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Protein

Putative pyridoxal kinase BUD16

Gene

BUD16

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection.By similarity1 Publication

Catalytic activityi

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei9SubstrateBy similarity1
Binding sitei44SubstrateBy similarity1
Binding sitei122SubstrateBy similarity1
Binding sitei224SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi183 – 184ATPBy similarity2
Nucleotide bindingi211 – 223ATPBy similarityAdd BLAST13

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • pyridoxal 5'-phosphate salvage Source: GO_Central
  • pyridoxal phosphate biosynthetic process Source: SGD
  • vitamin B6 metabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-37.
YEAST:MONOMER3O-37.
ReactomeiR-SCE-6798695. Neutrophil degranulation.
R-SCE-964975. Vitamins B6 activation to pyridoxal phosphate.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative pyridoxal kinase BUD16 (EC:2.7.1.35)
Alternative name(s):
Bud site selection protein 16
Gene namesi
Name:BUD16
Ordered Locus Names:YEL029C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL029C.
SGDiS000000755. BUD16.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002133481 – 312Putative pyridoxal kinase BUD16Add BLAST312

Proteomic databases

MaxQBiP39988.
PRIDEiP39988.

Interactioni

Protein-protein interaction databases

BioGridi36700. 20 interactors.
IntActiP39988. 2 interactors.
MINTiMINT-4483389.

Structurei

3D structure databases

ProteinModelPortaliP39988.
SMRiP39988.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyridoxine kinase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000003874.
HOGENOMiHOG000258174.
InParanoidiP39988.
KOiK00868.
OMAiSTPMAMV.
OrthoDBiEOG092C42OZ.

Family and domain databases

CDDicd01173. pyridoxal_pyridoxamine_kinase. 1 hit.
Gene3Di3.40.1190.20. 1 hit.
InterProiIPR013749. PM/HMP-P_kinase-1.
IPR004625. PyrdxlKinase.
IPR029056. Ribokinase-like.
[Graphical view]
PANTHERiPTHR10534. PTHR10534. 1 hit.
PfamiPF08543. Phos_pyr_kin. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00687. pyridox_kin. 1 hit.

Sequencei

Sequence statusi: Complete.

P39988-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRLLATQSH VVHGYVGNKA ATFPLQCLGW DVDCCNSVQF SNHTGYGLDK
60 70 80 90 100
VFGTITRETD LKELLSGLFD NFSQDYQALL SGYLPNKNSV RCMGTYYAKF
110 120 130 140 150
KEANPEMIWL MDPVMGDEGQ LYVSEDVIPE YRKLALSPKQ LVDIITPNQF
160 170 180 190 200
ELEILYGGEI KTKEHLKKAL KKLHQTIPVI IVTSCDCKMF DDKDFIYCVA
210 220 230 240 250
SMEGKTPIVY RVPFIDSYFT GVGDLFSALL LDRVYKILSN PTTTLKFEDQ
260 270 280 290 300
VNNVLNVIQK VLKITRSYAS GKMKAKMGSA LEMKEMELRL IESRDIYETI
310
NIHQTDYIYA RL
Length:312
Mass (Da):35,559
Last modified:February 1, 1995 - v1
Checksum:i0A6C10767DE34073
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18530 Genomic DNA. Translation: AAB64506.1.
BK006939 Genomic DNA. Translation: DAA07624.1.
PIRiS50430.
RefSeqiNP_010885.1. NM_001178844.1.

Genome annotation databases

EnsemblFungiiYEL029C; YEL029C; YEL029C.
GeneIDi856683.
KEGGisce:YEL029C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18530 Genomic DNA. Translation: AAB64506.1.
BK006939 Genomic DNA. Translation: DAA07624.1.
PIRiS50430.
RefSeqiNP_010885.1. NM_001178844.1.

3D structure databases

ProteinModelPortaliP39988.
SMRiP39988.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36700. 20 interactors.
IntActiP39988. 2 interactors.
MINTiMINT-4483389.

Proteomic databases

MaxQBiP39988.
PRIDEiP39988.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL029C; YEL029C; YEL029C.
GeneIDi856683.
KEGGisce:YEL029C.

Organism-specific databases

EuPathDBiFungiDB:YEL029C.
SGDiS000000755. BUD16.

Phylogenomic databases

GeneTreeiENSGT00390000003874.
HOGENOMiHOG000258174.
InParanoidiP39988.
KOiK00868.
OMAiSTPMAMV.
OrthoDBiEOG092C42OZ.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-37.
YEAST:MONOMER3O-37.
ReactomeiR-SCE-6798695. Neutrophil degranulation.
R-SCE-964975. Vitamins B6 activation to pyridoxal phosphate.

Miscellaneous databases

PROiP39988.

Family and domain databases

CDDicd01173. pyridoxal_pyridoxamine_kinase. 1 hit.
Gene3Di3.40.1190.20. 1 hit.
InterProiIPR013749. PM/HMP-P_kinase-1.
IPR004625. PyrdxlKinase.
IPR029056. Ribokinase-like.
[Graphical view]
PANTHERiPTHR10534. PTHR10534. 1 hit.
PfamiPF08543. Phos_pyr_kin. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00687. pyridox_kin. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBUD16_YEAST
AccessioniPrimary (citable) accession number: P39988
Secondary accession number(s): D3DLM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.