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Database: UniProt
Entry: THI42_MAIZE
LinkDB: THI42_MAIZE
Original site: THI42_MAIZE 
ID   THI42_MAIZE             Reviewed;         354 AA.
AC   Q41739;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-JUL-2019, entry version 107.
DE   RecName: Full=Thiamine thiazole synthase 2, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03158};
DE            EC=2.4.2.60 {ECO:0000255|HAMAP-Rule:MF_03158};
DE   AltName: Full=Thiazole biosynthetic enzyme 2 {ECO:0000255|HAMAP-Rule:MF_03158};
DE   Flags: Precursor;
GN   Name=THI1-2 {ECO:0000255|HAMAP-Rule:MF_03158};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
OC   Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Seedling;
RX   PubMed=8541506; DOI=10.1007/BF00041170;
RA   Belanger F.C., Leustek T., Chu B., Kriz A.L.;
RT   "Evidence for the thiamine biosynthetic pathway in higher-plant
RT   plastids and its developmental regulation.";
RL   Plant Mol. Biol. 29:809-821(1995).
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:8541506}.
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:0000255|HAMAP-Rule:MF_03158};
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: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_03158, ECO:0000269|PubMed:8541506}.
CC   -!- TISSUE SPECIFICITY: Highest expression in developing embryos and
CC       green leaves and a very low level expression seen in endosperm,
CC       roots, etiolated shoots and immature ears.
CC   -!- DEVELOPMENTAL STAGE: During embryo development, expression
CC       increases from 15-21 days after pollination and decreases slightly
CC       at day 24 and this level is maintained until day 36.
CC   -!- PTM: During the catalytic reaction, a sulfide is transferred from
CC       Cys-219 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}.
DR   EMBL; U17351; AAA96739.1; -; mRNA.
DR   PIR; S61420; S61420.
DR   SMR; Q41739; -.
DR   STRING; 4577.GRMZM2G074097_P01; -.
DR   PaxDb; Q41739; -.
DR   PRIDE; Q41739; -.
DR   MaizeGDB; 128724; -.
DR   eggNOG; KOG2960; Eukaryota.
DR   eggNOG; COG1635; LUCA.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q41739; baseline and differential.
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   2: Evidence at transcript level;
KW   Chloroplast; Complete proteome; Iron; Metal-binding; NAD; Plastid;
KW   Reference proteome; Thiamine biosynthesis; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     44       Chloroplast. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   CHAIN        45    354       Thiamine thiazole synthase 2,
FT                                chloroplastic.
FT                                /FTId=PRO_0000034063.
FT   REGION      117    118       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      298    300       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING      97     97       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   BINDING     125    125       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   BINDING     190    190       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     221    221       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     236    236       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     288    288       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   MOD_RES     219    219       2,3-didehydroalanine (Cys).
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   354 AA;  37234 MW;  452E905B46B6AF13 CRC64;
     MATTAASSLL KSSFAGSRLP SATRTTTPSS VAVATPRAGG GPIRASISSP NPPYDLTSFR
     FSPIKESIVS REMTRRYMTD MITHADTDVV IVGAGSAGLS CAYELSKDPT VSVAIVEQSV
     SPGGGAWLGG QLFSAMVVRR PAHLFLDELG VGYDEAEDYV VVKHAALFTS TVMSRLLARP
     NVKLFNAVAV EDLIVRRGRV GGVVTNWALV SMNHDTQSCM DPNVMEAKVV VSSCGHDGPF
     GATGVKRLQD IGMISAVPGM KALDMNAAED EIVRLTREVV PGMIVTGMEV AEIDGAPRMG
     PTFGAMMISG QKAAHLALKA LGRPNAVDGT IPEVSPALRE EFVIASKDDE VVDA
//
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