ID A0A0M5KZ42_9SPHN Unreviewed; 331 AA.
AC A0A0M5KZ42;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AMC99_02508 {ECO:0000313|EMBL:ALE17781.1};
OS Altererythrobacter epoxidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=361183 {ECO:0000313|EMBL:ALE17781.1, ECO:0000313|Proteomes:UP000057938};
RN [1] {ECO:0000313|EMBL:ALE17781.1, ECO:0000313|Proteomes:UP000057938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7731 {ECO:0000313|EMBL:ALE17781.1,
RC ECO:0000313|Proteomes:UP000057938};
RA Li Z., Cheng H., Huo Y., Xu X.;
RT "Complete genome sequence of a benzo[a]pyrene-degrading bacterium
RT Altererythrobacter epoxidivorans CGMCC 1.7731T.";
RL Submitted (SEP-2015) 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; CP012669; ALE17781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M5KZ42; -.
DR STRING; 361183.AMC99_02508; -.
DR KEGG; aep:AMC99_02508; -.
DR PATRIC; fig|361183.4.peg.2463; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000057938; Chromosome.
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:UP000057938};
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 82..326
FT /note="Thiazole synthase ThiG"
FT /evidence="ECO:0000259|Pfam:PF05690"
FT ACT_SITE 174
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 235
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 261..262
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 283..284
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
SQ SEQUENCE 331 AA; 34957 MW; F242E90FA44A8694 CRC64;
MCGAMSAHKQ ITVNGETRRS TASTIAELVR ELDLVPEKVA VERNGEIAPR SQLAEIALCD
GDTLEIVHFV GGGSANADSW TVAGRTFTSR LIVGTGKYKD FEQNAAAVEA SGAEIVTVAV
RRVNVSDPKA PMLTDYIDPK KITYLPNTAG CFTADDAIRT LRLAREAGGW DLVKLEVLGE
ARTLYPDMRE TLKATETLAK EGFLPMVYCV DDPIAAKQLE EAGAVAVMPL GAPIGSGLGI
QNQVTIRLIV EGANVPVLVD AGVGTASDAA VGMELGCDGI LMNTAIAEAK DPIRMARAMK
LAVEAGREAY LAGRMGRRKY ADPSSPLAGL I
//
