BUD16_YEAST
ID BUD16_YEAST Reviewed; 312 AA.
AC P39988; D3DLM0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Putative pyridoxal kinase BUD16;
DE EC=2.7.1.35;
DE AltName: Full=Bud site selection protein 16;
GN Name=BUD16; OrderedLocusNames=YEL029C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=11452010; DOI=10.1091/mbc.12.7.2147;
RA Ni L., Snyder M.;
RT "A genomic study of the bipolar bud site selection pattern in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 12:2147-2170(2001).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
CC -!- FUNCTION: Required for synthesis of pyridoxal-5-phosphate from vitamin
CC B6 (By similarity). Important for bud site selection. {ECO:0000250,
CC ECO:0000269|PubMed:11452010}.
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 {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase 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; U18530; AAB64506.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07624.1; -; Genomic_DNA.
DR PIR; S50430; S50430.
DR RefSeq; NP_010885.1; NM_001178844.1.
DR AlphaFoldDB; P39988; -.
DR SMR; P39988; -.
DR BioGRID; 36700; 80.
DR IntAct; P39988; 2.
DR STRING; 4932.YEL029C; -.
DR MaxQB; P39988; -.
DR PaxDb; P39988; -.
DR PRIDE; P39988; -.
DR EnsemblFungi; YEL029C_mRNA; YEL029C; YEL029C.
DR GeneID; 856683; -.
DR KEGG; sce:YEL029C; -.
DR SGD; S000000755; BUD16.
DR VEuPathDB; FungiDB:YEL029C; -.
DR eggNOG; KOG2599; Eukaryota.
DR GeneTree; ENSGT00390000003874; -.
DR HOGENOM; CLU_046496_1_0_1; -.
DR InParanoid; P39988; -.
DR OMA; CPNQLEL; -.
DR BioCyc; MetaCyc:MON3O-37; -.
DR BioCyc; YEAST:MON3O-37; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-964975; Vitamins B6 activation to pyridoxal phosphate.
DR PRO; PR:P39988; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39988; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; ISA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IBA:GO_Central.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IMP:SGD.
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; Cell cycle; Cytoplasm; Kinase; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Transferase; Zinc.
FT CHAIN 1..312
FT /note="Putative pyridoxal kinase BUD16"
FT /id="PRO_0000213348"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 211..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 312 AA; 35559 MW; 0A6C10767DE34073 CRC64;
MPRLLATQSH VVHGYVGNKA ATFPLQCLGW DVDCCNSVQF SNHTGYGLDK VFGTITRETD
LKELLSGLFD NFSQDYQALL SGYLPNKNSV RCMGTYYAKF KEANPEMIWL MDPVMGDEGQ
LYVSEDVIPE YRKLALSPKQ LVDIITPNQF ELEILYGGEI KTKEHLKKAL KKLHQTIPVI
IVTSCDCKMF DDKDFIYCVA SMEGKTPIVY RVPFIDSYFT GVGDLFSALL LDRVYKILSN
PTTTLKFEDQ VNNVLNVIQK VLKITRSYAS GKMKAKMGSA LEMKEMELRL IESRDIYETI
NIHQTDYIYA RL
