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Protein

Maltose-6'-phosphate glucosidase

Gene

glvA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Hydrolyzes maltose-6'-phosphate and trehalose-6'-phosphate. Is involved in the catabolism of alpha-glycosides accumulated via a phosphoenolpyruvate-dependent maltose phosphotransferase system (PEP-PTS). Is also able to significantly catalyze the hydrolysis of both 6-phospho-alpha- and 6-phospho-beta-glucosides containing activated leaving groups such as p-nitrophenol and does so with retention and inversion, respectively, of the substrate anomeric configuration.

Miscellaneous

Reaction proceeds via a redox-elimination-addition mechanism consistent with an E1cb-type mechanism. This includes redox steps involving NAD+ and stabilization of intermediates by Mn2+.
Because it hydrolyzes 6-phospho-alpha-glucopyranosides without activated leaving groups (such as maltose-6'-phosphate) but not glycosidic linkage of naturally occurring phospho-beta-glucosides such as cellobiose-6'-phosphate nor methyl 6-phospho-beta-D-glucopyranoside, GlvA is certainly more appropriately classified as a 6-phospho-alpha-glucosidase than as a 6-phospho-beta-glucosidase. The ability to hydrolyze beta-glycosidic linkages is exceptional and applies only to activated 6-phospho-beta-D-glucopyranosides.

Catalytic activityi

Alpha-maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-phosphate.

Cofactori

Protein has several cofactor binding sites:
  • Mn2+1 Publication, Fe2+1 Publication, Co2+1 Publication, Ni2+1 PublicationNote: Binds 1 divalent metal cation per subunit. Manganese, iron, cobalt or nickel enhance activity.1 Publication
  • NAD+1 PublicationNote: Binds 1 NAD+ per subunit. Is only active with NAD+, not NADH.1 Publication

Activity regulationi

Cellobiose-6'-phosphate and 6-phospho-beta-D-glucopyranoside are not substrates but competitive inhibitors of GlvA.1 Publication

Kineticsi

  1. KM=400 µM for maltose-6'-phosphate (at pH 7.5 and 37 degrees Celsius)1 Publication
  2. KM=360 µM for maltose-6'-phosphate (at pH 8.4 and 37 degrees Celsius)1 Publication
  3. KM=610 µM for methyl 6-phospho-alpha-D-glucoside (at pH 7.5 and 37 degrees Celsius)1 Publication
  4. KM=69 µM for phenyl 6-phospho-alpha-D-glucoside (at pH 7.5 and 37 degrees Celsius)1 Publication
  5. KM=52 µM for 4-nitrophenyl 6-phospho-alpha-D-glucoside (at pH 7.5 and 37 degrees Celsius)1 Publication
  6. KM=12 µM for 3,4-dinitrophenyl 6-phospho-alpha-D-glucoside (at pH 7.5 and 37 degrees Celsius)1 Publication
  7. KM=2.9 µM for 3,4-dinitrophenyl 6-phospho-beta-D-glucoside (at pH 7.5 and 37 degrees Celsius)1 Publication
  8. KM=27 µM for 3,5-dichlorophenyl 6-phospho-beta-D-glucoside (at pH 7.5 and 37 degrees Celsius)1 Publication
  9. KM=34 µM for 3-nitrophenyl 6-phospho-beta-D-glucoside (at pH 7.5 and 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is about 7.6-8.4. Stable from pH 4.0 to 10.0.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei95Substrate1
    Sitei111Increases basicity of active site Tyr1
    Binding sitei149Substrate1
    Metal bindingi171Manganese1
    Active sitei172Proton donor1
    Metal bindingi202Manganese1
    Active sitei265Proton acceptor1
    Binding sitei285Substrate1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi6 – 72NADAdd BLAST67

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionGlycosidase, Hydrolase
    Biological processCarbohydrate metabolism
    LigandCobalt, Iron, Manganese, Metal-binding, NAD, Nickel

    Enzyme and pathway databases

    BioCyciBSUB:BSU08180-MONOMER
    BRENDAi3.2.1.122 658
    SABIO-RKiP54716

    Protein family/group databases

    CAZyiGH4 Glycoside Hydrolase Family 4

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Maltose-6'-phosphate glucosidase (EC:3.2.1.122)
    Alternative name(s):
    6-phospho-alpha-D-glucosidase
    6-phosphoryl-O-alpha-D-glucopyranosyl:phosphoglucohydrolase
    Gene namesi
    Name:glvA
    Synonyms:glv-1, glvG, malA
    Ordered Locus Names:BSU08180
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi41D → E or G: Loss of activity. 1 Publication1
    Mutagenesisi111E → D or G: Loss of activity. 1 Publication1
    Mutagenesisi359E → D or G: Loss of activity. 1 Publication1

    Chemistry databases

    DrugBankiDB02007 alpha-D-glucose 6-phosphate

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001698591 – 449Maltose-6'-phosphate glucosidaseAdd BLAST449

    Proteomic databases

    PaxDbiP54716
    PRIDEiP54716

    Expressioni

    Inductioni

    By maltose; repressed by glucose.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100004548

    Structurei

    Secondary structure

    1449
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP54716
    SMRiP54716
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54716

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 4 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105F8D Bacteria
    COG1486 LUCA
    HOGENOMiHOG000239810
    KOiK01232
    OMAiYMETYSP
    PhylomeDBiP54716

    Family and domain databases

    Gene3Di3.90.110.10, 1 hit
    InterProiView protein in InterPro
    IPR019802 GlycHydrolase_4_CS
    IPR001088 Glyco_hydro_4
    IPR022616 Glyco_hydro_4_C
    IPR015955 Lactate_DH/Glyco_Ohase_4_C
    IPR036291 NAD(P)-bd_dom_sf
    PANTHERiPTHR32092 PTHR32092, 1 hit
    PfamiView protein in Pfam
    PF02056 Glyco_hydro_4, 1 hit
    PF11975 Glyco_hydro_4C, 1 hit
    PRINTSiPR00732 GLHYDRLASE4
    SUPFAMiSSF51735 SSF51735, 1 hit
    SSF56327 SSF56327, 1 hit
    PROSITEiView protein in PROSITE
    PS01324 GLYCOSYL_HYDROL_F4, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P54716-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKKKSFSIVI AGGGSTFTPG IVLMLLDHLE EFPIRKLKLY DNDKERQDRI
    60 70 80 90 100
    AGACDVFIRE KAPDIEFAAT TDPEEAFTDV DFVMAHIRVG KYAMRALDEQ
    110 120 130 140 150
    IPLKYGVVGQ ETCGPGGIAY GMRSIGGVLE ILDYMEKYSP DAWMLNYSNP
    160 170 180 190 200
    AAIVAEATRR LRPNSKILNI CDMPVGIEDR MAQILGLSSR KEMKVRYYGL
    210 220 230 240 250
    NHFGWWTSIQ DQEGNDLMPK LKEHVSQYGY IPKTEAEAVE ASWNDTFAKA
    260 270 280 290 300
    RDVQAADPDT LPNTYLQYYL FPDDMVKKSN PNHTRANEVM EGREAFIFSQ
    310 320 330 340 350
    CDMITREQSS ENSEIKIDDH ASYIVDLARA IAYNTGERML LIVENNGAIA
    360 370 380 390 400
    NFDPTAMVEV PCIVGSNGPE PITVGTIPQF QKGLMEQQVS VEKLTVEAWA
    410 420 430 440
    EKSFQKLWQA LILSKTVPNA RVARLILEDL VEANKDFWPE LDQSPTRIS
    Length:449
    Mass (Da):50,514
    Last modified:October 1, 1996 - v1
    Checksum:iA903F7E41CFEF7AB
    GO

    Mass spectrometryi

    Molecular mass is 50510 Da from positions 1 - 449. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D50543 Genomic DNA Translation: BAA09103.1
    AL009126 Genomic DNA Translation: CAB12647.1
    PIRiF69635
    RefSeqiNP_388699.1, NC_000964.3
    WP_003244008.1, NZ_JNCM01000032.1

    Genome annotation databases

    EnsemblBacteriaiCAB12647; CAB12647; BSU08180
    GeneIDi936161
    KEGGibsu:BSU08180
    PATRICifig|224308.179.peg.884

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D50543 Genomic DNA Translation: BAA09103.1
    AL009126 Genomic DNA Translation: CAB12647.1
    PIRiF69635
    RefSeqiNP_388699.1, NC_000964.3
    WP_003244008.1, NZ_JNCM01000032.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1U8XX-ray2.05X1-449[»]
    ProteinModelPortaliP54716
    SMRiP54716
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100004548

    Chemistry databases

    DrugBankiDB02007 alpha-D-glucose 6-phosphate

    Protein family/group databases

    CAZyiGH4 Glycoside Hydrolase Family 4

    Proteomic databases

    PaxDbiP54716
    PRIDEiP54716

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB12647; CAB12647; BSU08180
    GeneIDi936161
    KEGGibsu:BSU08180
    PATRICifig|224308.179.peg.884

    Phylogenomic databases

    eggNOGiENOG4105F8D Bacteria
    COG1486 LUCA
    HOGENOMiHOG000239810
    KOiK01232
    OMAiYMETYSP
    PhylomeDBiP54716

    Enzyme and pathway databases

    BioCyciBSUB:BSU08180-MONOMER
    BRENDAi3.2.1.122 658
    SABIO-RKiP54716

    Miscellaneous databases

    EvolutionaryTraceiP54716

    Family and domain databases

    Gene3Di3.90.110.10, 1 hit
    InterProiView protein in InterPro
    IPR019802 GlycHydrolase_4_CS
    IPR001088 Glyco_hydro_4
    IPR022616 Glyco_hydro_4_C
    IPR015955 Lactate_DH/Glyco_Ohase_4_C
    IPR036291 NAD(P)-bd_dom_sf
    PANTHERiPTHR32092 PTHR32092, 1 hit
    PfamiView protein in Pfam
    PF02056 Glyco_hydro_4, 1 hit
    PF11975 Glyco_hydro_4C, 1 hit
    PRINTSiPR00732 GLHYDRLASE4
    SUPFAMiSSF51735 SSF51735, 1 hit
    SSF56327 SSF56327, 1 hit
    PROSITEiView protein in PROSITE
    PS01324 GLYCOSYL_HYDROL_F4, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGLVA_BACSU
    AccessioniPrimary (citable) accession number: P54716
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: November 7, 2018
    This is version 137 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    4. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
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    Main funding by: National Institutes of Health

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