Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8W1X2

- PDXK_ARATH

UniProt

Q8W1X2 - PDXK_ARATH

Protein

Pyridoxal kinase

Gene

PK

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (06 Dec 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the transfer of a phosphate group from ATP to the 5-hydroxylmethyl group of pyridoxal to form the biologically active pyridoxal phosphate.1 Publication

    Catalytic activityi

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

    Cofactori

    Divalent cations. Zinc >> cobalt > magnesium > manganese > calcium.

    Kineticsi

    1. KM=98 µM for ATP
    2. KM=688 µM for pyridoxal

    Vmax=1.604 mmol/min/mg enzyme

    pH dependencei

    Optimum pH is 6.0. Active from pH 4.5 to 10.5.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei23 – 231SubstrateBy similarity
    Binding sitei58 – 581SubstrateBy similarity
    Binding sitei134 – 1341SubstrateBy similarity
    Binding sitei234 – 2341SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi193 – 1942ATPBy similarity
    Nucleotide bindingi221 – 23313ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. pyridoxal kinase activity Source: TAIR

    GO - Biological processi

    1. hyperosmotic salinity response Source: TAIR
    2. phosphorylation Source: GOC
    3. pyridoxal 5'-phosphate salvage Source: TAIR
    4. pyridoxine biosynthetic process Source: TAIR
    5. trichoblast differentiation Source: TAIR

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Pyridoxal phosphate, Zinc

    Enzyme and pathway databases

    BioCyciARA:GQT-1103-MONOMER.
    ARA:GQT-2581-MONOMER.
    ReactomeiREACT_187833. Vitamins B6 activation to pyridoxal phosphate.
    UniPathwayiUPA00190; UER00298.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyridoxal kinase (EC:2.7.1.35)
    Alternative name(s):
    Protein SALT OVERLY SENSITIVE 4
    Pyridoxal kinase-like protein SOS4
    Pyridoxine kinase
    Gene namesi
    Name:PK
    Synonyms:PDXK, SOS4
    Ordered Locus Names:At5g37850
    ORF Names:K18L3_10
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G37850.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309Pyridoxal kinasePRO_0000213341Add
    BLAST

    Proteomic databases

    PaxDbiQ8W1X2.
    PRIDEiQ8W1X2.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously in leaves, stems, roots, flowers and siliques.

    Developmental stagei

    Becomes detectable 60 hours after imbibition of the seeds and remains constant up to 101 hours after imbibition.

    Inductioni

    Both long and short transcripts are down-regulated in roots but not in shoots by NaCl and abscisic acid treatment. Under cold stress, the expression of the short transcript is increased while the long one becomes undetectable.

    Gene expression databases

    GenevestigatoriQ8W1X2.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi19014. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8W1X2.
    SMRiQ8W1X2. Positions 17-305.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pyridoxine kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG2240.
    HOGENOMiHOG000258174.
    InParanoidiQ8W1X2.
    KOiK00868.
    OMAiHVIKRTI.
    PhylomeDBiQ8W1X2.

    Family and domain databases

    Gene3Di3.40.1190.20. 1 hit.
    InterProiIPR013749. PM/HMP-P_kinase-1.
    IPR004625. PyrdxlP_synth_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.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8W1X2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTTPPVLSLA LPSDTGRVLS IQSHTVQGYV GNKSAVFPLQ LLGYDVDPIN    50
    SVQFSNHTGY PTFKGQVLNG QQLCDLIEGL EANDLLFYTH VLTGYIGSVS 100
    FLDTILEVIN KLRSVNPNLT YVCDPVMGDE GKLYVPEELV HVYREKVVPL 150
    ASMLTPNQFE AEKLTGLRIN SEEDGREACA ILHAAGPSKV VITSITIGGI 200
    LLLIGSHQKE KGLKPEQFKI LIHKIPAYFT GTGDLMTALL LGWSNKYPDN 250
    LDKAAELAVS TLQALLRRTL DDYKRAGYDP TSSSLEIRLI QSQEDIRNPK 300
    VELKAERYS 309
    Length:309
    Mass (Da):34,043
    Last modified:December 6, 2002 - v2
    Checksum:i3630575692F2B271
    GO
    Isoform 2 (identifier: Q8W1X2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MPFSFPTTTTTSLPFHKDHNHFNLNRNLRSRNRRM

    Note: No experimental confirmation available.

    Show »
    Length:343
    Mass (Da):38,167
    Checksum:i58DFE7EF6334C178
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MPFSFPTTTTTSLPFHKDHN HFNLNRNLRSRNRRM in isoform 2. CuratedVSP_004654

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF404865 mRNA. Translation: AAL57364.2.
    AF400125 Genomic DNA. Translation: AAK94020.1.
    AF400125 Genomic DNA. Translation: AAK94021.1.
    AB012241 Genomic DNA. Translation: BAB09031.1.
    CP002688 Genomic DNA. Translation: AED94239.1.
    CP002688 Genomic DNA. Translation: AED94240.1.
    AY136333 mRNA. Translation: AAM96999.1.
    BT008815 mRNA. Translation: AAP68254.1.
    AY084419 mRNA. Translation: AAM60993.1.
    RefSeqiNP_001078677.1. NM_001085208.1. [Q8W1X2-1]
    NP_198601.2. NM_123144.3. [Q8W1X2-2]
    UniGeneiAt.28304.

    Genome annotation databases

    EnsemblPlantsiAT5G37850.1; AT5G37850.1; AT5G37850. [Q8W1X2-2]
    AT5G37850.2; AT5G37850.2; AT5G37850. [Q8W1X2-1]
    GeneIDi833763.
    KEGGiath:AT5G37850.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF404865 mRNA. Translation: AAL57364.2 .
    AF400125 Genomic DNA. Translation: AAK94020.1 .
    AF400125 Genomic DNA. Translation: AAK94021.1 .
    AB012241 Genomic DNA. Translation: BAB09031.1 .
    CP002688 Genomic DNA. Translation: AED94239.1 .
    CP002688 Genomic DNA. Translation: AED94240.1 .
    AY136333 mRNA. Translation: AAM96999.1 .
    BT008815 mRNA. Translation: AAP68254.1 .
    AY084419 mRNA. Translation: AAM60993.1 .
    RefSeqi NP_001078677.1. NM_001085208.1. [Q8W1X2-1 ]
    NP_198601.2. NM_123144.3. [Q8W1X2-2 ]
    UniGenei At.28304.

    3D structure databases

    ProteinModelPortali Q8W1X2.
    SMRi Q8W1X2. Positions 17-305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 19014. 1 interaction.

    Proteomic databases

    PaxDbi Q8W1X2.
    PRIDEi Q8W1X2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G37850.1 ; AT5G37850.1 ; AT5G37850 . [Q8W1X2-2 ]
    AT5G37850.2 ; AT5G37850.2 ; AT5G37850 . [Q8W1X2-1 ]
    GeneIDi 833763.
    KEGGi ath:AT5G37850.

    Organism-specific databases

    TAIRi AT5G37850.

    Phylogenomic databases

    eggNOGi COG2240.
    HOGENOMi HOG000258174.
    InParanoidi Q8W1X2.
    KOi K00868.
    OMAi HVIKRTI.
    PhylomeDBi Q8W1X2.

    Enzyme and pathway databases

    UniPathwayi UPA00190 ; UER00298 .
    BioCyci ARA:GQT-1103-MONOMER.
    ARA:GQT-2581-MONOMER.
    Reactomei REACT_187833. Vitamins B6 activation to pyridoxal phosphate.

    Miscellaneous databases

    PROi Q8W1X2.

    Gene expression databases

    Genevestigatori Q8W1X2.

    Family and domain databases

    Gene3Di 3.40.1190.20. 1 hit.
    InterProi IPR013749. PM/HMP-P_kinase-1.
    IPR004625. PyrdxlP_synth_PyrdxlKinase.
    IPR029056. Ribokinase-like.
    [Graphical view ]
    PANTHERi PTHR10534. PTHR10534. 1 hit.
    Pfami PF08543. Phos_pyr_kin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53613. SSF53613. 1 hit.
    TIGRFAMsi TIGR00687. pyridox_kin. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of Arabidopsis thaliana pyridoxal kinase."
      Lum H.-K., Kwok F., Lo S.C.L.
      Planta 215:870-879(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 1-12.
      Strain: cv. Columbia.
    2. "The Arabidopsis salt overly sensitive 4 mutants uncover a critical role for vitamin B6 in plant salt tolerance."
      Shi H., Xiong L., Stevenson B., Lu T., Zhu J.-K.
      Plant Cell 14:575-588(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
      Strain: cv. Columbia.
    3. "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
      Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
      DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    6. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "SOS4, a pyridoxal kinase gene, is required for root hair development in Arabidopsis."
      Shi H., Zhu J.-K.
      Plant Physiol. 129:585-593(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiPDXK_ARATH
    AccessioniPrimary (citable) accession number: Q8W1X2
    Secondary accession number(s): Q94EN4, Q9FKE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2002
    Last sequence update: December 6, 2002
    Last modified: October 1, 2014
    This is version 103 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Defective pyridoxal kinase results in both salt hypersensitive and root hairless phenotypes.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3