ID   THI4_UROFA              Reviewed;         338 AA.
AC   Q9UVF8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-SEP-2015, entry version 58.
DE   RecName: Full=Thiamine thiazole synthase {ECO:0000255|HAMAP-Rule:MF_03158};
DE   AltName: Full=Planta-induced protein 4;
DE   AltName: Full=Thiazole biosynthetic enzyme {ECO:0000255|HAMAP-Rule:MF_03158};
GN   Name=THI2; Synonyms=PIG4;
OS   Uromyces fabae (Rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Uromyces.
OX   NCBI_TaxID=55588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10830262; DOI=10.1094/MPMI.2000.13.6.629;
RA   Sohn J., Voegele R.T., Mendgen K., Hahn M.;
RT   "High level activation of vitamin B1 biosynthesis genes in haustoria
RT   of the rust fungus Uromyces fabae.";
RL   Mol. Plant Microbe Interact. 13:629-636(2000).
CC   -!- FUNCTION: Involved in biosynthesis of the thiamine precursor
CC       thiazole. Catalyzes the conversion of NAD and glycine to adenosine
CC       diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid
CC       (ADT), an adenylated thiazole intermediate. The reaction includes
CC       an iron-dependent sulfide transfer from a conserved cysteine
CC       residue of the protein to a thiazole intermediate. The enzyme can
CC       only undergo a single turnover, which suggests it is a suicide
CC       enzyme. May have additional roles in adaptation to various stress
CC       conditions and in DNA damage tolerance. {ECO:0000255|HAMAP-
CC       Rule:MF_03158, ECO:0000269|PubMed:10830262}.
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-
CC       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   -!- TISSUE SPECIFICITY: Highly expressed in haustoria, and only in low
CC       amounts in intercellular hyphae. Found in the basal hyphae of the
CC       uredia, but not in the pedicels and only at very low levels in
CC       uredospores. {ECO:0000269|PubMed:10830262}.
CC   -!- PTM: During the catalytic reaction, a sulfide is transferred from
CC       Cys-221 to a reaction intermediate, generating a dehydroalanine
CC       residue. {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; AJ250427; CAB59856.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9UVF8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEA:InterPro.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_03158; THI4; 1.
DR   InterPro; IPR027495; Sti35.
DR   InterPro; IPR002922; Thi4_fam.
DR   TIGRFAMs; TIGR00292; TIGR00292; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Iron; Metal-binding; NAD; Nucleus; Thiamine biosynthesis.
FT   CHAIN         1    338       Thiamine thiazole synthase.
FT                                /FTId=PRO_0000034057.
FT   REGION      112    113       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      300    302       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING      91     91       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   BINDING     120    120       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   BINDING     185    185       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     223    223       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     238    238       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     290    290       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   MOD_RES     221    221       2,3-didehydroalanine (Cys).
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   338 AA;  36213 MW;  C3F9611094861230 CRC64;
     MSPVATESMY KPTTINQTAH QQAMDPLKSK QQSNATVNKP AFKPEPAVNL TPIKFAPIKE
     HQVQRAMVRR YFQDMEERAI SDVIIVGAGS AGLSCAYALG TARPDLKITI LESNVAPGGG
     CWLGGQLMSA MVCRKPADEF LDQVGVPYED EGNFVVVKHA ALFTSTVLSK VLAMPNVKMF
     NATACEDLII KPCPINPGVQ RIAGCVTNWT LVSLNHDHQS CMDPSTITAP LVCSFAGHDG
     PFGAFCVKRV ASAGLSEGLG DMRPLDMERA EDHIANKTRE ILPGLIVGGM ELSEFDGSAR
     MGPTFGAMLL SGKRAAEVAL QSLDRVKIEE GEVVGLAK
//