ID THI21_SCHPO Reviewed; 506 AA. AC O94265; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 1; DE EC=2.7.1.49 {ECO:0000250|UniProtKB:Q08224}; DE EC=2.7.4.7 {ECO:0000250|UniProtKB:Q08224}; DE AltName: Full=Hydroxymethylpyrimidine kinase 1; DE Short=HMP kinase 1; DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase 1; DE Short=HMP-P kinase 1; DE Short=HMP-phosphate kinase 1; DE Short=HMPP kinase 1; GN ORFNames=SPBP8B7.17c; 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:Q08224}. 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:Q08224}; 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:Q08224}; 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}. Nucleus CC {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}. 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; CU329671; CAA21802.1; -; Genomic_DNA. DR PIR; T40811; T40811. DR RefSeq; NP_596524.1; NM_001022445.2. DR AlphaFoldDB; O94265; -. DR SMR; O94265; -. DR BioGRID; 276740; 3. DR STRING; 284812.O94265; -. DR MaxQB; O94265; -. DR PaxDb; 4896-SPBP8B7-17c-1; -. DR EnsemblFungi; SPBP8B7.17c.1; SPBP8B7.17c.1:pep; SPBP8B7.17c. DR GeneID; 2540207; -. DR KEGG; spo:SPBP8B7.17c; -. DR PomBase; SPBP8B7.17c; -. DR VEuPathDB; FungiDB:SPBP8B7.17c; -. DR eggNOG; KOG2598; Eukaryota. DR HOGENOM; CLU_020520_2_1_1; -. DR InParanoid; O94265; -. DR OMA; AHSVYGM; -. DR PhylomeDB; O94265; -. DR UniPathway; UPA00060; UER00137. DR UniPathway; UPA00060; UER00138. DR PRO; PR:O94265; -. DR Proteomes; UP000002485; Chromosome II. DR GO; GO:0005737; C:cytoplasm; HDA:PomBase. DR GO; GO:0005829; C:cytosol; HDA:PomBase. DR GO; GO:0005634; C:nucleus; 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 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:SF22; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE 1-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; Nucleus; KW Reference proteome; Thiamine biosynthesis; Transferase. FT CHAIN 1..506 FT /note="Putative FT hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 1" FT /id="PRO_0000315972" FT BINDING 43 FT /ligand="4-amino-5-hydroxymethyl-2-methylpyrimidine" FT /ligand_id="ChEBI:CHEBI:16892" FT /evidence="ECO:0000250" SQ SEQUENCE 506 AA; 55754 MW; 139A034F41CF4482 CRC64; MISTCITVAG SDCSGGAGVQ ADLKVFTAHS VYGMSAVTAI TSQNTIGVNG VHLIPASYVE QQISACLLDV HCEVMKTGML FNQQILKVIV ESIDRFKIKK VVVDPLIATR KGALLVMPDY LELFVKELIP RAEVLIPNIA EALIILKHMT NEFVEIHHLE DVKAVGKKLI KAGCKNVVIR CDDIPFASDF FCSRETNMPP TWYLYVLCTS EGEVLLPQKW LASKTARGTS CALSSAVASN LAIGLDLVTA TQNAVSYTQR ALEMSFHLGR GANSLDYASA LTRLPYEKGE FINFVRYHPS ITPKWLSIVN HPFVEQLKAG TLSRLPFQKY LVLKYHMLIN NAQAAGMMAF SSSSISAIEH SAKIIQAIKE ENVTHLRICE QYGLSASQIT KSKPEIVKSH SLFIHDTAQQ DGLRGIQIAM LPFVFMIQEV VSQISASDGY PYVAWVEHCK DKSATSHIET LLESLETNSQ IISLSKVQHL LGILEKSLDF ERLVLDTSSS NESSVF //