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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)DescriptionActionsGraphical viewLength
    Metal bindingi156Zinc1
    Metal bindingi166Zinc1
    Metal bindingi168Zinc1
    Metal bindingi173Zinc1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi5 – 12ATPSequence analysis8
    Nucleotide bindingi132 – 139ATPSequence analysis8

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12815. nanK.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi84L → P: 12-fold increase in catalytic efficiency for glucose phosphorylation. 2-fold decrease in catalytic efficiency for N-acetylmannosamine phosphorylation. 1 Publication1
    Mutagenesisi138V → M: 6-fold increase in catalytic efficiency for glucose phosphorylation. No change in catalytic efficiency for N-acetylmannosamine phosphorylation. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000956951 – 291N-acetylmannosamine kinaseAdd BLAST291

    Proteomic databases

    PaxDbiP45425.
    PRIDEiP45425.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4261227. 316 interactors.
    DIPiDIP-12282N.
    IntActiP45425. 1 interactor.
    STRINGi511145.b3222.

    Structurei

    Secondary structure

    1291
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 8Combined sources6
    Beta strandi10 – 18Combined sources9
    Beta strandi24 – 31Combined sources8
    Helixi38 – 49Combined sources12
    Turni50 – 52Combined sources3
    Helixi53 – 55Combined sources3
    Beta strandi57 – 68Combined sources12
    Beta strandi71 – 73Combined sources3
    Helixi77 – 83Combined sources7
    Helixi88 – 96Combined sources9
    Beta strandi100 – 104Combined sources5
    Helixi105 – 115Combined sources11
    Beta strandi124 – 139Combined sources16
    Beta strandi142 – 144Combined sources3
    Helixi154 – 156Combined sources3
    Beta strandi157 – 159Combined sources3
    Beta strandi171 – 173Combined sources3
    Helixi174 – 178Combined sources5
    Helixi180 – 185Combined sources6
    Helixi189 – 191Combined sources3
    Helixi196 – 204Combined sources9
    Helixi208 – 232Combined sources25
    Beta strandi235 – 240Combined sources6
    Helixi241 – 244Combined sources4
    Helixi249 – 257Combined sources9
    Helixi262 – 264Combined sources3
    Beta strandi267 – 270Combined sources4
    Helixi277 – 287Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2AA4X-ray2.20A/B1-289[»]
    ProteinModelPortaliP45425.
    SMRiP45425.
    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.
    OMAiYRAGDTH.
    PhylomeDBiP45425.

    Family and domain databases

    HAMAPiMF_01234. ManNAc_kinase. 1 hit.
    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 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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2AA4X-ray2.20A/B1-289[»]
    ProteinModelPortaliP45425.
    SMRiP45425.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261227. 316 interactors.
    DIPiDIP-12282N.
    IntActiP45425. 1 interactor.
    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.
    OMAiYRAGDTH.
    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. 1 hit.
    InterProiIPR023945. ManNAc_kinase_bac.
    IPR000600. ROK.
    [Graphical view]
    PfamiPF00480. ROK. 1 hit.
    [Graphical view]
    PROSITEiPS01125. ROK. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 117 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.