HAMAP rule MF_03158
General rule information
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Accession | MF_03158 |
Dates | 13-JAN-2012 (Created)
1-JUN-2023 (Last updated, Version 12) |
Name | THI4 |
Scope(s) |
Eukaryota |
Template(s) | P32318 (THI4_YEAST); Q38814 (THI4_ARATH); Q1K6I4 (THI4_NEUCR); [ Recover all ] |
Triggered by |
HAMAP; MF_03158 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | THI4 |
case <OC:Viridiplantae> | |
Protein name | RecName: Full=Thiamine thiazole synthase, chloroplastic; AltName: Full=Thiazole biosynthetic enzyme; EC=2.4.2.60; |
else | |
Protein name | RecName: Full=Thiamine thiazole synthase; AltName: Full=Thiazole biosynthetic enzyme; EC=2.4.2.60; |
end case | |
case <OC:Saccharomycotina> | |
Gene name | Name=THI4; |
else case <OC:Trichocomaceae> | |
Gene name | Name=thiA; |
else case <OC:Viridiplantae> | |
Gene name | Name=THI1; |
end case |
Comments
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FUNCTION | Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5- (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron- dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance. |
CATALYTIC ACTIVITY | Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) = [ADP- thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-methylthiazole-2- carboxylate + 2 H(+) + 3 H2O + nicotinamide; Xref=Rhea:RHEA:55708, Rhea:RHEA-COMP:14264, Rhea:RHEA-COMP:14265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57305, ChEBI:CHEBI:57540, ChEBI:CHEBI:90873, ChEBI:CHEBI:139151; EC=2.4.2.60; |
COFACTOR | Name=Fe cation; Xref=ChEBI:CHEBI:24875; Note=Binds 1 Fe cation per subunit.; |
SUBUNIT | Homooctamer. |
case <OC:Viridiplantae> | |
SUBCELLULAR LOCATION | Plastid, chloroplast. |
else | |
SUBCELLULAR LOCATION | Cytoplasm. Nucleus. |
end case | |
PTM | During the catalytic reaction, a sulfide is transferred from #{Cys-205} to a reaction intermediate, generating a dehydroalanine residue. |
case <OC:Viridiplantae> and not <AnyFeature:TransitC> | |
MISCELLANEOUS | This protein may be expected to contain an N-terminal transit peptide but none has been predicted. |
end case | |
SIMILARITY | Belongs to the THI4 family. |
Keywords
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case <OC:Viridiplantae> | |
Chloroplast | |
Plastid | |
else | |
Cytoplasm | |
Nucleus | |
end case | |
Iron | |
Metal-binding | |
NAD | |
Thiamine biosynthesis | |
Transferase |
Gene Ontology
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GO:0005506; Molecular function:iron ion binding | |
GO:0016763; Molecular function:pentosyltransferase activity | |
GO:0005829; Cellular component:cytosol | |
case <OCellular component:Viridiplantae> | |
GO:0009570; Cellular component:chloroplast stroma | |
end case | |
GO:0009228; Biological process:thiamine biosynthetic process | |
GO:0052837; Biological process:thiazole biosynthetic process |
Cross-references
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Features
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From: THI4_YEAST (P32318) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 97 | 98 | /ligand="substrate" | E-x | ||||||||
BINDING | 301 | 303 | /ligand="substrate" | R-M-x | ||||||||
BINDING | 76 | 76 | /ligand="substrate" | |||||||||
BINDING | 105 | 105 | /ligand="substrate" | |||||||||
BINDING | 170 | 170 | /ligand="substrate" | |||||||||
BINDING | 207 | 207 | /ligand="substrate" | D | ||||||||
BINDING | 237 | 237 | /ligand="substrate" | H | ||||||||
BINDING | 291 | 291 | /ligand="substrate" | |||||||||
MOD_RES | 205 | 205 | /note="2,3-didehydroalanine (Cys)" | C |
Additional information
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Size range | 283-383 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |