ID THID_RHIME Reviewed; 266 AA. AC P56904; Q52914; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2001, sequence version 2. DT 27-MAR-2024, entry version 119. 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=RB1087; ORFNames=SMb20962; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OG Plasmid pSymB (megaplasmid 2). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=042B; RA Yang S., Chen X.; RT "Cloning of a DNA fragment related to salt tolerance in Sinorhizobium RT meliloti."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11481431; DOI=10.1073/pnas.161294698; RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J., RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.; RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing RT endosymbiont Sinorhizobium meliloti."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., RA Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(2001). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-266. RC STRAIN=RCR2011 / SU47; RX PubMed=8246891; DOI=10.1007/bf00284690; RA Becker A., Kleickmann A., Keller M., Arnold W., Puehler A.; RT "Identification and analysis of the Rhizobium meliloti exoAMONP genes RT involved in exopolysaccharide biosynthesis and mapping of promoters located RT on the exoHKLAMONP fragment."; RL Mol. Gen. Genet. 241:367-379(1993). 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 -!- 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; AF070520; AAD46983.1; -; Genomic_DNA. DR EMBL; AL591985; CAC49487.1; -; Genomic_DNA. DR EMBL; Z22636; CAA80350.1; ALT_SEQ; Genomic_DNA. DR PIR; G95977; G95977. DR PIR; S78110; S78110. DR RefSeq; NP_437627.1; NC_003078.1. DR RefSeq; WP_010975923.1; NC_003078.1. DR AlphaFoldDB; P56904; -. DR SMR; P56904; -. DR EnsemblBacteria; CAC49487; CAC49487; SM_b20962. DR GeneID; 61601043; -. DR KEGG; sme:SM_b20962; -. DR PATRIC; fig|266834.11.peg.6017; -. DR eggNOG; COG0351; Bacteria. DR HOGENOM; CLU_020520_0_1_5; -. DR OrthoDB; 9810880at2; -. DR UniPathway; UPA00060; UER00137. DR UniPathway; UPA00060; UER00138. DR Proteomes; UP000001976; Plasmid pSymB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. 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 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Plasmid; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1..266 FT /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine FT kinase" FT /id="PRO_0000192025" FT BINDING 43 FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine" FT /ligand_id="ChEBI:CHEBI:16892" FT /evidence="ECO:0000250" FT CONFLICT 98..99 FT /note="KR -> RL (in Ref. 1; AAD46983)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="L -> F (in Ref. 1; AAD46983)" FT /evidence="ECO:0000305" FT CONFLICT 134 FT /note="V -> A (in Ref. 1; AAD46983)" FT /evidence="ECO:0000305" SQ SEQUENCE 266 AA; 27423 MW; 803D0C58EB9A1830 CRC64; MTAIALSIAG SDSGGGAGIQ ADLKTFSALG VYGASVITAI TAQNTRGVTA VEDVSAEIVS AQMDAVFSDL DVKAVKIGMV SRRETIAAIA DGLRRFGKRA VVDPVMVATS GDALLRPDAV AALIEELLPL ALVVTPNLAE AALMTGRAIA GDEAEMARQA EAIMRTGAHA VLVKGGHLKG QEATDLFFDG DTLVRLPAGR IETRNDHGTG CTLSAAIAAG LAKGVPLIEA VSAAKAYLHA AISAADRLEI GQGRGPVHHF HRWWKD //