ID A0A0T7BV67_9CYAN Unreviewed; 638 AA.
AC A0A0T7BV67;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=IJ00_17985 {ECO:0000313|EMBL:AKG22914.1};
OS Calothrix sp. 336/3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG22914.1, ECO:0000313|Proteomes:UP000065745};
RN [1] {ECO:0000313|EMBL:AKG22914.1, ECO:0000313|Proteomes:UP000065745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=336/3 {ECO:0000313|EMBL:AKG22914.1,
RC ECO:0000313|Proteomes:UP000065745};
RX PubMed=25614574;
RA Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M.,
RA Battchikova N.;
RT "Draft genome sequence of calothrix strain 336/3, a novel h2-producing
RT cyanobacterium isolated from a finnish lake.";
RL Genome Announc. 3:0-0(2015).
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; CP011382; AKG22914.1; -; Genomic_DNA.
DR RefSeq; WP_035155198.1; NZ_CP011382.1.
DR AlphaFoldDB; A0A0T7BV67; -.
DR STRING; 1337936.IJ00_17985; -.
DR KEGG; calh:IJ00_17985; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG2022; Bacteria.
DR OrthoDB; 9805935at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000065745; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000065745};
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..334
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 381..632
FT /note="Thiazole synthase ThiG"
FT /evidence="ECO:0000259|Pfam:PF05690"
FT ACT_SITE 480
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 541
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 567..568
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
FT BINDING 589..590
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00443"
SQ SEQUENCE 638 AA; 68515 MW; 918BB5182D5CC75F CRC64;
MTRDCLIIGG GIIGLAIAVE LQSRGMKVRV ISRDSHSAAA YAAAGMLAPD AENITTGAMQ
ELCWRSRALY PEWTGKLERM TGLSPGYWAC GILAPVFNAP AHPNSAHWLD QATIHQYQLG
LGESVIGGYW YPEDAQVDNR ALVKVLLAAA YHLGVEIQEG VEVLGIMQQG GQVSGVQTDT
EIIRANHYIL AAGAWVNQVF PLPVRPRKGQ MLSLRVPDSE TELLPLTRVL FGEDIYIVPR
RDRRIIIGAT VEDVGFIPDN TPAGLNQLLQ GAIRLYPRLK DYPITETWWG FRPTTTDELP
ILGTSPCENL TLATGHHRNG ILLAPITAQL IADLICQQQT DSLLNHFHYS RFHSPMLSFP
SPVTTAPSPV NSSPIADTPL TIAGKTFKSR LMTGTGKYRS IQEMQQSVIA SGCEIVTVAV
RRVQTHAPGH EGLAEALDWS KIWMLPNTAG CKTAEEAVRV ARLGREMAKL LGQEDNNFIK
LEVIPDAKYL LPDPIGTLQA AEQLVKEGFA VLPYINADPI LAKHLEAAGC ATVMPLAAPI
GSGQGLKTAA NIQIIIENAQ VPVVVDAGIG SPSEAAQAME MGADALLINS AIALAENAPA
MAYAMNLAAI AGRTGYLAGR MPTKDYASAS SPVTGTIN
//
