00A39-400[»]
ProteinModelPortaliP45741.
SMRiP45741.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16819.
BRENDAi2.5.1.2. 710.

Miscellaneous databases

EvolutionaryTraceiP45741.

Family and domain databases

InterProiIPR006059. SBP_1_dom.
IPR030901. Thiaminase_BcmE.
[Graphical view]
PfamiPF01547. SBP_bac_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04541. thiaminase_BcmE. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 81 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

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.