ID THID_ECOLI Reviewed; 266 AA. AC P76422; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-SEP-2023, entry version 154. DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; DE EC=2.7.1.49 {ECO:0000269|PubMed:10075431}; DE EC=2.7.4.7 {ECO:0000269|PubMed:10075431}; 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=thiD; Synonyms=thiJ; OrderedLocusNames=b2103, JW2090; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, RP CATALYTIC ACTIVITY, AND SUBUNIT. RC STRAIN=K12; RX PubMed=10075431; DOI=10.1099/13500872-145-2-495; RA Mizote T., Tsuda M., Smith D.D.S., Nakayama H., Nakazawa T.; RT "Cloning and characterization of the thiD/J gene of Escherichia coli RT encoding a thiamin-synthesizing bifunctional enzyme, RT hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase."; RL Microbiology 145:495-501(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097040; DOI=10.1093/dnares/3.6.379; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., RA Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity CC with pyridoxal, pyridoxamine or pyridoxine. CC {ECO:0000269|PubMed:10075431}. 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:0000269|PubMed:10075431}; 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:0000269|PubMed:10075431}; 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 2/3. 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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10075431}. CC -!- SIMILARITY: Belongs to the ThiD family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D84200; BAA76742.1; -; Genomic_DNA. DR EMBL; U00096; AAC75164.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15971.1; -; Genomic_DNA. DR PIR; F64977; F64977. DR RefSeq; NP_416606.1; NC_000913.3. DR RefSeq; WP_000822274.1; NZ_STEB01000002.1. DR AlphaFoldDB; P76422; -. DR SMR; P76422; -. DR BioGRID; 4261536; 8. DR DIP; DIP-6867N; -. DR IntAct; P76422; 7. DR STRING; 511145.b2103; -. DR jPOST; P76422; -. DR PaxDb; P76422; -. DR EnsemblBacteria; AAC75164; AAC75164; b2103. DR EnsemblBacteria; BAA15971; BAA15971; BAA15971. DR GeneID; 75205961; -. DR GeneID; 946459; -. DR KEGG; ecj:JW2090; -. DR KEGG; eco:b2103; -. DR PATRIC; fig|1411691.4.peg.144; -. DR EchoBASE; EB3821; -. DR eggNOG; COG0351; Bacteria. DR HOGENOM; CLU_020520_0_1_6; -. DR InParanoid; P76422; -. DR OMA; DNRHTHG; -. DR OrthoDB; 9810880at2; -. DR PhylomeDB; P76422; -. DR BioCyc; EcoCyc:HMP-P-KIN-MONOMER; -. DR BioCyc; MetaCyc:HMP-P-KIN-MONOMER; -. DR BRENDA; 2.7.1.49; 2026. DR BRENDA; 2.7.4.7; 2026. DR UniPathway; UPA00060; UER00137. DR UniPathway; UPA00060; UER00138. DR PRO; PR:P76422; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IDA:EcoCyc. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IDA:EcoCyc. 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; IMP:EcoCyc. DR GO; GO:0036172; P:thiamine salvage; IGI:EcoCyc. DR CDD; cd01169; HMPP_kinase; 1. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR004399; HMP/HMP-P_kinase_dom. DR InterPro; IPR013749; PM/HMP-P_kinase-1. DR InterPro; IPR029056; Ribokinase-like. DR NCBIfam; TIGR00097; HMP-P_kinase; 1. DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE/PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1. DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1. DR Pfam; PF08543; Phos_pyr_kin; 1. DR SUPFAM; SSF53613; Ribokinase-like; 1. PE 1: Evidence at protein level; KW ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding; KW Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1..266 FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine FT kinase" FT /id="PRO_0000192018" FT BINDING 44 FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine" FT /ligand_id="ChEBI:CHEBI:16892" FT /evidence="ECO:0000250" SQ SEQUENCE 266 AA; 28634 MW; E555CEFE445B8F0A CRC64; MKRINALTIA GTDPSGGAGI QADLKTFSAL GAYGCSVITA LVAQNTRGVQ SVYRIEPDFV AAQLDSVFSD VRIDTTKIGM LAETDIVEAV AERLQRYQIQ NVVLDTVMLA KSGDPLLSPS AVATLRSRLL PQVSLITPNL PEAAALLDAP HARTEQEMLE QGRSLLAMGC GAVLMKGGHL DDEQSPDWLF TREGEQRFTA PRIMTKNTHG TGCTLSAALA ALRPRHTNWA DTVQEAKSWL SSALAQADTL EVGHGIGPVH HFHAWW //