ID A0A0C2PRL2_9CYAN Unreviewed; 681 AA.
AC A0A0C2PRL2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=SD81_33010 {ECO:0000313|EMBL:KIJ74154.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ74154.1};
RN [1] {ECO:0000313|EMBL:KIJ74154.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ74154.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-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:KIJ74154.1}.
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DR EMBL; JXCB01000012; KIJ74154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2PRL2; -.
DR OrthoDB; 9805935at2; -.
DR UniPathway; UPA00060; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR HAMAP; MF_00443; ThiG; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012727; Gly_oxidase_ThiO.
DR InterPro; IPR033983; Thiazole_synthase_ThiG.
DR InterPro; IPR008867; ThiG.
DR NCBIfam; TIGR02352; thiamin_ThiO; 1.
DR PANTHER; PTHR34266; THIAZOLE SYNTHASE; 1.
DR PANTHER; PTHR34266:SF2; THIAZOLE SYNTHASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF05690; ThiG; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF110399; ThiG-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00443};
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 4..367
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 423..674
FT /note="Thiazole synthase ThiG"
FT /evidence="ECO:0000259|Pfam:PF05690"
FT REGION 99..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 522
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 583
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 609..610
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 631..632
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
SQ SEQUENCE 681 AA; 73868 MW; 3514DDAF63BCC618 CRC64;
MTSDVLIIGG GVISLAIAIE LKLRGAKVTV VSREFRAAAT HAAAGMLAPT AERIPDQAMQ
ELCTRSLYLY PDWTRKLEEF TSINTGYWSC GILTPVYQET RGQENTEKEE GERERGREGG
KLLSLPVSLT PPLSPSSCPA YWLEKEVIHQ YQPGLGEEVV GGWWYPEDAQ VDNRALAQAL
LATAQSLGVE LKEGIVVEGI QQQQRQVVGV QTSAGVLSAQ HYVLAAGAWS NALFPLPVRP
VKGQMLSVRV PEFVPDLPLT RVLFREDIYI VPRRDRRIII GATVEDVGFT PHNTPAGIQT
LLQRAIRLFP QIQDYPIEEL WWGFRPATPD ESPILGTSPC ENLTLATGHY RNGILLAPVT
AALLADLILE QNSDPLLSHF HYSRFHTKPS TTSMLTYPTL KTQKPELAAR NSELSTLEDS
PLQIAGKTFQ SRLMTGTGKY RSIEEMQQSV VKSGCQIVTV AVRRVQNNAP GHEGLAEALD
WTKIWMLPNT AGCQTAEEAI RVARLGREMA KLLGQEDNNF VKLEVIPDLK YLLPDPIGTL
QAAEQLVKEG FAVLPYINAD PMLAKRLEEV GCATVMPLAA PIGSGQGLKT TANIQIIIEN
ANVPVVVDAG IGAPSEAAQA MEMGADALLI NSAIALAQNA PAMAHAMNLA TVAGRLAYLA
GRMPIKTHAI ASSPLTGTIT G
//
