AC   MF_00089;
DC   Protein; auto
TR   HAMAP; MF_00089; -; 1; level=0
XX
Names: ThiC
XX
ID   THIC
DE   RecName: Full=Phosphomethylpyrimidine synthase;
DE            EC=4.1.99.17;
DE   AltName: Full=Hydroxymethylpyrimidine phosphate synthase;
DE            Short=HMP-P synthase;
DE            Short=HMP-phosphate synthase;
DE            Short=HMPP synthase;
DE   AltName: Full=Thiamine biosynthesis protein ThiC;
GN   Name=thiC;
XX
CC   -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine
CC       phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR)
CC       in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-
CC         methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + CO +
CC         5'-deoxyadenosine + formate + L-methionine + 3 H(+);
CC         Xref=Rhea:RHEA:24840, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:17245, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58354, ChEBI:CHEBI:59789, ChEBI:CHEBI:137981;
CC         EC=4.1.99.17;
case <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine.;
end case
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
case <OC:Pseudomonadota>
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SIMILARITY: Belongs to the ThiC family.
XX
DR   Pfam; PF01964; ThiC; 1; trigger=no
DR   NCBIfam; TIGR00190; ThiC; 1; trigger=no
XX
case <FTGroup:2>
KW   4Fe-4S
KW   Iron
KW   Iron-sulfur
end case
KW   Lyase
KW   Metal-binding
KW   S-adenosyl-L-methionine
KW   Thiamine biosynthesis
case <FTGroup:1>
KW   Zinc
end case
XX
case <FTGroup:1>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0016829; F:lyase activity
case <FTGroup:2>
GO   GO:0051536; F:iron-sulfur cluster binding
end case
GO   GO:0009229; P:thiamine diphosphate biosynthetic process
XX
FT   From: THIC_CAUVC (Q9A6Q5)
FT   BINDING         333..335
FT                   /ligand="substrate"
FT   Condition: S-[RKY]-G
FT   BINDING         374..377
FT                   /ligand="substrate"
FT   Condition: [DN]-x-x-R
FT   BINDING         417
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         481
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         561
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Group: 2; Condition: C
FT   BINDING         564
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Group: 2; Condition: C
FT   BINDING         569
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Group: 2; Condition: C
FT   BINDING         219
FT                   /ligand="substrate"
FT   Optional; Condition: N
FT   BINDING         248
FT                   /ligand="substrate"
FT   Condition: M
FT   BINDING         277
FT                   /ligand="substrate"
FT   Condition: Y
FT   BINDING         313
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         413
FT                   /ligand="substrate"
FT   Condition: E
FT   BINDING         440
FT                   /ligand="substrate"
FT   Condition: [YF]
XX
Size: 424-721;
Related: None;
Template: Q9A6Q5; Q9L9I7; P30136; P45740;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: MF_00097 (thiE)
 Cter: None
Duplicate: in GEOMG, METAC, METBF, METMA, METST, METTH, MOOTA, SYNC1, SACS2
Plasmid: in RHIEC, RHIET, RHIME
Comments: Possible N-terminal domain in some bacterial ThiC.
 Fused with ThiE (thiamine-phosphate pyrophosphorylase, MF_00097) in BIFLO.
XX
# Version: 36
# Last updated date: 2024-09-03
# Created date: 2005-02-28
//