THI22_SCHPO
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 03-AUG-2022, entry version 115.
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}.
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; 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; 4896.SPBP8B7.18c.1; -.
DR iPTMnet; O94266; -.
DR MaxQB; O94266; -.
DR PaxDb; O94266; -.
DR PRIDE; O94266; -.
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 Gene3D; 1.20.910.10; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
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 InterPro; IPR004305; Thiaminase-2/PQQC.
DR PANTHER; PTHR20858; PTHR20858; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00097; HMP-P_kinase; 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
