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Protein

D-allose kinase

Gene

alsK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of D-allose to D-allose 6-phosphate. Has also low level glucokinase activity in vitro.UniRule annotation2 Publications

Catalytic activityi

ATP + D-allose = ADP + D-allose 6-phosphate.UniRule annotation1 Publication

Kineticsi

Catalytic efficiency with D-allose as substrate is 735-fold higher than that with D-glucose.

  1. KM=0.19 mM for D-allose (at 25 degrees Celsius and pH 7.6)1 Publication
  2. KM=0.27 mM for ATP (at 25 degrees Celsius and pH 7.6)1 Publication
  3. KM=29 mM for D-glucose (at 25 degrees Celsius and pH 7.6)1 Publication
  4. KM=210 mM for D-altrose (at 25 degrees Celsius and pH 7.6)1 Publication
  5. KM=380 mM for 2'-deoxy-D-glucose (at 25 degrees Celsius and pH 7.6)1 Publication
  6. KM=390 mM for D-mannose (at 25 degrees Celsius and pH 7.6)1 Publication

    Pathwayi: D-allose degradation

    This protein is involved in the pathway D-allose degradation, which is part of Carbohydrate degradation.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway D-allose degradation and in Carbohydrate degradation.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 178ATPUniRule annotation
    Nucleotide bindingi142 – 1498ATPUniRule annotation

    GO - Molecular functioni

    • allose kinase activity Source: EcoCyc
    • ATP binding Source: UniProtKB-HAMAP
    • glucokinase activity Source: EcoCyc

    GO - Biological processi

    • carbohydrate phosphorylation Source: GOC
    • D-allose catabolic process Source: EcoCyc
    • glucose 6-phosphate metabolic process Source: GOC
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11956-MONOMER.
    ECOL316407:JW5724-MONOMER.
    MetaCyc:EG11956-MONOMER.
    SABIO-RKP32718.
    UniPathwayiUPA00361.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-allose kinaseUniRule annotation (EC:2.7.1.55UniRule annotation)
    Short name:
    AllokinaseUniRule annotation
    Gene namesi
    Name:alsKUniRule annotation
    Synonyms:yjcT
    Ordered Locus Names:b4084, JW5724
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11956. alsK.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731A → G: 60-fold increase in catalytic efficiency for glucose phosphorylation. 45-fold increase in D-glucose affinity. No change in catalytic efficiency for D-allose phosphorylation. 1 Publication
    Mutagenesisi145 – 1451F → L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309D-allose kinasePRO_0000095688Add
    BLAST

    Proteomic databases

    PaxDbiP32718.
    PRIDEiP32718.

    Interactioni

    Protein-protein interaction databases

    BioGridi4262956. 15 interactions.
    DIPiDIP-9097N.
    IntActiP32718. 2 interactions.
    STRINGi511145.b4084.

    Structurei

    Secondary structure

    1
    309
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139Combined sources
    Beta strandi15 – 2410Combined sources
    Beta strandi29 – 368Combined sources
    Helixi37 – 415Combined sources
    Helixi45 – 6016Combined sources
    Beta strandi62 – 7312Combined sources
    Beta strandi87 – 893Combined sources
    Helixi92 – 954Combined sources
    Helixi98 – 1069Combined sources
    Beta strandi110 – 1145Combined sources
    Helixi115 – 12612Combined sources
    Beta strandi134 – 14916Combined sources
    Beta strandi152 – 1543Combined sources
    Beta strandi157 – 1593Combined sources
    Beta strandi187 – 1893Combined sources
    Helixi190 – 1978Combined sources
    Helixi206 – 2083Combined sources
    Helixi209 – 2135Combined sources
    Helixi217 – 23721Combined sources
    Beta strandi240 – 2456Combined sources
    Turni247 – 2504Combined sources
    Helixi256 – 26510Combined sources
    Turni269 – 2757Combined sources
    Beta strandi277 – 2804Combined sources
    Helixi287 – 30014Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HTVX-ray1.95A1-309[»]
    ProteinModelPortaliP32718.
    SMRiP32718. Positions 3-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32718.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ROK (NagC/XylR) family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4107TFG. Bacteria.
    COG1940. LUCA.
    HOGENOMiHOG000126964.
    InParanoidiP32718.
    KOiK00881.
    OMAiQSCAKAP.
    OrthoDBiEOG622PS4.
    PhylomeDBiP32718.

    Family and domain databases

    HAMAPiMF_00988. Allose_kinase.
    InterProiIPR030883. AlsK.
    IPR000600. ROK.
    [Graphical view]
    PfamiPF00480. ROK. 1 hit.
    [Graphical view]
    PROSITEiPS01125. ROK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32718-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQKQHNVVAG VDMGATHIRF CLRTAEGETL HCEKKRTAEV IAPGLVSGIG
    60 70 80 90 100
    EMIDEQLRRF NARCHGLVMG FPALVSKDKR TIISTPNLPL TAADLYDLAD
    110 120 130 140 150
    KLENTLNCPV EFSRDVNLQL SWDVVENRLT QQLVLAAYLG TGMGFAVWMN
    160 170 180 190 200
    GAPWTGAHGV AGELGHIPLG DMTQHCACGN PGCLETNCSG MALRRWYEQQ
    210 220 230 240 250
    PRNYPLRDLF VHAENAPFVQ SLLENAARAI ATSINLFDPD AVILGGGVMD
    260 270 280 290 300
    MPAFPRETLV AMTQKYLRRP LPHQVVRFIA ASSSDFNGAQ GAAILAHQRF

    LPQFCAKAP
    Length:309
    Mass (Da):33,821
    Last modified:October 1, 1993 - v1
    Checksum:i7C655FD2E5A8BF2E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti308 – 3092AP → EGANKRGNSSRLTQSFHFFM FEPIFSPVNALNQPI in BAE78087 (PubMed:16738553).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00006 Genomic DNA. Translation: AAC43178.1.
    U00096 Genomic DNA. Translation: AAC77045.1.
    AP009048 Genomic DNA. Translation: BAE78087.1.
    PIRiC65217.
    RefSeqiNP_418508.1. NC_000913.3.
    WP_001171687.1. NZ_CP014272.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77045; AAC77045; b4084.
    BAE78087; BAE78087; BAE78087.
    GeneIDi948596.
    KEGGiecj:JW5724.
    eco:b4084.
    PATRICi32123723. VBIEscCol129921_4210.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00006 Genomic DNA. Translation: AAC43178.1.
    U00096 Genomic DNA. Translation: AAC77045.1.
    AP009048 Genomic DNA. Translation: BAE78087.1.
    PIRiC65217.
    RefSeqiNP_418508.1. NC_000913.3.
    WP_001171687.1. NZ_CP014272.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HTVX-ray1.95A1-309[»]
    ProteinModelPortaliP32718.
    SMRiP32718. Positions 3-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262956. 15 interactions.
    DIPiDIP-9097N.
    IntActiP32718. 2 interactions.
    STRINGi511145.b4084.

    Proteomic databases

    PaxDbiP32718.
    PRIDEiP32718.

    Protocols and materials databases

    DNASUi948596.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC77045; AAC77045; b4084.
    BAE78087; BAE78087; BAE78087.
    GeneIDi948596.
    KEGGiecj:JW5724.
    eco:b4084.
    PATRICi32123723. VBIEscCol129921_4210.

    Organism-specific databases

    EchoBASEiEB1899.
    EcoGeneiEG11956. alsK.

    Phylogenomic databases

    eggNOGiENOG4107TFG. Bacteria.
    COG1940. LUCA.
    HOGENOMiHOG000126964.
    InParanoidiP32718.
    KOiK00881.
    OMAiQSCAKAP.
    OrthoDBiEOG622PS4.
    PhylomeDBiP32718.

    Enzyme and pathway databases

    UniPathwayiUPA00361.
    BioCyciEcoCyc:EG11956-MONOMER.
    ECOL316407:JW5724-MONOMER.
    MetaCyc:EG11956-MONOMER.
    SABIO-RKP32718.

    Miscellaneous databases

    EvolutionaryTraceiP32718.
    PROiP32718.

    Family and domain databases

    HAMAPiMF_00988. Allose_kinase.
    InterProiIPR030883. AlsK.
    IPR000600. ROK.
    [Graphical view]
    PfamiPF00480. ROK. 1 hit.
    [Graphical view]
    PROSITEiPS01125. ROK. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "The D-allose operon of Escherichia coli K-12."
      Kim C., Song S., Park C.
      J. Bacteriol. 179:7631-7637(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: K12.
    5. "Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity."
      Larion M., Moore L.B., Thompson S.M., Miller B.G.
      Biochemistry 46:13564-13572(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, MUTAGENESIS OF ALA-73 AND PHE-145.
    6. "Crystal structure of D-allose kinase (NP_418508.1) from Escherichia coli K12 at 1.95 A resolution."
      Joint Center for Structural Genomics (JCSG)
      Submitted (JUN-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).

    Entry informationi

    Entry nameiALSK_ECOLI
    AccessioniPrimary (citable) accession number: P32718
    Secondary accession number(s): Q2M6L9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: May 11, 2016
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    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.