ID A0A0T0PVN7_9SPHN Unreviewed; 337 AA.
AC A0A0T0PVN7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=ASG29_11355 {ECO:0000313|EMBL:KQT32959.1};
OS Sphingomonas sp. Leaf412.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT32959.1, ECO:0000313|Proteomes:UP000051178};
RN [1] {ECO:0000313|EMBL:KQT32959.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32959.1,
RC ECO:0000313|Proteomes:UP000051178};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT32959.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32959.1,
RC ECO:0000313|Proteomes:UP000051178};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQT32959.1}.
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DR EMBL; LMQP01000003; KQT32959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T0PVN7; -.
DR STRING; 1736370.ASG29_11355; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000051178; 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:UP000051178};
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 88..332
FT /note="Thiazole synthase ThiG"
FT /evidence="ECO:0000259|Pfam:PF05690"
FT ACT_SITE 180
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 241
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 267..268
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 289..290
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
SQ SEQUENCE 337 AA; 35275 MW; B6FA2C761273982F CRC64;
MSITVNGEHK RVTAGLTIAA LAESLGLVPE KLAVERNLEV VPRSTLGSVM VEDGDELEIV
HFVGGGDHPV AGGGGDHAAA VDADTWTVAG RTFRSRLIVG TGKYRDFAQN AAAVAASGAE
IVTVAVRRVN VSDPNAPMLT DYIDPKKVTY LPNTAGCFTA DDAIRTLRLA REAGGWDLVK
LEVLGEARTL YPNMRETLTA TEVLVREGFK PMVYCVDDPI AAKQLEEAGA VAIMPLGAPI
GSGLGIQNQV TIRLIVEGAK VPVLVDAGVG QASDAAVAME LGCDGVLMNT AIAEARDPIL
MAAAMRAAVE AGRMSYRAGR MGKRRYADPS SPLSGLI
//
