PDXK_DICDI
ID PDXK_DICDI Reviewed; 302 AA.
AC Q55EK9; Q9GV94;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Pyridoxal kinase {ECO:0000303|PubMed:10930737};
DE EC=2.7.1.35 {ECO:0000269|PubMed:10930737};
DE AltName: Full=Pyridoxine kinase;
GN Name=pykA; ORFNames=DDB_G0268628;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=AX2;
RX PubMed=10930737; DOI=10.1111/j.1574-6968.2000.tb09229.x;
RA Guo K., Newell P.C.;
RT "Pyridoxal kinase knockout of Dictyostelium complemented by the human
RT homologue.";
RL FEMS Microbiol. Lett. 189:195-200(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Required for synthesis of pyridoxal-5-phosphate from vitamin
CC B6. {ECO:0000269|PubMed:10930737}.
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; Evidence={ECO:0000269|PubMed:10930737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225;
CC Evidence={ECO:0000269|PubMed:10930737};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.7 uM for pyridoxal (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:10930737};
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxal: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. {ECO:0000305}.
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DR EMBL; AF136753; AAG01573.1; -; Genomic_DNA.
DR EMBL; AAFI02000004; EAL72903.1; -; Genomic_DNA.
DR RefSeq; XP_647011.1; XM_641919.1.
DR AlphaFoldDB; Q55EK9; -.
DR SMR; Q55EK9; -.
DR STRING; 44689.DDB0191114; -.
DR PaxDb; Q55EK9; -.
DR EnsemblProtists; EAL72903; EAL72903; DDB_G0268628.
DR GeneID; 8616704; -.
DR KEGG; ddi:DDB_G0268628; -.
DR dictyBase; DDB_G0268628; pykA.
DR eggNOG; KOG2599; Eukaryota.
DR HOGENOM; CLU_046496_1_1_1; -.
DR InParanoid; Q55EK9; -.
DR OMA; CPNQLEL; -.
DR PhylomeDB; Q55EK9; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-964975; Vitamins B6 activation to pyridoxal phosphate.
DR SABIO-RK; Q55EK9; -.
DR UniPathway; UPA01068; UER00298.
DR PRO; PR:Q55EK9; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IDA:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IBA:GO_Central.
DR GO; GO:0042816; P:vitamin B6 metabolic process; IC:dictyBase.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..302
FT /note="Pyridoxal kinase"
FT /id="PRO_0000327815"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 215..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 5
FT /note="V -> L (in Ref. 1; AAG01573)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="Missing (in Ref. 1; AAG01573)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="E -> V (in Ref. 1; AAG01573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 34319 MW; 9D862C51E6627865 CRC64;
MEPKVLSIQS WVCHGYVGNK CAVFALQHLG IEVDPINSVH LSNNTAYPTW KGESLTPNKL
GDLFQGLEDN HLTSNYTHVL TGYNNSVQTL HTVLKIVKKL KSENPNLIYV CDPVLGDNNE
LYVPEDLVEV YKNEVIPNAD YIFPNQTEVE FLTGIKIKND QDALKAIDQF HKMGVKNVVI
TSLFFDTNPN DIIVIGSTIN DDDNNNKYNQ FKIKVGPKFN DYYTGTGDLL SSLLLGWSIR
EPTDLSLVCE KAISILYNII NETHNSKKSI PSNKEKQYYE LRLVQSRKFI ENSEIRFKSE
KL
