GenomeNet

Database: UniProt
Entry: A0A061F760_THECC
LinkDB: A0A061F760_THECC
Original site: A0A061F760_THECC 
ID   A0A061F760_THECC        Unreviewed;       358 AA.
AC   A0A061F760;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   03-JUL-2019, entry version 29.
DE   RecName: Full=Thiamine thiazole synthase, chloroplastic {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   Name=THI1 {ECO:0000256|HAMAP-Rule:MF_03158};
GN   ORFNames=TCM_031067 {ECO:0000313|EMBL:EOY12547.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Malvales; Malvaceae; Byttnerioideae;
OC   Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY12547.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY12547.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23731509;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C.,
RA   Feltus F.A., Mustiga G.M., Amores F., Phillips W., Marelli J.P.,
RA   May G.D., Shapiro H., Ma J., Bustamante C.D., Schnell R.J., Main D.,
RA   Gilbert D., Parida L., Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its
RT   use to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53-R53(2013).
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: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_03158}.
CC   -!- PTM: During the catalytic reaction, a sulfide is transferred from
CC       Cys-225 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CM001885; EOY12547.1; -; Genomic_DNA.
DR   RefSeq; XP_007021022.1; XM_007020960.2.
DR   STRING; 3641.EOY12547; -.
DR   EnsemblPlants; EOY12547; EOY12547; TCM_031067.
DR   GeneID; 18593644; -.
DR   Gramene; EOY12547; EOY12547; TCM_031067.
DR   KEGG; tcc:18593644; -.
DR   KO; K03146; -.
DR   OMA; YDLNNFR; -.
DR   OrthoDB; 1111148at2759; -.
DR   Proteomes; UP000026915; Chromosome 7.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-UniRule.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
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   Chloroplast {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Complete proteome {ECO:0000313|Proteomes:UP000026915};
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   Plastid {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   REGION      123    124       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      304    306       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     103    103       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     131    131       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     196    196       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     227    227       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     242    242       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     294    294       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   MOD_RES     225    225       2,3-didehydroalanine (Cys).
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   358 AA;  37979 MW;  819287385C71502A CRC64;
     MASSVATTLT SSTKLYRNTS LFESSFHGVP ITPLSFHLKA KSSPRNASVS MSAASSPPPY
     DLNNFRFDPI KESIVSREMT RRYMMDMITH ADTDVVVVGA GSAGLSCAYE LSKNPSVQVA
     IVEQSVSPGG GAWLGGQLFS AMVVRKPAHR FLDELGIEYD EQDDYVVIKH AALFTSTIMS
     KLLARPNVKL FNAVAAEDLI VKGGRVGGVV TNWALVSMNH DTQSCMDPNV MEAKVVVSSC
     GHDGPFGATG VKRLKSIGMI DSVPGMKALD MNTAEDAIVR LTREIVPGMI VTGMEVAEID
     GSPRMGPTFG AMMISGQKAA HLALQSLGLP NALDGTYVGN IHPELILAAA DSAETADA
//
DBGET integrated database retrieval system