P45741 (THI1_PANTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Thiaminase-1 EC=2.5.1.2 Alternative name(s): Thiaminase I Thiamine pyridinylase
Organism	Paenibacillus thiaminolyticus (Bacillus thiaminolyticus)
Taxonomic identifier	49283 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Thiamine catabolism
Cellular component	Secreted
Domain	Signal
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	thiamine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	thiamine pyridinylase activity Inferred from electronic annotation. Source: EC transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Chain

30 – 409

380

Thiaminase-1

PRO_0000022489

Sites

Active site

143

1

Nucleophile

Active site

271

1

Proton acceptor

Natural variations

Natural variant

30

1

Missing in part of the chains.

Natural variant

31

1

Missing in part of the chains.

Experimental info

Mutagenesis

143

1

C → S: Loss of activity.

Mutagenesis

271

1

E → Q: Loss of activity.

Secondary structure

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409

Helix Strand Turn

Details...

Beta strand

40 – 44

5

Helix

52 – 66

15

Beta strand

70 – 74

5

Turn

79 – 81

3

Beta strand

90 – 94

5

Helix

95 – 97

3

Helix

98 – 103

6

Helix

112 – 114

3

Helix

118 – 120

3

Helix

123 – 128

6

Beta strand

138 – 143

6

Beta strand

145 – 150

6

Helix

154 – 157

4

Helix

162 – 169

8

Beta strand

181 – 187

7

Helix

192 – 207

16

Beta strand

219 – 221

3

Helix

224 – 237

14

Helix

239 – 243

5

Helix

253 – 260

8

Beta strand

262 – 269

8

Helix

272 – 276

5

Helix

277 – 281

5

Beta strand

283 – 286

4

Beta strand

289 – 293

5

Beta strand

298 – 307

10

Helix

313 – 324

12

Helix

326 – 333

8

Beta strand

346 – 349

4

Helix

350 – 356

7

Turn

357 – 359

3

Helix

362 – 370

9

Helix

384 – 391

8

Turn

392 – 394

3

Helix

395 – 399

5

Sequences

	Sequence		Length	Mass (Da)
	P45741 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 9A5BD988C5C9182A	FASTA	409	45,214
	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

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.

PIR

T47118.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P45741.

SMR

P45741. Positions 39-400.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16819.

Family and domain databases

InterPro

IPR006059. Solute-bd_1_bac.
[Graphical view]

Pfam

PF01547. SBP_bac_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P45741.

Entry information

Entry name

THI1_PANTH

Accession

Primary (citable) accession number: P45741

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program