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Database: UniProt
Entry: A0A0Q4KVB4_9SPHN
LinkDB: A0A0Q4KVB4_9SPHN
Original site: A0A0Q4KVB4_9SPHN 
ID   A0A0Q4KVB4_9SPHN        Unreviewed;       332 AA.
AC   A0A0Q4KVB4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-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=ASE86_10980 {ECO:0000313|EMBL:KQN26595.1};
OS   Sphingomonas sp. Leaf33.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736215 {ECO:0000313|EMBL:KQN26595.1, ECO:0000313|Proteomes:UP000051455};
RN   [1] {ECO:0000313|EMBL:KQN26595.1, ECO:0000313|Proteomes:UP000051455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf33 {ECO:0000313|EMBL:KQN26595.1,
RC   ECO:0000313|Proteomes:UP000051455};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN26595.1, ECO:0000313|Proteomes:UP000051455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf33 {ECO:0000313|EMBL:KQN26595.1,
RC   ECO:0000313|Proteomes:UP000051455};
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:KQN26595.1}.
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DR   EMBL; LMLB01000001; KQN26595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4KVB4; -.
DR   STRING; 1736215.ASE86_10980; -.
DR   OrthoDB; 9805935at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000051455; 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:UP000051455};
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          83..327
FT                   /note="Thiazole synthase ThiG"
FT                   /evidence="ECO:0000259|Pfam:PF05690"
FT   ACT_SITE        175
FT                   /note="Schiff-base intermediate with DXP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT   BINDING         236
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT   BINDING         262..263
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT   BINDING         284..285
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
SQ   SEQUENCE   332 AA;  34875 MW;  2F73782315BA3BDD CRC64;
     MAHSDGTVSI TLNGEHKRVA AGLTIAALAE SLGLVPAKLA VERNLEVVPR STLHEVMVED
     GDELEIVHFV GGGDHVADDS WSVASRTFRS RLIVGTGKYK DFEQNAAAVA ASGAEIVTVA
     VRRVNVSDPG APMLTDYIDP KTITYLPNTA GCFDADSAIR TLRLAREAGG WDLVKLEVLG
     EARTLYPDMV ETLRATEVLA KEGFKPMVYC VDDPIAAKRL EDVGAVAIMP LGAPIGSGLG
     IQNQVTIRLI VEGAKVPVLV DAGVGTASDA AAAMELGCDG VLMNTAIAEA RDPILMAAAM
     KSAVESGRLA YRAGRMAKRR YADPSSPLAG LI
//
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