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Database: UniProt
Entry: THI42_VITVI
LinkDB: THI42_VITVI
Original site: THI42_VITVI 
ID   THI42_VITVI             Reviewed;         355 AA.
AC   F6H7K5;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-JUL-2019, entry version 50.
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};
GN   OrderedLocusNames=VIT_10s0116g00530;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024;
RX   PubMed=17721507; DOI=10.1038/nature06148;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C.,
RA   Casagrande A., Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A.,
RA   Legeai F., Hugueney P., Dasilva C., Horner D., Mica E., Jublot D.,
RA   Poulain J., Bruyere C., Billault A., Segurens B., Gouyvenoux M.,
RA   Ugarte E., Cattonaro F., Anthouard V., Vico V., Del Fabbro C.,
RA   Alaux M., Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I.,
RA   Moroldo M., Scalabrin S., Canaguier A., Le Clainche I., Malacrida G.,
RA   Durand E., Pesole G., Laucou V., Chatelet P., Merdinoglu D.,
RA   Delledonne M., Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F.,
RA   Pe M.E., Valle G., Morgante M., Caboche M., Adam-Blondon A.-F.,
RA   Weissenbach J., Quetier F., Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in
RT   major angiosperm phyla.";
RL   Nature 449:463-467(2007).
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}.
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}.
CC   -!- PTM: During the catalytic reaction, a sulfide is transferred from
CC       Cys-220 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; FN595248; CCB48166.1; -; Genomic_DNA.
DR   RefSeq; XP_002267414.1; XM_002267378.4.
DR   SMR; F6H7K5; -.
DR   STRING; 29760.VIT_10s0116g00530.t01; -.
DR   PRIDE; F6H7K5; -.
DR   EnsemblPlants; VIT_10s0116g00530.t01; VIT_10s0116g00530.t01; VIT_10s0116g00530.
DR   GeneID; 100265774; -.
DR   Gramene; VIT_10s0116g00530.t01; VIT_10s0116g00530.t01; VIT_10s0116g00530.
DR   KEGG; vvi:100265774; -.
DR   eggNOG; KOG2960; Eukaryota.
DR   eggNOG; COG1635; LUCA.
DR   InParanoid; F6H7K5; -.
DR   KO; K03146; -.
DR   OrthoDB; 1111148at2759; -.
DR   Proteomes; UP000009183; Chromosome 10.
DR   ExpressionAtlas; F6H7K5; 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   3: Inferred from homology;
KW   Chloroplast; Complete proteome; Iron; Metal-binding; NAD; Plastid;
KW   Reference proteome; Thiamine biosynthesis; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     72       Chloroplast. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   CHAIN        73    355       Thiamine thiazole synthase 2,
FT                                chloroplastic.
FT                                /FTId=PRO_0000415868.
FT   REGION      118    119       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      299    301       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING      98     98       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   BINDING     126    126       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   BINDING     191    191       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     222    222       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     237    237       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     289    289       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
FT   MOD_RES     220    220       2,3-didehydroalanine (Cys).
FT                                {ECO:0000255|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   355 AA;  38105 MW;  E6A798A618EFAB4E CRC64;
     MASMATTLTS LSSNPKPAFF DNKSSFHGSP ISYRVLPIKV SHQSPTISMS SVSPYDLQSF
     KFEPIKESIV AREMTRRYMM DMITYADTDV VIVGAGSAGL SCAYELSKNP SIRVAIIEQS
     VSPGGGAWLG GQLFSAMVVR KPAHHFLDEL GIEYDEQDNY VVIKHAALFT STIMSKLLAR
     PNVKLFNAVA AEDLIVKEER VAGVVTNWAL VSMNHDTQSC MDPNVMEAKV VVSSCGHDGP
     FGATGVKRLK SIGMIDSVPG MKALDMNTAE DAIVRLTREI VPGMIVTGME VAEIDGAPRM
     GPTFGAMMIS GQKAAHLALR ALGQPNAIDG NYTEAETMQP ELILAAAETG EIVDA
//
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