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YQ9A_SCHPO
ID   YQ9A_SCHPO              Reviewed;         340 AA.
AC   O74860;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Putative pyridoxal kinase C18.10;
DE            EC=2.7.1.35;
GN   ORFNames=SPCC18.10;
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).
CC   -!- FUNCTION: Required for synthesis of pyridoxal-5-phosphate from vitamin
CC       B6. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate;
CC         Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326;
CC         EC=2.7.1.35;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA21424.1; -; Genomic_DNA.
DR   PIR; T41153; T41153.
DR   RefSeq; NP_588389.1; NM_001023380.2.
DR   AlphaFoldDB; O74860; -.
DR   SMR; O74860; -.
DR   BioGRID; 275540; 96.
DR   STRING; 4896.SPCC18.10.1; -.
DR   MaxQB; O74860; -.
DR   PaxDb; O74860; -.
DR   EnsemblFungi; SPCC18.10.1; SPCC18.10.1:pep; SPCC18.10.
DR   GeneID; 2538966; -.
DR   KEGG; spo:SPCC18.10; -.
DR   PomBase; SPCC18.10; -.
DR   VEuPathDB; FungiDB:SPCC18.10; -.
DR   eggNOG; KOG2599; Eukaryota.
DR   HOGENOM; CLU_046496_1_0_1; -.
DR   InParanoid; O74860; -.
DR   OMA; ITYICDP; -.
DR   PhylomeDB; O74860; -.
DR   PRO; PR:O74860; -.
DR   Proteomes; UP000002485; Chromosome III.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008478; F:pyridoxal kinase activity; ISO:PomBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IBA:GO_Central.
DR   CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR004625; PyrdxlKinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR10534; PTHR10534; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Metal-binding; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN           1..340
FT                   /note="Putative pyridoxal kinase C18.10"
FT                   /id="PRO_0000339163"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         189..190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         218..230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  38080 MW;  A15393DEA7ABE7A0 CRC64;
     MTFPNVKFIG NKRVLSIQSS VSHGYVGNRS ATFPLQLHEW EVDVVPTVHF SNHLGYGATR
     GSACIPEEVH DLLNALLQDN GIVYDAILTG FVPNHDIIQV IFDCVLAYKK DHPKVLWLLD
     PVMGDQGKMY VDTNVISTYK AMIPHAFAIT PNAFEVEILT DIVIHTQMDA KRGLEKIYQL
     YGIQNAIITS FEVEESPGTL FCMGYSCEHG KPQLFLYQFP SLSGVFTGTG DLFSGLLLAK
     YREELDKRKH QQSDETKQTK RPTVLACAVG QVLSCMHTVL VNTKTYADEI LLEDPKIASD
     EFLLSNAREL RLIQSRTALL SKKSIYEAEF LPGFEEGEDV
 
 
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