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Entry: A0A1E5QEB5_9CYAN
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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
//
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