THIE_SYNS3
ID THIE_SYNS3 Reviewed; 353 AA.
AC Q0IC17;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Thiamine-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01327};
DE Short=TP synthase {ECO:0000255|HAMAP-Rule:MF_01327};
DE Short=TPS {ECO:0000255|HAMAP-Rule:MF_01327};
DE EC=2.5.1.3 {ECO:0000255|HAMAP-Rule:MF_01327};
DE AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01327};
DE Short=TMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01327};
DE Short=TMP-PPase {ECO:0000255|HAMAP-Rule:MF_01327};
GN Name=thiE {ECO:0000255|HAMAP-Rule:MF_01327}; OrderedLocusNames=sync_0791;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine
CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
CC {ECO:0000255|HAMAP-Rule:MF_01327}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl
CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2
CC H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-
CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate
CC + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575,
CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-
CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine
CC phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58296; EC=2.5.1.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01327};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01327};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01327};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine
CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01327}.
CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_01327}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI45071.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000435; ABI45071.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041426911.1; NC_008319.1.
DR AlphaFoldDB; Q0IC17; -.
DR SMR; Q0IC17; -.
DR STRING; 64471.sync_0791; -.
DR EnsemblBacteria; ABI45071; ABI45071; sync_0791.
DR KEGG; syg:sync_0791; -.
DR eggNOG; COG0352; Bacteria.
DR HOGENOM; CLU_064900_0_0_3; -.
DR OrthoDB; 461201at2; -.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000001961; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00097; TMP_synthase; 1.
DR HAMAP; MF_01327; TMP_synthase_cyanobact; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR041397; ThiD2.
DR InterPro; IPR034291; TMP_synthase.
DR InterPro; IPR016229; TMP_synthase_cyanobac_bac.
DR Pfam; PF17792; ThiD2; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1.
DR SUPFAM; SSF51391; SSF51391; 1.
DR TIGRFAMs; TIGR00693; thiE; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Reference proteome; Thiamine biosynthesis;
KW Transferase.
FT CHAIN 1..353
FT /note="Thiamine-phosphate synthase"
FT /id="PRO_0000415379"
FT REGION 1..128
FT /note="Unknown"
FT REGION 129..353
FT /note="Thiamine-phosphate synthase"
FT BINDING 185..189
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 217
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 256
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 282..284
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 285
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
FT BINDING 312
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01327"
SQ SEQUENCE 353 AA; 39116 MW; B47DC1A90AD05BCA CRC64;
MELMVVEADA KLRVARLIDA NLDRAREGLR VIEDWCRFGL DRDDLVLPLK DWRQRLGQQH
HDRYRRARST ATDVAAGLGH PAQTSRCSAP AIIKANASRV QEALRVLEEF GRNLDPDLAS
TAAEIRYGLY DLEVRILEAC GRQHRQERLE GAKLCLITDP DRDNNLERLL HGVEAALMAG
VSLVQYRRKQ GNDKQRLLEA QALKTLCSRF EALFIVNDRI DLALLVDADG VHLGQDDLPL
SEARQLLGPE RLLGRSTHRL EHLLEAQQAG ADYLGVGPVF ATKTKRDLSP AGLSWVTEAS
RHAAVPWFAI GGIDIETIPS VRAAGAQRVA VVSAIMSSND PEEASRTLLQ TLA
