ID A0A0M4U0M8_9NOSO Unreviewed; 371 AA.
AC A0A0M4U0M8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Thiamine-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01327};
DE Short=TP synthase {ECO:0000256|HAMAP-Rule:MF_01327};
DE Short=TPS {ECO:0000256|HAMAP-Rule:MF_01327};
DE EC=2.5.1.3 {ECO:0000256|HAMAP-Rule:MF_01327};
DE AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01327};
DE Short=TMP pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_01327};
DE Short=TMP-PPase {ECO:0000256|HAMAP-Rule:MF_01327};
GN Name=thiE {ECO:0000256|HAMAP-Rule:MF_01327};
GN ORFNames=ACX27_29190 {ECO:0000313|EMBL:ALF56001.1};
OS Nostoc piscinale CENA21.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=224013 {ECO:0000313|EMBL:ALF56001.1, ECO:0000313|Proteomes:UP000062645};
RN [1] {ECO:0000313|Proteomes:UP000062645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA21 {ECO:0000313|Proteomes:UP000062645};
RA Leao T.F., Leao P.N., Guimaraes P.I., de Melo A.G.C., Ramos R.T.J.,
RA Silva A., Fiore M.F., Schneider M.P.C.;
RT "Genome Of Nitrogen-Fixing Cyanobacterium Nostoc piscinale CENA21 From
RT Solimoes/Amazon River Floodplain Sediments And Comparative Genomics To
RT Uncover Biosynthetic Natural Products Potential.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALF56001.1, ECO:0000313|Proteomes:UP000062645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA21 {ECO:0000313|EMBL:ALF56001.1,
RC ECO:0000313|Proteomes:UP000062645};
RX PubMed=27034496;
RA Leao T., Guimaraes P.I., de Melo A.G., Ramos R.T., Leao P.N., Silva A.,
RA Fiore M.F., Schneider M.P.;
RT "Draft Genome Sequence of the N2-Fixing Cyanobacterium Nostoc piscinale
RT CENA21, Isolated from the Brazilian Amazon Floodplain.";
RL Genome Announc. 4:0-0(2016).
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:0000256|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:0000256|ARBA:ARBA00000876, ECO:0000256|HAMAP-
CC Rule:MF_01327, ECO:0000256|RuleBase:RU003826};
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:0000256|ARBA:ARBA00001829, ECO:0000256|HAMAP-
CC Rule:MF_01327, ECO:0000256|RuleBase:RU003826};
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001159, ECO:0000256|HAMAP-
CC Rule:MF_01327, ECO:0000256|RuleBase:RU003826};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01327};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|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.
CC {ECO:0000256|ARBA:ARBA00005165, ECO:0000256|HAMAP-Rule:MF_01327}.
CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_01327, ECO:0000256|RuleBase:RU003826}.
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DR EMBL; CP012036; ALF56001.1; -; Genomic_DNA.
DR RefSeq; WP_062297698.1; NZ_CP012036.1.
DR AlphaFoldDB; A0A0M4U0M8; -.
DR STRING; 224013.ACX27_29190; -.
DR PATRIC; fig|224013.5.peg.6977; -.
DR OrthoDB; 9812206at2; -.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000062645; 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; Aldolase class I; 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 NCBIfam; TIGR00693; thiE; 1.
DR PANTHER; PTHR20857:SF15; THIAMINE BIOSYNTHETIC BIFUNCTIONAL ENZYME; 1.
DR PANTHER; PTHR20857; THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; 1.
DR Pfam; PF17792; ThiD2; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR PIRSF; PIRSF000512; TMP_PPase_Cyanobac_prd; 1.
DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01327};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01327};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_01327};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01327}.
FT DOMAIN 32..150
FT /note="ThiD2"
FT /evidence="ECO:0000259|Pfam:PF17792"
FT DOMAIN 166..341
FT /note="Thiamine phosphate synthase/TenI"
FT /evidence="ECO:0000259|Pfam:PF02581"
FT REGION 1..144
FT /note="Unknown"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT REGION 145..371
FT /note="Thiamine-phosphate synthase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 192..196
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 224
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 263
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 289..291
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 292
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 319
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
SQ SEQUENCE 371 AA; 41830 MW; 9314613171018589 CRC64;
MKEADYYEST NGVVVMVEPY SQQEQIQQIV YRILDANLDR TREGLRIIEE WCRFGLNNAQ
LAGECKYLRQ ELAKWHTAEI RAARDTVGDI GTDLSHPQEE QRASIKSLLQ ANFCRVQEAL
RVLEEYGKLY SPNMGKAFKQ MRYRVYTLES SLMGYQRHQL LWRSHLYLVT SPSDSLFATV
ESALKGGLTL VQYRDKNSDD TVRLEQATRL RQLCHAYGAL LIMNDRVDLA LAVDADGVHL
GQQDMPIALA RQLLGPQRII GRSTTNSEEM HRAINEGADY IGVGPIYETP TKAGKAAAGL
EYVRYAAQNS PIPWFAIGGI DANNINDVID AGAERVAVVR SLMQAEQPTL VTQYLLSQLN
RVRPQPEIVQ N
//
