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Database: UniProt
Entry: A0A194W7Q3_9PEZI
LinkDB: A0A194W7Q3_9PEZI
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ID   A0A194W7Q3_9PEZI        Unreviewed;       326 AA.
AC   A0A194W7Q3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   03-JUL-2019, entry version 10.
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=VM1G_07962 {ECO:0000313|EMBL:KUI72113.1};
OS   Valsa mali.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI72113.1, ECO:0000313|Proteomes:UP000078559};
RN   [1] {ECO:0000313|EMBL:KUI72113.1, ECO:0000313|Proteomes:UP000078559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-8 {ECO:0000313|EMBL:KUI72113.1,
RC   ECO:0000313|Proteomes:UP000078559};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific
RT   Adaption of Colonization on Woody Bark.";
RL   Submitted (DEC-2014) 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; CM003105; KUI72113.1; -; Genomic_DNA.
DR   EnsemblFungi; KUI72113; KUI72113; VM1G_07962.
DR   OrthoDB; 1111148at2759; -.
DR   Proteomes; UP000078559; Chromosome 8.
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:transferase activity, transferring pentosyl groups; 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   Complete proteome {ECO:0000313|Proteomes:UP000078559};
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   Reference proteome {ECO:0000313|Proteomes:UP000078559};
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;  34776 MW;  0B252ADD8A5D75AA CRC64;
     MAPSAVSPVL ASAEADLGHL AIKGMNKANI QASTQAVEAM MGQWDTFSFA PIRESQVSRA
     MTSRYFKDLD TYAESDIVII GAGSCGLSAA YMLGKARPDL KIAIIEAGVA PGGGAWLGGQ
     LFSAMVMRKP ADAFLTELGV PFEDEGDYVV VKHAALFTST VLSKVLQFPN VKLFNATTVE
     DLITRRTPDG EHDLRIAGVV TNWTLVSMHH DDQSCMDPNT INAPVLISTT GHDGPFGAFS
     VKRLVSMKQL EQLGGMRGLD MQTAEDAIVK GTREIIPGLI VGGMELSEVD GANRMGPTFG
     AMALSGVKAA EEALRVFEQR KAENLK
//
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