ID   THID_HELPY              Reviewed;         270 AA.
AC   O25515;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 118.
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=HP_0844;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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}.
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DR   EMBL; AE000511; AAD07890.1; -; Genomic_DNA.
DR   PIR; D64625; D64625.
DR   RefSeq; NP_207637.1; NC_000915.1.
DR   AlphaFoldDB; O25515; -.
DR   SMR; O25515; -.
DR   STRING; 85962.HP_0844; -.
DR   PaxDb; 85962-C694_04325; -.
DR   EnsemblBacteria; AAD07890; AAD07890; HP_0844.
DR   KEGG; hpy:HP_0844; -.
DR   PATRIC; fig|85962.8.peg.878; -.
DR   eggNOG; COG0351; Bacteria.
DR   InParanoid; O25515; -.
DR   OrthoDB; 9810880at2; -.
DR   PhylomeDB; O25515; -.
DR   UniPathway; UPA00060; UER00137.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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; 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; Reference proteome;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN           1..270
FT                   /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT                   kinase"
FT                   /id="PRO_0000192020"
FT   BINDING         46
FT                   /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:16892"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  28925 MW;  C4F99BCABBD7204E CRC64;
     MVKIYPQVLS IAGSDSGGGS GIQADLKAFQ TLGVFGTSVI TCITAQNTQG VHGVYPLSVE
     SVKAQILAIR DDFSIKAFKM GALCNAQIIE CVADTLETCD FGLCVLDPVM VAKNGALLLE
     EEAILSLKKR LLPTTHLLTP NLPEVYALTG VQVRDDKSAS KAMGVLRDLG VKNAVIKGGH
     TEHFQGEYSN DWVFLEDAEF ILNAKRFNTK NTHGTGCTLS SLIVGLLAQG LDLKNAISKA
     KELLTIIIQN PLNIGHGHGP LNLWSIKELV
//