THI4_PUCGT
ID THI4_PUCGT Reviewed; 336 AA.
AC E3JV98;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Thiamine thiazole synthase {ECO:0000255|HAMAP-Rule:MF_03158};
DE EC=2.4.2.60 {ECO:0000255|HAMAP-Rule:MF_03158};
DE AltName: Full=Thiazole biosynthetic enzyme {ECO:0000255|HAMAP-Rule:MF_03158};
GN ORFNames=PGTG_01304;
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL;
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_03158};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03158};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|HAMAP-Rule:MF_03158};
CC -!- SUBUNIT: Homooctamer. {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03158}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC 219 to a reaction intermediate, generating a dehydroalanine residue.
CC {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC Rule:MF_03158}.
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DR EMBL; DS178264; EFP75973.1; -; Genomic_DNA.
DR RefSeq; XP_003320392.1; XM_003320344.2.
DR AlphaFoldDB; E3JV98; -.
DR SMR; E3JV98; -.
DR STRING; 5297.GMQ_18806T0; -.
DR EnsemblFungi; EFP75973; EFP75973; PGTG_01304.
DR GeneID; 10533053; -.
DR KEGG; pgr:PGTG_01304; -.
DR VEuPathDB; FungiDB:PGTG_01304; -.
DR eggNOG; KOG2960; Eukaryota.
DR HOGENOM; CLU_053727_0_0_1; -.
DR InParanoid; E3JV98; -.
DR OMA; MWGGGMM; -.
DR OrthoDB; 1111148at2759; -.
DR Proteomes; UP000008783; 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; 3.50.50.60; -; 1.
DR HAMAP; MF_03158; THI4; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027495; Sti35.
DR InterPro; IPR002922; Thi4_fam.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00292; TIGR00292; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Iron; Metal-binding; NAD; Nucleus; Reference proteome;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..336
FT /note="Thiamine thiazole synthase"
FT /id="PRO_0000415879"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 110..111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 298..300
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT MOD_RES 219
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
SQ SEQUENCE 336 AA; 35723 MW; BF7D75C19CE5E389 CRC64;
MSPPVATESM YKPTTIGTEA HDQALAAMKS NQAAPAKPVF KPEPAVNLEP IKFAPIKEHQ
VQRAMVRRYF QDMEERAISD VIIVGAGSAG LSCAYALGKA RPDLKITILE SNVAPGGGCW
LGGQLMSAMV CRKPADKFLD EVGVPYEDEG NFVVVKHAAL FTSTVLSKVL AMPNVKMFNA
TACEDLIIKP CPINPGVQRV AGCVTNWTLV SLNHDHQSCM DPSTITAPLV CSFAGHDGPF
GAFCVKRIAS AGLSEGLGDM RPLDMERAED HIANKTREIV PGLIVGGMEL SEFDGSARMG
PTFGAMLLSG KRAAEVALQS LGRVKVEEGE VVGSAK
