ID   THID_STAAR              Reviewed;         276 AA.
AC   Q6GEY2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SAR2182;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG41162.1; -; Genomic_DNA.
DR   RefSeq; WP_000594963.1; NC_002952.2.
DR   AlphaFoldDB; Q6GEY2; -.
DR   SMR; Q6GEY2; -.
DR   KEGG; sar:SAR2182; -.
DR   HOGENOM; CLU_020520_0_0_9; -.
DR   OMA; DNRHTHG; -.
DR   OrthoDB; 461201at2; -.
DR   UniPathway; UPA00060; UER00137.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000000596; Chromosome.
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; 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; Thiamine biosynthesis;
KW   Transferase.
FT   CHAIN           1..276
FT                   /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT                   kinase"
FT                   /id="PRO_0000192030"
FT   BINDING         45
FT                   /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:16892"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  30212 MW;  0A09A048CB42D752 CRC64;
     MIKPKIALTI AGTDPTGGAG VMADLKSFHS CGVYGMGVVT SIVAQNTLGV QHIHNLNHQW
     VDEQLDSVFN DTLPHAIKTG MIATADTMET IRHYLMQHES IPYVIDPVML AKSGDSLMDN
     NTKQNLQHTL LPLADVVTPN LPEAEEITGL TIDSEEKIMQ AGRIFINEIG SKGVIIKGGH
     SNDADIAKDY LFTKEGVQTF ENERFKTKHT HGTGCTFSAV ITAELAKGRP LFEAVHKAKK
     FISMSIQYTP EIGRGRGPVN HFAYLKKEGL DDELSK