ID THID_ECOLI STANDARD; PRT; 266 AA. AC P76422; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) DE Phosphomethylpyrimidine kinase (EC 2.7.4.7) (HMP-phosphate kinase) DE (HMP-P kinase). GN Name=thiD; OrderedLocusNames=b2103; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; 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., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=K12; RX MEDLINE=97251358; PubMed=9097040; 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., RA Yamamoto Y., Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). RN [3] RP NUCLEOTIDE SEQUENCE, AND CHARACTERIZATION. RC STRAIN=K12 / W3310; RX MEDLINE=99173753; PubMed=10075431; 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). CC -!- FUNCTION: Catalyzes the phosphorylation of HMP-P to HMP-PP. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-2-methyl-5- CC phosphomethylpyrimidine = ADP + 4-amino-2-methyl-5- CC diphosphomethylpyrimidine. CC -!- PATHWAY: Thiamine biosynthesis. CC -!- SIMILARITY: Belongs to the thiD family. 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; U00096; AAC75164.1; -. DR EMBL; D90848; BAA15971.1; -. DR EMBL; D84200; BAA76742.1; -. DR PIR; F64977; F64977. DR HSSP; P55882; 1JXH. DR SMR; P76422; 1-266. DR EchoBASE; EB3821; -. DR EcoGene; EG14068; thiD. DR InterPro; IPR004399; HMP-P_kinase. DR TIGRFAMs; TIGR00097; HMP-P_kinase; 1. KW Complete proteome; Kinase; Thiamine biosynthesis; Transferase. 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 //