THIED_GEOSL
ID THIED_GEOSL Reviewed; 490 AA.
AC P61422;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Thiamine biosynthesis bifunctional protein ThiED;
DE Includes:
DE RecName: Full=Thiamine-phosphate synthase;
DE Short=TMP-PPase;
DE Short=TP synthase;
DE Short=TPS;
DE EC=2.5.1.3 {ECO:0000250|UniProtKB:P39594};
DE AltName: Full=Thiamine-phosphate pyrophosphorylase;
DE Short=TMP pyrophosphorylase;
DE Includes:
DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase;
DE EC=2.7.1.49 {ECO:0000250|UniProtKB:P76422};
DE EC=2.7.4.7 {ECO:0000250|UniProtKB:P76422};
DE AltName: Full=Hydroxymethylpyrimidine kinase;
DE Short=HMP kinase;
DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase;
DE Short=HMP-P kinase;
DE Short=HMP-phosphate kinase;
DE Short=HMPP kinase;
GN Name=thiDE; OrderedLocusNames=GSU0605;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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:0000250|UniProtKB:P39594}.
CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
CC {ECO:0000250|UniProtKB:P76422}.
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:0000250|UniProtKB:P39594};
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:0000250|UniProtKB:P39594};
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:0000250|UniProtKB:P39594};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC EC=2.7.1.49; Evidence={ECO:0000250|UniProtKB:P76422};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC Evidence={ECO:0000250|UniProtKB:P76422};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 3/3.
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 -!- SIMILARITY: In the N-terminal section; belongs to the thiamine-
CC phosphate synthase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ThiD family.
CC {ECO:0000305}.
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DR EMBL; AE017180; AAR33936.1; -; Genomic_DNA.
DR RefSeq; NP_951663.1; NC_002939.5.
DR RefSeq; WP_010941267.1; NC_002939.5.
DR AlphaFoldDB; P61422; -.
DR SMR; P61422; -.
DR STRING; 243231.GSU0605; -.
DR EnsemblBacteria; AAR33936; AAR33936; GSU0605.
DR KEGG; gsu:GSU0605; -.
DR PATRIC; fig|243231.5.peg.603; -.
DR eggNOG; COG0351; Bacteria.
DR eggNOG; COG0352; Bacteria.
DR HOGENOM; CLU_020520_5_1_7; -.
DR InParanoid; P61422; -.
DR OMA; HSGKERR; -.
DR UniPathway; UPA00060; UER00138.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01169; HMPP_kinase; 1.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_00097; TMP_synthase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045029; HMP/HMP-P_kinase.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR034291; TMP_synthase.
DR PANTHER; PTHR20858; PTHR20858; 2.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR SUPFAM; SSF51391; SSF51391; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1.
DR TIGRFAMs; TIGR00693; thiE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..490
FT /note="Thiamine biosynthesis bifunctional protein ThiED"
FT /id="PRO_0000192040"
FT REGION 1..213
FT /note="Thiamine-phosphate synthase"
FT REGION 229..490
FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT kinase"
FT BINDING 50..54
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 147..149
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT BINDING 197..198
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT /ligand_id="ChEBI:CHEBI:16892"
FT /evidence="ECO:0000250"
SQ SEQUENCE 490 AA; 51910 MW; 924B153FCD5E83D4 CRC64;
MASNGHTLRL VINRDKHDSV IRGLYLVTDH DDNLIPRVEA AIDGGARVVQ YRNKNQDRES
RLALGLELRE LCRRRSIPFI VNDDLEMAVS LKADGLHLGQ GDGDPREARR VLGPGKIIGV
STHTLSEALE AQAAGVDYIG LGAMFPSRSK EVEHVAGSEL LAAIRSSISI PIVAIGGITR
DNGASVIDAG ADAVAVISAV LSHPDPALAA TEIALLFNRR APFPRGSVLT VAGSDSGGGA
GIQADLKTVT LLGSYGSSVL TALTAQNTRG VSGIHGVPPA FVADQLDAVF SDIPVDVVKT
GMLFSAETIV AIAAKLTEYR RRMVVVDPVM VAKGGANLID RGAVSVLKER LFPLAYLVTP
NIPEAERLTG ANISDEESMR EAARRLHRLG ARNVLLKGGH LLAGDSVDIL FDGAAFHRFV
SPRILSKNTH GTGCTFASAI ATYLAQGDPL REAIARAKRY ITAAIRLAQP LGRGHGPVNH
ILAAEDVRDR
