THI4_CITSI
ID THI4_CITSI Reviewed; 356 AA.
AC O23787;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Thiamine thiazole synthase, 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 {ECO:0000255|HAMAP-Rule:MF_03158};
DE Flags: Precursor;
GN Name=THI1 {ECO:0000255|HAMAP-Rule:MF_03158};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Peelings;
RX PubMed=9349287; DOI=10.1023/a:1005833724582;
RA Jacob-Wilk D., Goldschmidt E.E., Riov J., Sadka A., Holland D.;
RT "Induction of a Citrus gene highly homologous to plant and yeast thi genes
RT involved in thiamine biosynthesis during natural and ethylene-induced fruit
RT maturation.";
RL Plant Mol. Biol. 35:661-666(1997).
CC -!- FUNCTION: Involved in biosynthesis of the thiamine precursor thiazole.
CC Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-
CC (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an
CC adenylated thiazole intermediate. The reaction includes an iron-
CC dependent sulfide transfer from a conserved cysteine residue of the
CC protein to a thiazole intermediate. The enzyme can only undergo a
CC single turnover, which suggests it is a suicide enzyme. May have
CC additional roles in adaptation to various stress conditions and in DNA
CC damage tolerance. {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) = [ADP-
CC thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-methylthiazole-2-
CC carboxylate + 2 H(+) + 3 H2O + nicotinamide; Xref=Rhea:RHEA:55708,
CC Rhea:RHEA-COMP:14264, Rhea:RHEA-COMP:14265, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57540, ChEBI:CHEBI:90873,
CC ChEBI:CHEBI:139151; EC=2.4.2.60; Evidence={ECO:0000255|HAMAP-
CC 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-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 -!- DEVELOPMENTAL STAGE: Levels increase in fruit peel during fruit
CC maturation. {ECO:0000269|PubMed:9349287}.
CC -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC 223 to a reaction intermediate, generating a dehydroalanine residue.
CC {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC Rule:MF_03158}.
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DR EMBL; Z82983; CAB05370.1; -; mRNA.
DR PIR; T10474; T10474.
DR RefSeq; NP_001275783.1; NM_001288854.1.
DR AlphaFoldDB; O23787; -.
DR SMR; O23787; -.
DR STRING; 2711.XP_006475203.1; -.
DR GeneID; 102626594; -.
DR KEGG; cit:102626594; -.
DR eggNOG; KOG2960; Eukaryota.
DR OrthoDB; 1111148at2759; -.
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:pentosyltransferase activity; 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; Iron; Metal-binding; NAD; Plastid; Thiamine biosynthesis;
KW Transferase; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT CHAIN 52..356
FT /note="Thiamine thiazole synthase, chloroplastic"
FT /id="PRO_0000034061"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 121..122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 302..304
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT MOD_RES 223
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
SQ SEQUENCE 356 AA; 37595 MW; BC53C1CD94D61866 CRC64;
MAAMASTAFA PSVSSTTNKL FDSSFHGAPM SPSLLRLQPI KSSRPNNLSI SASASPPYDL
NTFKFDPIKE SIVSREMTRR YMTDMITYAD TDVVVVGAGS AGLSCAYELS KNPNIQIAII
EQSVSPGGGA WLGGQLFSAM VVRKPAHIFL DELGIDYDEQ DNYVVIKHAA LFTSTIMSKL
LARPNVKLFN AVAAEDLIVK GGRVGGVVTN WALVSMNHDT QSCMDPNVME AKVVVSSCGH
DGPFGATGVK RLKSIGMIEE VPGMKALDMN SAEDAIVRLT REVVPGMIVT GMEVAEIDGA
PRMGPTFGAM MISGQKAAHL ALKSLGQPNA LDGTYVGGVH PELILAAADS AETADA
