ID K8GID6_9CYAN Unreviewed; 352 AA.
AC K8GID6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=OsccyDRAFT_4343 {ECO:0000313|EMBL:EKQ67266.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ67266.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ67266.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ67266.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-2012) 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:EKQ67266.1}.
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DR EMBL; AJUB01000017; EKQ67266.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GID6; -.
DR STRING; 864702.OsccyDRAFT_4343; -.
DR PATRIC; fig|864702.5.peg.4652; -.
DR eggNOG; COG0352; Bacteria.
DR HOGENOM; CLU_064900_0_0_3; -.
DR OrthoDB; 9812206at2; -.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000001332; 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 Reference proteome {ECO:0000313|Proteomes:UP000001332};
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..328
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..352
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 305
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 352 AA; 39291 MW; 826FE382C061D6D1 CRC64;
MSAMHNQNRF IQLSLYRILD ANLDRAREGL RIIEEWCRFG LDNAQLTEEC KTLRQELAQW
HTAELRAARD TPSDAGTELT HPSEEQRADI QQVLQANLCR VQEALRVLEE YGKVYRADMG
AACKQMRYRV YTLESQLIRH DYQQKLQSAR LYLVTAPSEK LFATVEAALQ GGLTLVQHRD
KEADDETRLV TAHQLCQLCH RFGALFIVND RVDIALAVGA DGVHLGQQDL PLPLARRLLG
SQRIIGCSTK NPDEMHRAIQ EGADYIGVGP VYATPTKAGR AAAGLEYVRY AAEHAATIPW
FAIGGIDATN VQDVLAAGAR RVAVVRAIMQ SDQPTAVTQQ LLSQITSTQK EY
//
