THID_HELPY
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 03-AUG-2022, entry version 109.
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; Proteobacteria; 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}.
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; AE000511; AAD07890.1; -; Genomic_DNA.
DR PIR; D64625; D64625.
DR RefSeq; NP_207637.1; NC_000915.1.
DR RefSeq; WP_010875551.1; NC_018939.1.
DR AlphaFoldDB; O25515; -.
DR SMR; O25515; -.
DR STRING; 85962.C694_04325; -.
DR PaxDb; O25515; -.
DR EnsemblBacteria; AAD07890; AAD07890; HP_0844.
DR KEGG; hpy:HP_0844; -.
DR PATRIC; fig|85962.8.peg.878; -.
DR eggNOG; COG0351; Bacteria.
DR OMA; DNRHTHG; -.
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; 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 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
