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Database: UniProt
Entry: A0A078INE1_BRANA
LinkDB: A0A078INE1_BRANA
Original site: A0A078INE1_BRANA 
ID   A0A078INE1_BRANA        Unreviewed;       352 AA.
AC   A0A078INE1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   03-JUL-2019, entry version 22.
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=BnaC03g71780D {ECO:0000313|EMBL:CDY52570.1};
GN   Synonyms=THI1 {ECO:0000256|HAMAP-Rule:MF_03158};
GN   ORFNames=GSBRNA2T00007278001 {ECO:0000313|EMBL:CDY52570.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae;
OC   Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY52570.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY52570.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X.,
RA   Chiquet J., Belcram H., Tong C., Samans B., Correa M., Da Silva C.,
RA   Just J., Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P.,
RA   Noel B., Labadie K., Alberti A., Charles M., Arnaud D., Guo H.,
RA   Daviaud C., Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H.,
RA   Tack D., Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G.,
RA   Renault V., Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H.,
RA   Chalabi S., Hu Q., Fan C., Tollenaere R., Lu Y., Battail C., Shen J.,
RA   Sidebottom C.H., Wang X., Canaguier A., Chauveau A., Berard A.,
RA   Deniot G., Guan M., Liu Z., Sun F., Lim Y.P., Lyons E., Town C.D.,
RA   Bancroft I., Wang X., Meng J., Ma J., Pires J.C., King G.J.,
RA   Brunel D., Delourme R., Renard M., Aury J.M., Adams K.L., Batley J.,
RA   Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W., Sharpe A.G.,
RA   Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
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-218 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; LK033104; CDY52570.1; -; Genomic_DNA.
DR   EnsemblPlants; CDY52570; CDY52570; GSBRNA2T00007278001.
DR   Gramene; CDY52570; CDY52570; GSBRNA2T00007278001.
DR   OMA; GIVMNWT; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
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:UP000028999};
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:UP000028999};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   REGION      116    117       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      298    300       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING      96     96       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     124    124       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     189    189       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     220    220       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     236    236       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     288    288       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   MOD_RES     218    218       2,3-didehydroalanine (Cys).
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   352 AA;  37079 MW;  488C070CB32B28AF CRC64;
     MAAVTSTLSL SSTKPQRLFD SSFHGSSISA SPVSVGLKPR SFSTVSVRAT AGYDLNAFTF
     APIKESIVSR EMTRRYMTDM ITYAETDVVV VGAGSAGLSC AYEISKNPNV QVAIIEQSVS
     PGGGAWLGGQ LFSAMIVRKP AHLFLDEIGV PYDEQDNYVV IKHAALFTST IMSKLLARPN
     VKLFNAVAAE DLIVKGNRVG GVVTNWALVS MNHDTQSCMD PNVMEAKIIV VSSCGHDGPF
     GATGVKRLKS IGLIDHVPGM KALDMNTAED AIVRLTREVV PGMIVTGMEV AEIDGAPRMG
     PTFGAMMISG QKAGHLALKA LGQPNALDGT YVGDLSPELV LAAADSAETV DA
//
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