ID A0A1E5QEB5_9CYAN Unreviewed; 355 AA.
AC A0A1E5QEB5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=BH720_22305 {ECO:0000313|EMBL:OEJ72951.1};
OS Desertifilum tharense IPPAS B-1220.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Desertifilum.
OX NCBI_TaxID=1781255 {ECO:0000313|EMBL:OEJ72951.1, ECO:0000313|Proteomes:UP000095472};
RN [1] {ECO:0000313|EMBL:OEJ72951.1, ECO:0000313|Proteomes:UP000095472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPPAS B-1220 {ECO:0000313|EMBL:OEJ72951.1,
RC ECO:0000313|Proteomes:UP000095472};
RA Sinetova M.A., Bolakhan K., Zayadan B.K., Mironov K.S., Ustinova V.,
RA Kupriyanova E.V., Sidorov R.A., Skrypnik A.N., Gogoleva N.E., Gogolev Y.V.,
RA Los D.A.;
RT "Draft genome of thermotolerant cyanobacterium Desertifilum sp. strain
RT IPPAS B-1220.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OEJ72951.1}.
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DR EMBL; MJGC01000106; OEJ72951.1; -; Genomic_DNA.
DR RefSeq; WP_069969430.1; NZ_MJGC01000106.1.
DR AlphaFoldDB; A0A1E5QEB5; -.
DR STRING; 1781255.BH720_22305; -.
DR OrthoDB; 9812206at2; -.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000095472; Unassembled WGS sequence.
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; THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; 1.
DR PANTHER; PTHR20857:SF15; THIAMINE-PHOSPHATE SYNTHASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000095472};
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 17..135
FT /note="ThiD2"
FT /evidence="ECO:0000259|Pfam:PF17792"
FT DOMAIN 151..327
FT /note="Thiamine phosphate synthase/TenI"
FT /evidence="ECO:0000259|Pfam:PF02581"
FT REGION 1..129
FT /note="Unknown"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT REGION 130..355
FT /note="Thiamine-phosphate synthase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 177..181
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 209
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 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01327"
FT BINDING 248
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 274..276
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 277
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 304
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 355 AA; 39794 MW; AA8164CDCF179A37 CRC64;
MGDIYEQSRA FQPTVHRILD ANLDRAREGL RIIEEWCRFG LNSEGLTNEC KQLRQALAVW
HTPEIRAARN TAGDPGTELT HPQEKERSSI GQLLQVNLCR VEEALRVLEE YGKLHHAKMG
EACKQMRYRV YLLETNLMAY QRRQRLRDST LYLITSPSDR LLTVVEAALQ GGLTLVQYRS
KTADDLVRLE EAQKLRSLCD RYGALLIVND RVDIALAVDA DGVHLGQQDI PIGLARQLLG
PQRLIGRSTT NPEEMQRAIA EGADYIGVGP VYATPTKADK AAAGLEYVRY AAEKASVPWF
AIGGIDLENL NQVLDAGATR ISVVRAVMQA EQPTLTTQYF LSQLTRMQTM RSLHP
//