ID THID_SALTY Reviewed; 266 AA. AC P55882; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 02-SEP-2026, entry version 146. 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=thiD; OrderedLocusNames=STM2146; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2; RX PubMed=9244280; DOI=10.1128/jb.179.15.4894-4900.1997; RA Petersen L.A., Downs D.M.; RT "Identification and characterization of an operon in Salmonella typhimurium RT involved in thiamine biosynthesis."; RL J. Bacteriol. 179:4894-4900(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH RP 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE, AND SUBUNIT. RX PubMed=11839308; DOI=10.1016/s0969-2126(02)00708-6; RA Cheng G., Bennett E.M., Begley T.P., Ealick S.E.; RT "Crystal structure of 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate RT kinase from Salmonella typhimurium at 2.3 A resolution."; RL Structure 10:225-235(2002). 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=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 -!- 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: Homodimer. {ECO:0000269|PubMed:11839308}. 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; U87940; AAB66492.1; -; Genomic_DNA. DR EMBL; AE006468; AAL21049.1; -; Genomic_DNA. DR RefSeq; NP_461090.1; NC_003197.2. DR RefSeq; WP_001188957.1; NC_003197.2. DR PDB; 1JXH; X-ray; 2.30 A; A/B=1-266. DR PDB; 1JXI; X-ray; 2.64 A; A/B=1-266. DR AlphaFoldDB; P55882; -. DR SMR; P55882; -. DR STRING; 99287.STM2146; -. DR DrugBank; DB02022; 4-Amino-5-Hydroxymethyl-2-Methylpyrimidine. DR PaxDb; 99287-STM2146; -. DR GeneID; 1253667; -. DR KEGG; stm:STM2146; -. DR PATRIC; fig|99287.12.peg.2271; -. DR HOGENOM; CLU_020520_0_1_6; -. DR OMA; NRHTHGT; -. DR PhylomeDB; P55882; -. DR BioCyc; SENT99287:STM2146-MONOMER; -. DR BRENDA; 2.7.1.49; 5542. DR BRENDA; 2.7.4.7; 5542. DR UniPathway; UPA00060; UER00137. DR UniPathway; UPA00060; UER00138. DR EvolutionaryTrace; P55882; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IBA:GO_Central. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01169; HMPP_kinase; 1. DR FunFam; 3.40.1190.20:FF:000003; Phosphomethylpyrimidine kinase ThiD; 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. DR PDBsum; 1JXH; -. DR PDBsum; 1JXI; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1..266 FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine FT kinase" FT /id="PRO_0000192026" FT BINDING 44 FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine" FT /ligand_id="ChEBI:CHEBI:16892" FT /evidence="ECO:0000269|PubMed:11839308" FT CONFLICT 44 FT /note="Q -> E (in Ref. 1; AAB66492)" FT /evidence="ECO:0000305" FT STRAND 5..11 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 19..29 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 33..45 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 48..54 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 57..68 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 74..78 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 84..96 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 119..124 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 125..129 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 140..147 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 155..167 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 171..176 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 211..222 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 223..225 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 229..244 FT /evidence="ECO:0007829|PDB:1JXH" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:1JXH" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:1JXH" FT TURN 261..265 FT /evidence="ECO:0007829|PDB:1JXH" SQ SEQUENCE 266 AA; 28544 MW; F8B94332E1616368 CRC64; MQRINALTIA GTDPSGGAGI QADLKTFSAL GAYGCSVITA LVAQNTCGVQ SVYRIEPDFV AAQLDSVFSD VRIDTTKIGM LAETDIVEAV AERLQRHHVR NVVLDTVMLA KSGDPLLSPS AIETLRVRLL PQVSLITPNL PEAAALLDAP HARTEQEMLA QGRALLAMGC EAVLMKGGHL EDAQSPDWLF TREGEQRFSA PRVNTKNTHG TGCTLSAALA ALRPRHRSWG ETVNEAKAWL SAALAQADTL EVGKGIGPVH HFHAWW //