AC   MF_00304;
DC   Protein; auto
TR   HAMAP; MF_00304; -; 1; level=0
XX
Names: Thi4
XX
ID   THI4
case <FTTag:dehydroala>
DE   RecName: Full=Thiamine thiazole synthase;
DE            EC=2.4.2.60;
else
DE   RecName: Full=Thiamine thiazole synthase;
DE            EC=2.4.2.59;
end case
GN   Name=thi4;
XX
case <FTTag:dehydroala>
CC   -!- FUNCTION: Involved in biosynthesis of the thiamine precursor thiazole.
CC       Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-
CC       (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an
CC       adenylated thiazole intermediate. The reaction includes an iron-
CC       dependent sulfide transfer from a conserved cysteine residue of the
CC       protein to a thiazole intermediate. The enzyme can only undergo a
CC       single turnover, which suggests it is a suicide enzyme.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) = [ADP-
CC         thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-methylthiazole-2-
CC         carboxylate + 2 H(+) + 3 H2O + nicotinamide; Xref=Rhea:RHEA:55708,
CC         Rhea:RHEA-COMP:14264, Rhea:RHEA-COMP:14265, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57540, ChEBI:CHEBI:90873,
CC         ChEBI:CHEBI:139151; EC=2.4.2.60;
CC   -!- PTM: During the catalytic reaction, a sulfide is transferred from
CC       #{Cys-165} to a reaction intermediate, generating a dehydroalanine
CC       residue.
else
CC   -!- FUNCTION: Involved in the biosynthesis of the thiazole moiety of
CC       thiamine. Catalyzes the conversion of NAD and glycine to adenosine
CC       diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an
CC       adenylated thiazole intermediate, using free sulfide as a source of
CC       sulfur.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + hydrogen sulfide + NAD(+) = ADP-5-ethyl-4-
CC         methylthiazole-2-carboxylate + H(+) + 3 H2O + nicotinamide;
CC         Xref=Rhea:RHEA:55704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29919, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:139151; EC=2.4.2.59;
end case
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers.
CC   -!- SIMILARITY: Belongs to the THI4 family.
XX
DR   NCBIfam; TIGR00292; TIGR00292; 1; trigger=no
XX
KW   Iron
KW   Metal-binding
KW   NAD
KW   Thiamine biosynthesis
KW   Transferase
XX
GO   GO:0005506; F:iron ion binding
GO   GO:0016763; F:pentosyltransferase activity
GO   GO:0009228; P:thiamine biosynthetic process
GO   GO:0052837; P:thiazole biosynthetic process
XX
FT   From: THI4_METJA (Q58018)
FT   BINDING         66..67
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT                   /note="in other chain"
FT   Condition: E-[RKQE]
FT   BINDING         164..166
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT   Optional; Condition: H-x-D
case not <FT:2>
FT   BINDING         166
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT   Condition: D
end case
FT   BINDING         166
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT   Condition: D
FT   BINDING         181
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT                   /note="in other chain"
FT   Condition: H
FT   BINDING         47
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT                   /note="in other chain"
FT   Optional; Condition: S
case not <FT:6>
FT   BINDING         47
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT                   /note="in other chain"
FT   Condition: A
end case
FT   BINDING         74
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT                   /note="in other chain"
FT   Condition: G
FT   BINDING         138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT                   /note="in other chain"
FT   Optional; Condition: [VIL]
FT   BINDING         184
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT                   /note="in other chain"
FT   Optional; Condition: S
FT   BINDING         230
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent
FT                   protomers"
FT                   /note="in other chain"
FT   Condition: [MLI]
FT   BINDING         240
FT                   /ligand="glycine"
FT                   /ligand_id="ChEBI:CHEBI:57305"
FT   Condition: R
FT   From: THI4_HALVD (D4GSS5)
FT   MOD_RES         165
FT                   /note="2,3-didehydroalanine (Cys)"
FT   Tag: dehydroala; Optional; Condition: C
XX
Size: 250-310;
Related: None;
Template: Q58018; P32318; D4GSS5;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None.
XX
# Revision 1.31 2023/06/01
//