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Database: UniProt
Entry: E3RJW6_PYRTT
LinkDB: E3RJW6_PYRTT
Original site: E3RJW6_PYRTT 
ID   E3RJW6_PYRTT            Unreviewed;       329 AA.
AC   E3RJW6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   03-JUL-2019, entry version 46.
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=PTT_08482 {ECO:0000313|EMBL:EFQ93956.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ93956.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ93956.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F.,
RA   Moffat C.S., Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora
RT   teres f. teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
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-217 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; GL533563; EFQ93956.1; -; Genomic_DNA.
DR   RefSeq; XP_003297921.1; XM_003297873.1.
DR   STRING; 53485.EFQ93956; -.
DR   EnsemblFungi; EFQ93956; EFQ93956; PTT_08482.
DR   KEGG; pte:PTT_08482; -.
DR   eggNOG; KOG2960; Eukaryota.
DR   eggNOG; COG1635; LUCA.
DR   KO; K03146; -.
DR   OrthoDB; 1111148at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000001067};
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:UP000001067};
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      296    298       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     219    219       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     234    234       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     286    286       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   MOD_RES     217    217       2,3-didehydroalanine (Cys).
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   329 AA;  35244 MW;  BDF9E7F219DD2FB1 CRC64;
     MSPPAAIYEV PVAAANDMGI KKDLAVKAAA NSQAKTVAEL ENNWETFTFA PIRESQVSRA
     MTRRYFNDLD TYAESDVVIV GAGSCGLSAA FTLATKRPDL KIAIVEAGVA PGGGAWLGGQ
     LFSAMVMRKP AELFLNEIGV PYEDEDDFVV VKHAALFTST LLSKVLQFPN VKLFNATAVE
     DLITRPAPTS SDPNAIRIAG VVTNWTLVSM HHDDQSCMDP NTINAPLVIS TTGHDGPFGA
     FCVKRLVSMQ QIEKLGGMRG LDMRTAEDAI VKRTREVVPG LIVGGMELSE VDGANRMGPT
     FGAMALSGVK AAEEAVNVWE ERKAQNLES
//
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