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Database: UniProt
Entry: R8BRG8_TOGMI
LinkDB: R8BRG8_TOGMI
Original site: R8BRG8_TOGMI 
ID   R8BRG8_TOGMI            Unreviewed;       326 AA.
AC   R8BRG8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   03-JUL-2019, entry version 31.
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=UCRPA7_2510 {ECO:0000313|EMBL:EOO01967.1};
OS   Togninia minima (strain UCR-PA7) (Esca disease fungus)
OS   (Phaeoacremonium aleophilum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Togniniales; Togniniaceae;
OC   Phaeoacremonium.
OX   NCBI_TaxID=1286976 {ECO:0000313|EMBL:EOO01967.1};
RN   [1] {ECO:0000313|EMBL:EOO01967.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCRPA7 {ECO:0000313|EMBL:EOO01967.1};
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Genome sequence of Togninia minima (Phoeoacremonium aleophilum)
RT   isolate UCRPA7, causal agent of esca and grapevine decline.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_03158}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) =
CC         [ADP-thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-
CC         methylthiazole-2-carboxylate + 2 H(+) + 3 H2O + nicotinamide;
CC         Xref=Rhea:RHEA:55708, Rhea:RHEA-COMP:14264, Rhea:RHEA-
CC         COMP:14265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:90873, ChEBI:CHEBI:139151;
CC         EC=2.4.2.60; Evidence={ECO:0000256|HAMAP-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-
CC       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
CC       Cys-215 to a reaction intermediate, generating a dehydroalanine
CC       residue. {ECO:0000256|HAMAP-Rule:MF_03158}.
CC   -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03158}.
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DR   EMBL; KB932935; EOO01967.1; -; Genomic_DNA.
DR   RefSeq; XP_007913237.1; XM_007915046.1.
DR   STRING; 223192.XP_007913237.1; -.
DR   EnsemblFungi; EOO01967; EOO01967; UCRPA7_2510.
DR   GeneID; 19322767; -.
DR   KEGG; tmn:UCRPA7_2510; -.
DR   KO; K03146; -.
DR   OrthoDB; 1111148at2759; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:EnsemblFungi.
DR   GO; GO:0016763; F:transferase activity, transferring pentosyl groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
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 {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03158};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   REGION      106    107       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      294    296       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING      85     85       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     114    114       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     179    179       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     217    217       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     232    232       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     284    284       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   MOD_RES     215    215       2,3-didehydroalanine (Cys).
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   326 AA;  34587 MW;  ECC6B95B117AD5A4 CRC64;
     MAPSATSVEP SSAQVAVLTA KKANGAETKA NGQTKTIESM MGKWDTFTFN PIRESQVSRA
     MTRRYFSDLD TYAESDIVII GAGSCGLSAA YTLGKARPDL KIAIIEAGVS PGGGAWLGGQ
     LFSAMVMRKP AEVFLDDIGV PYEDEGNFVV VKHAALFTST VLSKVLQFPN IKLFNATAVE
     DLITRPSAGE EDGVRIAGVV TNWTLVSMHH DDQSCMDPNT INAPLVISTT GHDGPFGAFS
     VKRLVSMKQL EQLGGMRGLD MASAEDAIVK GTREIVPGLI VGGMELSEVD GANRMGPTFG
     AMALSGVKAA EEALKVFDLR KAENEH
//
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