THI21_SCHPO
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 03-AUG-2022, entry version 112.
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}.
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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; 4896.SPBP8B7.17c.1; -.
DR MaxQB; O94265; -.
DR PaxDb; O94265; -.
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; 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; 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
