ID   THI22_SCHPO             Reviewed;         551 AA.
AC   O94266;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2;
DE            EC=2.7.1.49 {ECO:0000250|UniProtKB:Q08975};
DE            EC=2.7.4.7 {ECO:0000250|UniProtKB:Q08975};
DE   AltName: Full=Hydroxymethylpyrimidine kinase 2;
DE            Short=HMP kinase 2;
DE   AltName: Full=Hydroxymethylpyrimidine phosphate kinase 2;
DE            Short=HMP-P kinase 2;
DE            Short=HMP-phosphate kinase 2;
DE            Short=HMPP kinase 2;
GN   ORFNames=SPBP8B7.18c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC       phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
CC       {ECO:0000250|UniProtKB:Q08975}.
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:Q08975};
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:Q08975};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ThiD family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the thiaminase-2
CC       family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA21803.1; -; Genomic_DNA.
DR   PIR; T40812; T40812.
DR   RefSeq; NP_596525.1; NM_001022446.2.
DR   AlphaFoldDB; O94266; -.
DR   SMR; O94266; -.
DR   BioGRID; 277884; 18.
DR   STRING; 284812.O94266; -.
DR   iPTMnet; O94266; -.
DR   MaxQB; O94266; -.
DR   PaxDb; 4896-SPBP8B7-18c-1; -.
DR   EnsemblFungi; SPBP8B7.18c.1; SPBP8B7.18c.1:pep; SPBP8B7.18c.
DR   GeneID; 2541373; -.
DR   KEGG; spo:SPBP8B7.18c; -.
DR   PomBase; SPBP8B7.18c; -.
DR   VEuPathDB; FungiDB:SPBP8B7.18c; -.
DR   eggNOG; KOG2598; Eukaryota.
DR   HOGENOM; CLU_020520_2_1_1; -.
DR   InParanoid; O94266; -.
DR   OMA; FWEMFPY; -.
DR   PhylomeDB; O94266; -.
DR   UniPathway; UPA00060; UER00137.
DR   UniPathway; UPA00060; UER00138.
DR   PRO; PR:O94266; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
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   CDD; cd19367; TenA_C_ScTHI20-like; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR   InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR004305; Thiaminase-2/PQQC.
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   Pfam; PF03070; TENA_THI-4; 1.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN           1..551
FT                   /note="Putative
FT                   hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2"
FT                   /id="PRO_0000315973"
FT   BINDING         76
FT                   /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine"
FT                   /ligand_id="ChEBI:CHEBI:16892"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   551 AA;  61354 MW;  8FA207F9F1472C00 CRC64;
     MPYNPLYESL SNQFDPSRIE TVLDPMGYTI KRRALPVSLT IAGSDCSGGA GIQADLKTMT
     SLGVYGMSAI TCLVAENAGG VDSVEEMSPA FVESQIDCCI RDIPCHVVKT GMLGSPEIVK
     AVARSAKKFN FSKLVVDPVM VATSGDSLVT KDIVSVLNEE LLPLTYLVTP NIPEAIVLAK
     NQGLDISNIN SVSDMERCAA VIHKLGPKHV LLKGGHMPVN NLGLKSSDDE DLRVVDILYD
     GNRFYHFSSS YLKKGEVHGT GCTLSSAIAS FLAWEHSLTE AVQFGIDYVH GAITHSPPIN
     NCSTNILNHM TRLRIVPFAP GHFIEYILSH PQVVPAWKEY INHKFTNMLA KGTLPLPAFQ
     DYLKQDYLYL VNFARAYSLK GYKENTFPNI LEAAQSVIHV IEEKELHVSM CSSYGVSLQD
     LKSCEESPAC TAYSRYILDT GAAQDVAALD FVQAPCLIGY YVIAARLMKE PFRNPQGPYQ
     KWVDNYFCED YLSAVRRGCR QIEEIVLKLS PERIQELIEI FIRATKFETL FWETPYYEYV
     TKQNLEDKEF S
//