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Annotation rule MF_00443
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General rule information [?]

Accession MF_00443
Dates 28-AUG-2001 (Created)
18-NOV-2019 (Last updated, Version 35)
Name ThiG
Templates O31618 (THIG_BACSU); P30139 (THIG_ECOLI): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Thiazole synthase;
Gene name

Comments [?]

Function Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Catalytic activity RHEA:26297: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O
Pathway Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Subunit Homotetramer. Forms heterodimers with either ThiH or ThiS.
case <OG:Chloroplast>
Subcellular location Plastid, chloroplast.
else case not <OG:Chloroplast>
Subcellular location Cytoplasm.
end case
Similarity Belongs to the ThiG family.

Keywords [?]

case not <OG:Chloroplast>
end case

Gene Ontology [?]

GO:0016783; Molecular function: sulfurtransferase activity.
GO:0009228; Biological process: thiamine biosynthetic process.
case <OG:Chloroplast>
GO:0009507; Cellular component: chloroplast.
else case not <OG:Chloroplast>
GO:0005737; Cellular component: cytoplasm.
end case

Cross-references [?]

Pfam PF05690; ThiG; 1;

Features [?]

From: THIG_BACSU (O31618)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     185     186       DXP binding     A-G  
REGION     207     208       DXP binding     x-[TS]  
ACT_SITE     98     98       Schiff-base intermediate with DXP     K  
BINDING     159     159       DXP; via amide nitrogen     G  

Additional information [?]

Size range 252-337 amino acids
Related rules None
Fusion Nter: <thiO>, <thiS>; Cter: None
Comments ThiO N-terminal domain (glycine oxidase) in NOSS1, TRIV2, and SYNY3. Possible wrong start in CYACA.