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P54716

- GLVA_BACSU

UniProt

P54716 - GLVA_BACSU

Protein

Maltose-6'-phosphate glucosidase

Gene

glvA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

    Binds 1 divalent metal ion per subunit. Manganese, iron, cobalt or nickel enhance activity.1 Publication
    Binds 1 NAD+ per subunit. Is only active in the presence of the nicotinamide cofactor in its oxidized, and not the reduced NADH, form.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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei95 – 951Substrate
    Sitei111 – 1111Increases basicity of active site Tyr
    Binding sitei149 – 1491Substrate
    Metal bindingi171 – 1711Manganese
    Active sitei172 – 1721Proton donor
    Metal bindingi202 – 2021Manganese
    Active sitei265 – 2651Proton acceptor
    Binding sitei285 – 2851Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi6 – 7267NADAdd
    BLAST

    GO - Molecular functioni

    1. maltose-6'-phosphate glucosidase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    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. 700.
    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
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU08180. [Micado]

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi41 – 411D → E or G: Loss of activity. 1 Publication
    Mutagenesisi111 – 1111E → D or G: Loss of activity. 1 Publication
    Mutagenesisi359 – 3591E → D or G: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 449449Maltose-6'-phosphate glucosidasePRO_0000169859Add
    BLAST

    Proteomic databases

    PaxDbiP54716.

    Expressioni

    Inductioni

    By maltose; repressed by glucose.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi224308.BSU08180.

    Structurei

    Secondary structure

    1
    449
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 116
    Beta strandi15 – 173
    Helixi18 – 2710
    Turni28 – 314
    Beta strandi34 – 407
    Helixi44 – 6118
    Beta strandi65 – 717
    Helixi73 – 775
    Beta strandi81 – 855
    Helixi91 – 10313
    Turni104 – 1063
    Beta strandi111 – 1133
    Helixi114 – 13825
    Beta strandi143 – 1464
    Helixi151 – 16111
    Beta strandi167 – 1693
    Helixi173 – 18513
    Helixi190 – 1923
    Beta strandi193 – 2008
    Beta strandi203 – 2119
    Helixi218 – 22811
    Helixi246 – 25510
    Beta strandi260 – 2623
    Helixi264 – 2663
    Helixi267 – 2704
    Helixi272 – 2765
    Beta strandi281 – 2833
    Helixi285 – 2928
    Turni293 – 3008
    Helixi301 – 3077
    Turni319 – 3213
    Helixi322 – 33312
    Beta strandi337 – 3448
    Beta strandi356 – 36510
    Beta strandi368 – 3714
    Helixi379 – 40123
    Helixi404 – 41310
    Helixi420 – 43314
    Turni434 – 4374

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U8XX-ray2.05X1-449[»]
    ProteinModelPortaliP54716.
    SMRiP54716. Positions 3-445.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54716.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 4 family.Curated

    Phylogenomic databases

    eggNOGiCOG1486.
    HOGENOMiHOG000239810.
    KOiK01232.
    OMAiKYPMREK.
    OrthoDBiEOG632D2X.
    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.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    PROSITEiPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54716-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKKSFSIVI AGGGSTFTPG IVLMLLDHLE EFPIRKLKLY DNDKERQDRI    50
    AGACDVFIRE KAPDIEFAAT TDPEEAFTDV DFVMAHIRVG KYAMRALDEQ 100
    IPLKYGVVGQ ETCGPGGIAY GMRSIGGVLE ILDYMEKYSP DAWMLNYSNP 150
    AAIVAEATRR LRPNSKILNI CDMPVGIEDR MAQILGLSSR KEMKVRYYGL 200
    NHFGWWTSIQ DQEGNDLMPK LKEHVSQYGY IPKTEAEAVE ASWNDTFAKA 250
    RDVQAADPDT LPNTYLQYYL FPDDMVKKSN PNHTRANEVM EGREAFIFSQ 300
    CDMITREQSS ENSEIKIDDH ASYIVDLARA IAYNTGERML LIVENNGAIA 350
    NFDPTAMVEV PCIVGSNGPE PITVGTIPQF QKGLMEQQVS VEKLTVEAWA 400
    EKSFQKLWQA LILSKTVPNA RVARLILEDL VEANKDFWPE LDQSPTRIS 449
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50543 Genomic DNA. Translation: BAA09103.1.
    AL009126 Genomic DNA. Translation: CAB12647.1.
    PIRiF69635.
    RefSeqiNP_388699.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12647; CAB12647; BSU08180.
    GeneIDi936161.
    KEGGibsu:BSU08180.
    PATRICi18973286. VBIBacSub10457_0857.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50543 Genomic DNA. Translation: BAA09103.1 .
    AL009126 Genomic DNA. Translation: CAB12647.1 .
    PIRi F69635.
    RefSeqi NP_388699.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U8X X-ray 2.05 X 1-449 [» ]
    ProteinModelPortali P54716.
    SMRi P54716. Positions 3-445.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU08180.

    Protein family/group databases

    CAZyi GH4. Glycoside Hydrolase Family 4.

    Proteomic databases

    PaxDbi P54716.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12647 ; CAB12647 ; BSU08180 .
    GeneIDi 936161.
    KEGGi bsu:BSU08180.
    PATRICi 18973286. VBIBacSub10457_0857.

    Organism-specific databases

    GenoListi BSU08180. [Micado ]

    Phylogenomic databases

    eggNOGi COG1486.
    HOGENOMi HOG000239810.
    KOi K01232.
    OMAi KYPMREK.
    OrthoDBi EOG632D2X.
    PhylomeDBi P54716.

    Enzyme and pathway databases

    BioCyci BSUB:BSU08180-MONOMER.
    BRENDAi 3.2.1.122. 700.
    SABIO-RK P54716.

    Miscellaneous databases

    EvolutionaryTracei P54716.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    InterProi IPR019802. 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 ]
    Pfami PF02056. Glyco_hydro_4. 1 hit.
    PF11975. Glyco_hydro_4C. 1 hit.
    [Graphical view ]
    PRINTSi PR00732. GLHYDRLASE4.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    PROSITEi PS01324. GLYCOSYL_HYDROL_F4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Determination of a 12 kb nucleotide sequence around the 76 degrees region of the Bacillus subtilis chromosome."
      Yamamoto H., Uchiyama S., Fajar A.N., Ogasawara N., Sekiguchi J.
      Microbiology 142:1417-1421(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-alpha-glucosidase. Assignment to family 4 of the glycosylhydrolase superfamily."
      Thompson J., Pikis A., Ruvinov S.B., Henrissat B., Yamamoto H., Sekiguchi J.
      J. Biol. Chem. 273:27347-27356(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-37, CHARACTERIZATION, MASS SPECTROMETRY, MUTAGENESIS.
    4. "Regulation of the glv operon in Bacillus subtilis: YfiA (GlvR) is a positive regulator of the operon that is repressed through CcpA and cre."
      Yamamoto H., Serizawa M., Thompson J., Sekiguchi J.
      J. Bacteriol. 183:5110-5121(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    5. "Crystallization and preliminary X-ray analysis of the 6-phospho-alpha-glucosidase from Bacillus subtilis."
      Varrot A., Yamamoto H., Sekiguchi J., Thompson J., Davies G.J.
      Acta Crystallogr. D 55:1212-1214(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
    6. "Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from glycoside hydrolase family 4."
      Yip V.L.Y., Thompson J., Withers S.G.
      Biochemistry 46:9840-9852(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REACTION MECHANISM, CHARACTERIZATION, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis."
      Rajan S.S., Yang X., Collart F., Yip V.L.Y., Withers S.G., Varrot A., Thompson J., Davies G.J., Anderson W.F.
      Structure 12:1619-1629(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF COMPLEX WITH NAD(H) AND ALPHA-D-GLUCOSE-6-PHOSPHATE, REACTION MECHANISM.

    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: October 1, 2014
    This is version 115 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

    External Data

    Dasty 3