ID A0A285R4Q1_9SPHN Unreviewed; 335 AA.
AC A0A285R4Q1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ORFNames=SAMN06297144_2467 {ECO:0000313|EMBL:SOB87337.1};
OS Sphingomonas guangdongensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1141890 {ECO:0000313|EMBL:SOB87337.1, ECO:0000313|Proteomes:UP000219494};
RN [1] {ECO:0000313|EMBL:SOB87337.1, ECO:0000313|Proteomes:UP000219494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12672 {ECO:0000313|EMBL:SOB87337.1,
RC ECO:0000313|Proteomes:UP000219494};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443}.
CC -!- SIMILARITY: Belongs to the ThiG family. {ECO:0000256|HAMAP-
CC Rule:MF_00443}.
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DR EMBL; OBMI01000003; SOB87337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285R4Q1; -.
DR OrthoDB; 9805935at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000219494; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990107; F:thiazole synthase activity; IEA:RHEA.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04728; ThiG; 1.
DR CDD; cd00565; Ubl_ThiS; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00443; ThiG; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR010035; Thi_S.
DR InterPro; IPR033983; Thiazole_synthase_ThiG.
DR InterPro; IPR008867; ThiG.
DR InterPro; IPR003749; ThiS/MoaD-like.
DR NCBIfam; TIGR01683; thiS; 1.
DR PANTHER; PTHR34266; THIAZOLE SYNTHASE; 1.
DR PANTHER; PTHR34266:SF2; THIAZOLE SYNTHASE; 1.
DR Pfam; PF05690; ThiG; 1.
DR Pfam; PF02597; ThiS; 1.
DR SUPFAM; SSF54285; MoaD/ThiS; 1.
DR SUPFAM; SSF110399; ThiG-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443};
KW Reference proteome {ECO:0000313|Proteomes:UP000219494};
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 86..330
FT /note="Thiazole synthase ThiG"
FT /evidence="ECO:0000259|Pfam:PF05690"
FT ACT_SITE 178
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 239
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 265..266
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 287..288
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
SQ SEQUENCE 335 AA; 35247 MW; AFA6AA2757E6CE4E CRC64;
MAHTDGTVSI TVNGEHKRVP AGTTLTQLAE SLGLVPAKLA IERNLEVVPR STHDQVTVED
GDDLEIVHFV GGGDHGASVD QDSWTVAGRT FRSRLIVGTG KYKDFAQNAA ALEASGAEIV
TVAVRRVNVS DPSAPRLTDF IDPAKVTYLP NTAGCFDAES AVRTLRLARE AGGWDLVKLE
VLGEARTLYP DMRETLKATE VLVREGFKPM VYCVDDPIAA KQLEEAGAVA IMPLGAPIGS
GLGIQNRVTI RLIVEGAKVP VLVDAGVGTA SDAAVAMELG CDGVLMNTAI AEAKDSVMMA
AAMKASVEAG RLAYRAGRMG QRRYADPSSP LAGLI
//
