ID A0A175VUA7_9PEZI Unreviewed; 326 AA.
AC A0A175VUA7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Thiamine thiazole synthase {ECO:0000256|HAMAP-Rule:MF_03158};
DE AltName: Full=Thiazole biosynthetic enzyme {ECO:0000256|HAMAP-Rule:MF_03158};
DE EC=2.4.2.60 {ECO:0000256|HAMAP-Rule:MF_03158};
GN ORFNames=MMYC01_208219 {ECO:0000313|EMBL:KXX74610.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX74610.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX74610.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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. May have
CC additional roles in adaptation to various stress conditions and in DNA
CC damage tolerance. {ECO:0000256|HAMAP-Rule:MF_03158}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03158};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03158};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000256|HAMAP-Rule:MF_03158};
CC -!- SUBUNIT: Homooctamer. {ECO:0000256|HAMAP-Rule:MF_03158}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03158}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03158}.
CC -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC 215 to a reaction intermediate, generating a dehydroalanine residue.
CC {ECO:0000256|HAMAP-Rule:MF_03158}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000256|HAMAP-
CC Rule:MF_03158}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXX74610.1}.
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DR EMBL; LCTW02000335; KXX74610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175VUA7; -.
DR STRING; 100816.A0A175VUA7; -.
DR VEuPathDB; FungiDB:MMYC01_208219; -.
DR OrthoDB; 1382331at2759; -.
DR Proteomes; UP000078237; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 6.10.250.2840; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR HAMAP; MF_03158; THI4; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027495; Sti35.
DR InterPro; IPR002922; Thi4_fam.
DR NCBIfam; TIGR00292; sulfide-dependent adenosine diphosphate thiazole synthase; 1.
DR PANTHER; PTHR43422; THIAMINE THIAZOLE SYNTHASE; 1.
DR PANTHER; PTHR43422:SF3; THIAMINE THIAZOLE SYNTHASE; 1.
DR Pfam; PF01946; Thi4; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03158};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03158};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03158};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03158};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03158};
KW Reference proteome {ECO:0000313|Proteomes:UP000078237};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_03158}; Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 107..108
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 294..296
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT MOD_RES 215
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
SQ SEQUENCE 326 AA; 34834 MW; EBEFFB6BCB361528 CRC64;
MAPSAVSPAQ KHAQLAVHPK KAGDATVDDG ATQLSKPLVD LMGNWDSFSF APIRESTVSR
AMTRRYFADL DAHAESDVVI IGAGSCGLSC AYTLAKLRPD LRISLVEAGV SPGGGAWLGG
QLFSAMVLRK PADVFLSEVG VPFEDEGDYV VVKHAALFTS TVLSRVLAMP NVKLFNATAV
EDLITRPDED GEGVRIAGVV TNWTLVSMHH DDQSCMDPNT INAPVVVSTT GHDGPFGAFS
VKRLVSMKQL QQLEGMRGLD MLRAEDSIVK NTREIVPGLI VGGMELSEID GANRMGPTFG
AMALSGVKAA EEVLRVFDLR KKQNEL
//
