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Database: UniProt
Entry: D2QZS3_PIRSD
LinkDB: D2QZS3_PIRSD
Original site: D2QZS3_PIRSD 
ID   D2QZS3_PIRSD            Unreviewed;       380 AA.
AC   D2QZS3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Thiamine-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TP synthase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TPS {ECO:0000256|HAMAP-Rule:MF_00097};
DE            EC=2.5.1.3 {ECO:0000256|HAMAP-Rule:MF_00097};
DE   AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TMP pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00097};
DE            Short=TMP-PPase {ECO:0000256|HAMAP-Rule:MF_00097};
GN   Name=thiE {ECO:0000256|HAMAP-Rule:MF_00097};
GN   OrderedLocusNames=Psta_1882 {ECO:0000313|EMBL:ADB16556.1};
OS   Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS   staleyi).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Pirellula.
OX   NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB16556.1, ECO:0000313|Proteomes:UP000001887};
RN   [1] {ECO:0000313|EMBL:ADB16556.1, ECO:0000313|Proteomes:UP000001887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC   {ECO:0000313|Proteomes:UP000001887};
RX   PubMed=21304671; DOI=10.4056/sigs.51657;
RA   Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA   Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL   Stand. Genomic Sci. 1:308-316(2009).
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_00097}.
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_00097, 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_00097, 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_00097, ECO:0000256|RuleBase:RU003826};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00097};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00097};
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_00097}.
CC   -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00097, ECO:0000256|RuleBase:RU003826}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00097}.
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DR   EMBL; CP001848; ADB16556.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2QZS3; -.
DR   STRING; 530564.Psta_1882; -.
DR   KEGG; psl:Psta_1882; -.
DR   eggNOG; COG0352; Bacteria.
DR   HOGENOM; CLU_064900_0_0_0; -.
DR   OMA; EEWCRFG; -.
DR   OrthoDB; 9812206at2; -.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000001887; 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   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_00097};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001887};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW   Rule:MF_00097};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00097}.
FT   DOMAIN          27..149
FT                   /note="ThiD2"
FT                   /evidence="ECO:0000259|Pfam:PF17792"
FT   DOMAIN          166..355
FT                   /note="Thiamine phosphate synthase/TenI"
FT                   /evidence="ECO:0000259|Pfam:PF02581"
FT   BINDING         195..199
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         237
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         276
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         302..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_00097"
FT   BINDING         305
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00097"
FT   BINDING         332
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_00097"
SQ   SEQUENCE   380 AA;  41201 MW;  15423EBDD672E02B CRC64;
     MTYDKNSGDD HRPNLPPSSG EQLAALRILD ANFNRVSEGL RVVEEYCRFA LEDRHLAQNA
     KEIRHDIGHL AAGISPETLA KARETLRDVG TGVTLGSEKT RAGILDVVIA STKRVEQSLR
     AIEEYAKLGY PQLSAAAKQL RYRAYTLARA MLLTDHHRQQ MAKRLLYVLI DGRASDAEFA
     SLVRMLVEAR VDVLQLRDKR LTDRQLLEKA QLLKSLVEQF APAGAEETAE RPLLVMNDRP
     DLALLARLDG VHVGQDELPV DAVRKIVGPE MLVGVSTHSI EQARQAVLDG ASYIGCGPVF
     PSNTKQFGSF VGTEFLAQVA AEIQLPAFAI GGITLENLPQ VTAAGFSRVA VSAAVSSAAD
     PATAARLLKT ELLAAAARQA
//
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