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Protein

N-acetylmannosamine kinase

Gene

nanK

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 N-acetylmannosamine (ManNAc) to ManNAc-6-P. Has also low level glucokinase activity in vitro.2 Publications

Catalytic activityi

ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate.

Kineticsi

Catalytic efficiency with N-acyl-D-mannosamine as substrate is 136-fold higher than that with D-glucose.

  1. KM=0.36 mM for N-acyl-D-mannosamine (at 25 degrees Celsius and pH 7.6)2 Publications
  2. KM=0.26 mM for ATP (at 25 degrees Celsius and pH 7.6)2 Publications
  3. KM=20 mM for D-glucose (at 25 degrees Celsius and pH 7.6)2 Publications
  4. KM=84 mM for D-mannose (at 25 degrees Celsius and pH 7.6)2 Publications

    Pathwayi: N-acetylneuraminate degradation

    This protein is involved in step 2 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. N-acetylneuraminate lyase (nanA)
    2. N-acetylmannosamine kinase (nanK)
    3. Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
    4. N-acetylglucosamine-6-phosphate deacetylase (nagA)
    5. Glucosamine-6-phosphate deaminase (nagB)
    This subpathway is part of the pathway N-acetylneuraminate degradation, which is itself part of Amino-sugar metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate, the pathway N-acetylneuraminate degradation and in Amino-sugar metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi156 – 1561Zinc
    Metal bindingi166 – 1661Zinc
    Metal bindingi168 – 1681Zinc
    Metal bindingi173 – 1731Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi5 – 128ATPSequence analysis
    Nucleotide bindingi132 – 1398ATPSequence analysis

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-HAMAP
    • N-acylmannosamine kinase activity Source: EcoCyc
    • zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    • cellular response to DNA damage stimulus Source: EcoliWiki
    • N-acetylmannosamine metabolic process Source: UniProtKB-HAMAP
    • N-acetylneuraminate catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciEcoCyc:NANK-MONOMER.
    ECOL316407:JW5538-MONOMER.
    MetaCyc:NANK-MONOMER.
    SABIO-RKP45425.
    UniPathwayiUPA00629; UER00681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylmannosamine kinase (EC:2.7.1.60)
    Alternative name(s):
    ManNAc kinase
    N-acetyl-D-mannosamine kinase
    Gene namesi
    Name:nanK
    Synonyms:yhcI
    Ordered Locus Names:b3222, JW5538
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12815. nanK.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi84 – 841L → P: 12-fold increase in catalytic efficiency for glucose phosphorylation. 2-fold decrease in catalytic efficiency for N-acetylmannosamine phosphorylation. 1 Publication
    Mutagenesisi138 – 1381V → M: 6-fold increase in catalytic efficiency for glucose phosphorylation. No change in catalytic efficiency for N-acetylmannosamine phosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 291291N-acetylmannosamine kinasePRO_0000095695Add
    BLAST

    Proteomic databases

    PaxDbiP45425.
    PRIDEiP45425.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4261227. 316 interactions.
    DIPiDIP-12282N.
    IntActiP45425. 1 interaction.
    STRINGi511145.b3222.

    Structurei

    Secondary structure

    1
    291
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86Combined sources
    Beta strandi10 – 189Combined sources
    Beta strandi24 – 318Combined sources
    Helixi38 – 4912Combined sources
    Turni50 – 523Combined sources
    Helixi53 – 553Combined sources
    Beta strandi57 – 6812Combined sources
    Beta strandi71 – 733Combined sources
    Helixi77 – 837Combined sources
    Helixi88 – 969Combined sources
    Beta strandi100 – 1045Combined sources
    Helixi105 – 11511Combined sources
    Beta strandi124 – 13916Combined sources
    Beta strandi142 – 1443Combined sources
    Helixi154 – 1563Combined sources
    Beta strandi157 – 1593Combined sources
    Beta strandi171 – 1733Combined sources
    Helixi174 – 1785Combined sources
    Helixi180 – 1856Combined sources
    Helixi189 – 1913Combined sources
    Helixi196 – 2049Combined sources
    Helixi208 – 23225Combined sources
    Beta strandi235 – 2406Combined sources
    Helixi241 – 2444Combined sources
    Helixi249 – 2579Combined sources
    Helixi262 – 2643Combined sources
    Beta strandi267 – 2704Combined sources
    Helixi277 – 28711Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AA4X-ray2.20A/B1-289[»]
    ProteinModelPortaliP45425.
    SMRiP45425. Positions 1-289.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45425.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ROK (NagC/XylR) family. NanK subfamily.Curated

    Phylogenomic databases

    eggNOGiENOG41061DF. Bacteria.
    COG1940. LUCA.
    HOGENOMiHOG000150087.
    InParanoidiP45425.
    KOiK00885.
    OMAiIASPNIF.
    OrthoDBiEOG618QQT.
    PhylomeDBiP45425.

    Family and domain databases

    HAMAPiMF_01234. ManNAc_kinase.
    InterProiIPR023945. ManNAc_kinase_bac.
    IPR000600. ROK.
    [Graphical view]
    PfamiPF00480. ROK. 1 hit.
    [Graphical view]
    PROSITEiPS01125. ROK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P45425-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTTLAIDIGG TKLAAALIGA DGQIRDRREL PTPASQTPEA LRDALSALVS
    60 70 80 90 100
    PLQAHAQRVA IASTGIIRDG SLLALNPHNL GGLLHFPLVK TLEQLTNLPT
    110 120 130 140 150
    IAINDAQAAA WAEFQALDGD ITDMVFITVS TGVGGGVVSG CKLLTGPGGL
    160 170 180 190 200
    AGHIGHTLAD PHGPVCGCGR TGCVEAIASG RGIAAAAQGE LAGADAKTIF
    210 220 230 240 250
    TRAGQGDEQA QQLIHRSART LARLIADIKA TTDCQCVVVG GSVGLAEGYL
    260 270 280 290
    ALVETYLAQE PAAFHVDLLA AHYRHDAGLL GAALLAQGEK L
    Length:291
    Mass (Da):29,644
    Last modified:December 15, 1998 - v2
    Checksum:iE3109E2756B08612
    GO

    Sequence cautioni

    The sequence AAA58024.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18997 Genomic DNA. Translation: AAA58024.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76254.2.
    AP009048 Genomic DNA. Translation: BAE77265.1.
    PIRiH65113.
    RefSeqiNP_417689.4. NC_000913.3.
    WP_000209011.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76254; AAC76254; b3222.
    BAE77265; BAE77265; BAE77265.
    GeneIDi947757.
    KEGGiecj:JW5538.
    eco:b3222.
    PATRICi32121868. VBIEscCol129921_3318.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18997 Genomic DNA. Translation: AAA58024.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC76254.2.
    AP009048 Genomic DNA. Translation: BAE77265.1.
    PIRiH65113.
    RefSeqiNP_417689.4. NC_000913.3.
    WP_000209011.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AA4X-ray2.20A/B1-289[»]
    ProteinModelPortaliP45425.
    SMRiP45425. Positions 1-289.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261227. 316 interactions.
    DIPiDIP-12282N.
    IntActiP45425. 1 interaction.
    STRINGi511145.b3222.

    Proteomic databases

    PaxDbiP45425.
    PRIDEiP45425.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76254; AAC76254; b3222.
    BAE77265; BAE77265; BAE77265.
    GeneIDi947757.
    KEGGiecj:JW5538.
    eco:b3222.
    PATRICi32121868. VBIEscCol129921_3318.

    Organism-specific databases

    EchoBASEiEB2666.
    EcoGeneiEG12815. nanK.

    Phylogenomic databases

    eggNOGiENOG41061DF. Bacteria.
    COG1940. LUCA.
    HOGENOMiHOG000150087.
    InParanoidiP45425.
    KOiK00885.
    OMAiIASPNIF.
    OrthoDBiEOG618QQT.
    PhylomeDBiP45425.

    Enzyme and pathway databases

    UniPathwayiUPA00629; UER00681.
    BioCyciEcoCyc:NANK-MONOMER.
    ECOL316407:JW5538-MONOMER.
    MetaCyc:NANK-MONOMER.
    SABIO-RKP45425.

    Miscellaneous databases

    EvolutionaryTraceiP45425.
    PROiP45425.

    Family and domain databases

    HAMAPiMF_01234. ManNAc_kinase.
    InterProiIPR023945. ManNAc_kinase_bac.
    IPR000600. ROK.
    [Graphical view]
    PfamiPF00480. ROK. 1 hit.
    [Graphical view]
    PROSITEiPS01125. ROK. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. "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.
    3. "Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli."
      Plumbridge J., Vimr E.
      J. Bacteriol. 181:47-54(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PUTATIVE FUNCTION.
    4. "Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases."
      Miller B.G., Raines R.T.
      Biochemistry 43:6387-6392(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, KINETIC PARAMETERS.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    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, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, MUTAGENESIS OF LEU-84 AND VAL-138.
    6. "Crystal structure of Escherichia coli putative N-acetylmannosamine kinase."
      New York structural genomics research consortium (NYSGRC)
      Submitted (JUL-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-289 IN COMPLEX WITH ZINC IONS, SUBUNIT.

    Entry informationi

    Entry nameiNANK_ECOLI
    AccessioniPrimary (citable) accession number: P45425
    Secondary accession number(s): Q2M8Z1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: December 15, 1998
    Last modified: July 6, 2016
    This is version 115 of the entry and version 2 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.