ID   A0A8B6NHY2_9PHAE        Unreviewed;       269 AA.
AC   A0A8B6NHY2;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   RecName: Full=Thiazole synthase {ECO:0000256|ARBA:ARBA00011960, ECO:0000256|HAMAP-Rule:MF_00443};
DE            EC=2.8.1.10 {ECO:0000256|ARBA:ARBA00011960, ECO:0000256|HAMAP-Rule:MF_00443};
GN   Name=thiG {ECO:0000256|HAMAP-Rule:MF_00443,
GN   ECO:0000313|EMBL:QNU09455.1};
OS   Sargassum horneri.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:QNU09455.1}.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae; Fucales;
OC   Sargassaceae; Sargassum.
OX   NCBI_TaxID=74089 {ECO:0000313|EMBL:QNU09455.1};
RN   [1] {ECO:0000313|EMBL:QNU09455.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SC {ECO:0000313|EMBL:QNU09455.1};
RA   Byeon S.Y., Cheon K.-S., Kim S., Yun S.-H., Oh H.-J., Park S.R., Kim T.-H.,
RA   Kim J.K., Lee H.J.;
RT   "Comparative Analysis of Sequence Polymorphism in Complete Organelle
RT   Genomes of the 'Golden Tide' Seaweed Sargassum horneri between Korean and
RT   Chinese Forms.";
RL   Sustainability 12:0-0(0).
CC   -!- FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate
CC       (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is
CC       provided by the thiocarboxylate moiety of the carrier protein ThiS. In
CC       vitro, sulfur can be provided by H(2)S. {ECO:0000256|ARBA:ARBA00002834,
CC       ECO:0000256|HAMAP-Rule:MF_00443}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-
CC         carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-
CC         carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-
CC         carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O;
CC         Xref=Rhea:RHEA:26297, Rhea:RHEA-COMP:12908, Rhea:RHEA-COMP:12909,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:62899, ChEBI:CHEBI:77846, ChEBI:CHEBI:90619,
CC         ChEBI:CHEBI:90778; EC=2.8.1.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00000887, ECO:0000256|HAMAP-
CC         Rule:MF_00443};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948, ECO:0000256|HAMAP-Rule:MF_00443}.
CC   -!- SUBUNIT: Homotetramer. Forms heterodimers with either ThiH or ThiS.
CC       {ECO:0000256|HAMAP-Rule:MF_00443}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_00443}.
CC   -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00443}.
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DR   EMBL; MT795189; QNU09455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8B6NHY2; -.
DR   UniPathway; UPA00060; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04728; ThiG; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00443; ThiG; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR033983; Thiazole_synthase_ThiG.
DR   InterPro; IPR008867; ThiG.
DR   PANTHER; PTHR34266; THIAZOLE SYNTHASE; 1.
DR   PANTHER; PTHR34266:SF2; THIAZOLE SYNTHASE; 1.
DR   Pfam; PF05690; ThiG; 1.
DR   SUPFAM; SSF110399; ThiG-like; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000313|EMBL:QNU09455.1};
KW   Plastid {ECO:0000313|EMBL:QNU09455.1};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_00443};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW   Rule:MF_00443};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00443}.
FT   DOMAIN          9..259
FT                   /note="Thiazole synthase ThiG"
FT                   /evidence="ECO:0000259|Pfam:PF05690"
FT   ACT_SITE        107
FT                   /note="Schiff-base intermediate with DXP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT   BINDING         168
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT   BINDING         194..195
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT   BINDING         216..217
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
SQ   SEQUENCE   269 AA;  29288 MW;  8925F8138EDFCB6A CRC64;
     MRKQDPLIIG NKSFNSRLII GTGKYRNLHD MTSCLEKSGA EIVTVAIRRL NLSTVTTNNL
     IAKINWNKLW LLPNTAGAKT TEEAIRLAFL GRELSKRLGQ QENNFIKLEV ISDPKYLFPD
     PIGTLKAAEF LIKKGFSVLP YTNTDPMLAK HLEDIGCSTI MPLGSPIGSG QGIQNIENIK
     IIIENSKVPV IIDAGIGSSS EATYAMELGA EAVLINSAIA QAKNSIEMAT AMNLAVRAGR
     KAYLAGQMIP QKFAQSSSPR KGLDFLKSE
//