THI1_PANTH
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 03-AUG-2022, entry version 93.
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; Firmicutes; 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};
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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:MON-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 InterPro; IPR006059; SBP.
DR InterPro; IPR030901; Thiaminase_BcmE.
DR Pfam; PF01547; SBP_bac_1; 1.
DR TIGRFAMs; TIGR04541; thiaminase_BcmE; 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
