ID   THIED_CORGL             Reviewed;         763 AA.
AC   Q8NQH1;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Thiamine biosynthesis multifunctional 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=theD; Synonyms=thiD1; OrderedLocusNames=Cgl1463, cg1654;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(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 central section; belongs to the ThiD family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the thiaminase-2
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB98856.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000036; BAB98856.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BX927152; CAF21472.1; -; Genomic_DNA.
DR   RefSeq; NP_600680.3; NC_003450.3.
DR   RefSeq; WP_011014382.1; NC_006958.1.
DR   AlphaFoldDB; Q8NQH1; -.
DR   SMR; Q8NQH1; -.
DR   STRING; 196627.cg1654; -.
DR   DNASU; 3345397; -.
DR   KEGG; cgb:cg1654; -.
DR   KEGG; cgl:Cgl1463; -.
DR   PATRIC; fig|196627.13.peg.1430; -.
DR   eggNOG; COG0351; Bacteria.
DR   eggNOG; COG0352; Bacteria.
DR   eggNOG; COG0819; Bacteria.
DR   HOGENOM; CLU_020520_2_0_11; -.
DR   OrthoDB; 34166at2; -.
DR   BioCyc; CORYNE:G18NG-11046-MONOMER; -.
DR   UniPathway; UPA00060; UER00138.
DR   UniPathway; UPA00060; UER00141.
DR   Proteomes; UP000000582; Chromosome.
DR   Proteomes; UP000001009; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01169; HMPP_kinase; 1.
DR   CDD; cd19365; TenA_C-like; 1.
DR   CDD; cd00564; TMP_TenI; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR   HAMAP; MF_00097; TMP_synthase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR004305; Thiaminase-2/PQQC.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   InterPro; IPR034291; TMP_synthase.
DR   NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR   NCBIfam; TIGR00693; thiE; 1.
DR   PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR   PANTHER; PTHR20858:SF21; THIAMINE-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   Pfam; PF03070; TENA_THI-4; 1.
DR   Pfam; PF02581; TMP-TENI; 1.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   SUPFAM; SSF51391; Thiamin phosphate synthase; 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..763
FT                   /note="Thiamine biosynthesis multifunctional protein ThiED"
FT                   /id="PRO_0000192039"
FT   REGION          1..210
FT                   /note="Thiamine-phosphate synthase"
FT   REGION          245..500
FT                   /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT                   kinase"
FT   REGION          550..763
FT                   /note="Thiaminase-2"
FT   BINDING         37..41
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000250"
FT   BINDING         140..142
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         143
FT                   /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:57841"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
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         194..195
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         282
FT                   /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:16892"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   763 AA;  80355 MW;  CA992321E884577F CRC64;
     MTDFSLYLVT DPVLGGGPEK VAGIVDSAIS GGVSVVQLRD KNSGVEDVRA AAKELKELCD
     ARGVALVVND YLDIAVELGL HLHIGQGDTP YTQARELLPA HLELGLSIEN LDQLHAVIAQ
     CAETGVALPD VIGIGPVAST ATKPDAAPAL GVEGIAEIAA VAQDHGIASV AIGGVGLRNA
     AELAATPIDG LCVVSEIMTA ANPAAAATRL RTAFQPTFSP ETQTELSQTE LQGAFVNSPS
     APRVLSIAGT DPTGGAGIQA DLKSIAAGGG YGMCVVTSLV AQNTHGVNTI HTPPLTFLEE
     QLEAVFSDVT VDAIKLGMLG SADTVDLVAS WLGSHEHGPV VLDPVMIATS GDRLLDASAE
     ESLRRLAVHV DVVTPNIPEL AVLCDSAPAI TMDEAIAQAQ GFARTHDTIV IVKGGHLTGA
     LADNAVVRPD GSVFQVENLR VNTTNSHGTG CSLSASLATK IAAGESVEKA LEWSTRWLNE
     ALRHADHLAV GTGNGPVDHG HLARRMTHAA ETTPWAHLRA PRLDGATAAS FTTPSTVKSP
     APRIEPAGPF TRALWEASGD IIAGINSSDF ITMLGDGTLR RPEFDFYIDQ DAQYLAQYSR
     ALARLSSIAP DSHAQIEWAQ SAAECLVVEA ELHRSYMAGK EVSAPSHITM AYTDFLIART
     YTEDYVCGVA AVLPCYWLYA EIGLMLAEQN HDEHPYKDWL NTYSGEEFIA GTRAAIARLE
     KALENAGAEQ RVDAARAFLS ASVHEREFFD QATRHGWTMV GSS
//