ID THI1_PANTH Reviewed; 409 AA. AC P45741; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 13-SEP-2023, entry version 96. DE RecName: Full=Thiaminase-1; DE EC=2.5.1.2; DE AltName: Full=Thiaminase I; DE AltName: Full=Thiamine pyridinylase; DE Flags: Precursor; OS Paenibacillus thiaminolyticus (Bacillus thiaminolyticus). OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=49283; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-50, AND MASS RP SPECTROMETRY. RX PubMed=8631946; DOI=10.1074/jbc.271.7.3445; RA Costello C.A., Kelleher N.L., Abe M., McLafferty F.W., Begley T.P.; RT "Mechanistic studies on thiaminase I. Overexpression and identification of RT the active site nucleophile."; RL J. Biol. Chem. 271:3445-3452(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=9843405; DOI=10.1021/bi981673l; RA Campobasso N., Costello C.A., Kinsland C., Begley T.P., Ealick S.E.; RT "Crystal structure of thiaminase-I from Bacillus thiaminolyticus at 2.0-A RT resolution."; RL Biochemistry 37:15981-15989(1998). CC -!- FUNCTION: Degrades thiamine by replacing its thiazole moiety with a CC wide range of nucleophiles. CC -!- CATALYTIC ACTIVITY: CC Reaction=pyridine + thiamine = 5-(2-hydroxyethyl)-4-methylthiazole + CC heteropyrithiamine; Xref=Rhea:RHEA:17697, ChEBI:CHEBI:11222, CC ChEBI:CHEBI:16227, ChEBI:CHEBI:17957, ChEBI:CHEBI:18385; EC=2.5.1.2; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- INDUCTION: Inhibited by organomercurials and iodoacetate. CC -!- MASS SPECTROMETRY: Mass=42198; Mass_error=1; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:8631946}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U17168; AAC44156.1; -; Genomic_DNA. DR PIR; T47118; T47118. DR PDB; 2THI; X-ray; 2.50 A; A/B=31-409. DR PDB; 3THI; X-ray; 2.00 A; A=39-409. DR PDB; 4THI; X-ray; 2.00 A; A=39-400. DR PDBsum; 2THI; -. DR PDBsum; 3THI; -. DR PDBsum; 4THI; -. DR AlphaFoldDB; P45741; -. DR SMR; P45741; -. DR BioCyc; MetaCyc:MONOMER-16819; -. DR BRENDA; 2.5.1.2; 710. DR EvolutionaryTrace; P45741; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050332; F:thiamine pyridinylase activity; IEA:UniProtKB-EC. DR GO; GO:0009230; P:thiamine catabolic process; IEA:UniProtKB-KW. DR CDD; cd13524; PBP2_Thiaminase_I; 1. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2. DR InterPro; IPR006059; SBP. DR InterPro; IPR030901; Thiaminase_BcmE. DR NCBIfam; TIGR04541; thiaminase_BcmE; 1. DR Pfam; PF01547; SBP_bac_1; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Secreted; Signal; KW Thiamine catabolism; Transferase. FT SIGNAL 1..29 FT CHAIN 30..409 FT /note="Thiaminase-1" FT /id="PRO_0000022489" FT ACT_SITE 143 FT /note="Nucleophile" FT ACT_SITE 271 FT /note="Proton acceptor" FT VARIANT 30 FT /note="Missing (in part of the chains)" FT VARIANT 31 FT /note="Missing (in part of the chains)" FT MUTAGEN 143 FT /note="C->S: Loss of activity." FT MUTAGEN 271 FT /note="E->Q: Loss of activity." FT STRAND 40..44 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 52..66 FT /evidence="ECO:0007829|PDB:3THI" FT STRAND 70..74 FT /evidence="ECO:0007829|PDB:3THI" FT TURN 79..81 FT /evidence="ECO:0007829|PDB:3THI" FT STRAND 90..94 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 98..103 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 123..128 FT /evidence="ECO:0007829|PDB:3THI" FT STRAND 138..143 FT /evidence="ECO:0007829|PDB:3THI" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 154..157 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 162..169 FT /evidence="ECO:0007829|PDB:3THI" FT STRAND 181..187 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 192..207 FT /evidence="ECO:0007829|PDB:3THI" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 224..237 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 239..243 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 253..260 FT /evidence="ECO:0007829|PDB:3THI" FT STRAND 262..269 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 272..276 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 277..281 FT /evidence="ECO:0007829|PDB:3THI" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:3THI" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:4THI" FT STRAND 298..307 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 313..324 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 326..333 FT /evidence="ECO:0007829|PDB:3THI" FT STRAND 346..349 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 350..356 FT /evidence="ECO:0007829|PDB:3THI" FT TURN 357..359 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 362..370 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 384..391 FT /evidence="ECO:0007829|PDB:3THI" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:3THI" FT HELIX 395..399 FT /evidence="ECO:0007829|PDB:3THI" SQ SEQUENCE 409 AA; 45214 MW; 9A5BD988C5C9182A CRC64; MSKVKGFIYK PLMVMLALLL VVVSPAGAGA AHSDASSDIT LKVAIYPYVP DPARFQAAVL DQWQRQEPGV KLEFTDWDSY SADPPDDLDV FVLDSIFLSH FVDAGYLLPF GSQDIDQAED VLPFALQGAK RNGEVYGLPQ ILCTNLLFYR KGDLKIGQVD NIYELYKKIG TSHSEQIPPP QNKGLLINMA GGTTKASMYL EALIDVTGQY TEYDLLPPLD PLNDKVIRGL RLLINMAGEK PSQYVPEDGD AYVRASWFAQ GSGRAFIGYS ESMMRMGDYA EQVRFKPISS SAGQDIPLFY SDVVSVNSKT AHPELAKKLA NVMASADTVE QALRPQADGQ YPQYLLPARH QVYEALMQDY PIYSELAQIV NKPSNRVFRL GPEVRTWLKD AKQVLPEALG LTDVSSLAS //