ID   THID_AQUAE              Reviewed;         255 AA.
AC   O67772;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 121.
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=aq_1960;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07733.1; -; Genomic_DNA.
DR   PIR; H70467; H70467.
DR   RefSeq; NP_214341.1; NC_000918.1.
DR   RefSeq; WP_010881277.1; NC_000918.1.
DR   AlphaFoldDB; O67772; -.
DR   SMR; O67772; -.
DR   STRING; 224324.aq_1960; -.
DR   EnsemblBacteria; AAC07733; AAC07733; aq_1960.
DR   KEGG; aae:aq_1960; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_0_0; -.
DR   InParanoid; O67772; -.
DR   OrthoDB; 9810880at2; -.
DR   UniPathway; UPA00060; UER00137.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000000798; 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..255
FT                   /note="Hydroxymethylpyrimidine/phosphomethylpyrimidine
FT                   kinase"
FT                   /id="PRO_0000192016"
FT   BINDING         41
FT                   /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:16892"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   255 AA;  28066 MW;  95A4CA5F662F708F CRC64;
     MIALSIAGFD NSGGAGTLAD IRTFKHFGIY GVAVITALAV QNTQKVYEVF PIPPDVVKEE
     LKAIFEDFPI KGVKIGMLAN KEIAEVVYET LKSKKTNFIV LDPVFRSKSG RELLSEEGVE
     FLKSEFIKIV DLITPNVPEA EILCGEEIKS LEDVKNCAQK IYSLGAKSVL IKGGHLKGNY
     AIDILYDGKS FYEFKAPKIA GKTPRGTGCV YSSAILANYL RHKDLIKAIK TAKDFITEAI
     KNSKKLGKGY EIMDF
//