ID A0A2H0ZS62_CANAR Unreviewed; 330 AA.
AC A0A2H0ZS62; A0A5Q7YE06;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Name=THI4 {ECO:0000256|HAMAP-Rule:MF_03158};
GN ORFNames=B9J08_003099 {ECO:0000313|EMBL:PIS51509.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS51509.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS51509.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS51509.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
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 207 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:PIS51509.1}.
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DR EMBL; PEKT02000007; PIS51509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H0ZS62; -.
DR STRING; 498019.A0A2H0ZS62; -.
DR EnsemblFungi; B9J08_003099-t37_1; B9J08_003099-t37_1-p1; B9J08_003099.
DR VEuPathDB; FungiDB:B9J08_003099; -.
DR VEuPathDB; FungiDB:CJI96_0001634; -.
DR VEuPathDB; FungiDB:CJI97_003172; -.
DR VEuPathDB; FungiDB:CJJ07_005310; -.
DR VEuPathDB; FungiDB:CJJ09_001007; -.
DR VEuPathDB; FungiDB:QG37_05249; -.
DR OMA; MFPRIVV; -.
DR OrthoDB; 1382331at2759; -.
DR Proteomes; UP000230249; 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:UP000230249};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_03158}; Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 291..293
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT MOD_RES 207
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
SQ SEQUENCE 330 AA; 35724 MW; B4C0660293DD3A1A CRC64;
MSPPTMVQKP VGNVDLKTPV VRLESNSTDS QVSFADWDKF NFAPIRESTV SRAMTKRYFN
DLDKYTESDV IVVGAGSAGL SAAYVLAKNR PDLKIAIIEA SVSPGGGCWL GGQLFSAMVM
RKPAHLFLDE LEIAYEDEGD YVVVKHAALF MSTLMSKTLQ FPNVKLFNAT AVEDLITRRD
ESTGELRIAG VVTNWTLVTL NHDTQSCMDP NTLNANVVLS TTGHDGPFGA FCAKRLESLR
PKSANEPFEL GGMRGLDMNK AEDAIVKGTR EVAPGLVIAG MELAEVDGSN RMGPTFGAMA
LSGVKAAESV LNVYETRRKQ NEACYGGLQN
//
