THID_ECOLI
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 03-AUG-2022, entry version 149.
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; Proteobacteria; 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}.
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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 PRIDE; P76422; -.
DR EnsemblBacteria; AAC75164; AAC75164; b2103.
DR EnsemblBacteria; BAA15971; BAA15971; BAA15971.
DR GeneID; 66674001; -.
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 PhylomeDB; P76422; -.
DR BioCyc; EcoCyc:HMP-P-KIN-MON; -.
DR BioCyc; MetaCyc:HMP-P-KIN-MON; -.
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; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IDA:EcoCyc.
DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IDA:EcoCyc.
DR CDD; cd01169; HMPP_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR045029; HMP/HMP-P_kinase.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR20858; PTHR20858; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00097; HMP-P_kinase; 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
