AC   MF_00443;
DC   Protein; auto
TR   HAMAP; MF_00443; -; 1; level=0
XX
Names: ThiG
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ID   THIG
DE   RecName: Full=Thiazole synthase;
DE            EC=2.8.1.10;
GN   Name=thiG;
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CC   -!- FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate
CC       (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is
CC       provided by the thiocarboxylate moiety of the carrier protein ThiS. In
CC       vitro, sulfur can be provided by H(2)S.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-
CC         carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-
CC         carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-
CC         carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O;
CC         Xref=Rhea:RHEA:26297, Rhea:RHEA-COMP:12908, Rhea:RHEA-COMP:12909,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:62899, ChEBI:CHEBI:77846, ChEBI:CHEBI:90619,
CC         ChEBI:CHEBI:90778; EC=2.8.1.10;
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC   -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or ThiS.
case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
else case not <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- SIMILARITY: Belongs to the ThiG family.
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DR   Pfam; PF05690; ThiG; 1; trigger=no
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case not <OG:Chloroplast>
KW   Cytoplasm
end case
KW   Schiff base
KW   Thiamine biosynthesis
KW   Transferase
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GO   GO:0016783; F:sulfurtransferase activity
GO   GO:0009228; P:thiamine biosynthetic process
case <OG:Chloroplast>
GO   GO:0009507; C:chloroplast
else case not <OG:Chloroplast>
GO   GO:0005737; C:cytoplasm
end case
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FT   From: THIG_BACSU (O31618)
FT   BINDING         185..186
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT   Condition: A-G
FT   BINDING         207..208
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT   Condition: x-[TS]
FT   ACT_SITE        98
FT                   /note="Schiff-base intermediate with DXP"
FT   Condition: K
FT   BINDING         159
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT   Condition: G
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Size: 252-337;
Related: None;
Template: O31618; P30139;
Scope:
 Bacteria
 Plastid
Fusion:
 Nter: <thiO>; <thiS>
 Cter: None
Duplicate: in SYNC1
Plasmid: in ERWAM, ERWPY, RHIET, RHIME, STAS1
Comments: ThiO N-terminal domain (glycine oxidase) in NOSS1, TRIV2, and SYNY3.
 Possible wrong start in CYACA.
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# Revision 1.39 2022/11/19
//