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Protein

Maltose-6'-phosphate glucosidase

Gene

glvA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

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

Enzyme 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

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Cobalt, Iron, Manganese, Metal-binding, NAD, Nickel

    Enzyme and pathway databases

    BioCyciBSUB:BSU08180-MONOMER.
    BRENDAi3.2.1.122. 658.
    SABIO-RKP54716.

    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

    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
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 11Combined sources6
    Beta strandi15 – 17Combined sources3
    Helixi18 – 27Combined sources10
    Turni28 – 31Combined sources4
    Beta strandi34 – 40Combined sources7
    Helixi44 – 61Combined sources18
    Beta strandi65 – 71Combined sources7
    Helixi73 – 77Combined sources5
    Beta strandi81 – 85Combined sources5
    Helixi91 – 103Combined sources13
    Turni104 – 106Combined sources3
    Beta strandi111 – 113Combined sources3
    Helixi114 – 138Combined sources25
    Beta strandi143 – 146Combined sources4
    Helixi151 – 161Combined sources11
    Beta strandi167 – 169Combined sources3
    Helixi173 – 185Combined sources13
    Helixi190 – 192Combined sources3
    Beta strandi193 – 200Combined sources8
    Beta strandi203 – 211Combined sources9
    Helixi218 – 228Combined sources11
    Helixi246 – 255Combined sources10
    Beta strandi260 – 262Combined sources3
    Helixi264 – 266Combined sources3
    Helixi267 – 270Combined sources4
    Helixi272 – 276Combined sources5
    Beta strandi281 – 283Combined sources3
    Helixi285 – 292Combined sources8
    Turni293 – 300Combined sources8
    Helixi301 – 307Combined sources7
    Turni319 – 321Combined sources3
    Helixi322 – 333Combined sources12
    Beta strandi337 – 344Combined sources8
    Beta strandi356 – 365Combined sources10
    Beta strandi368 – 371Combined sources4
    Helixi379 – 401Combined sources23
    Helixi404 – 413Combined sources10
    Helixi420 – 433Combined sources14
    Turni434 – 437Combined sources4

    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...

    Miscellaneous databases

    EvolutionaryTraceiP54716.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 4 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105F8D. Bacteria.
    COG1486. LUCA.
    HOGENOMiHOG000239810.
    KOiK01232.
    OMAiKYPMREK.
    PhylomeDBiP54716.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProiIPR019802. GlycHydrolase_4_CS.
    IPR001088. Glyco_hydro_4.
    IPR022616. Glyco_hydro_4_C.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF02056. Glyco_hydro_4. 1 hit.
    PF11975. Glyco_hydro_4C. 1 hit.
    [Graphical view]
    PRINTSiPR00732. GLHYDRLASE4.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    SSF56327. SSF56327. 1 hit.
    PROSITEiPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
    [Graphical view]

    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.
    PATRICi18973286. VBIBacSub10457_0857.

    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.

    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.
    PATRICi18973286. VBIBacSub10457_0857.

    Phylogenomic databases

    eggNOGiENOG4105F8D. Bacteria.
    COG1486. LUCA.
    HOGENOMiHOG000239810.
    KOiK01232.
    OMAiKYPMREK.
    PhylomeDBiP54716.

    Enzyme and pathway databases

    BioCyciBSUB:BSU08180-MONOMER.
    BRENDAi3.2.1.122. 658.
    SABIO-RKP54716.

    Miscellaneous databases

    EvolutionaryTraceiP54716.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProiIPR019802. GlycHydrolase_4_CS.
    IPR001088. Glyco_hydro_4.
    IPR022616. Glyco_hydro_4_C.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF02056. Glyco_hydro_4. 1 hit.
    PF11975. Glyco_hydro_4C. 1 hit.
    [Graphical view]
    PRINTSiPR00732. GLHYDRLASE4.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    SSF56327. SSF56327. 1 hit.
    PROSITEiPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGLVA_BACSU
    AccessioniPrimary (citable) accession number: P54716
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: November 2, 2016
    This is version 130 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

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

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    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.