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P54716

- GLVA_BACSU

UniProt

P54716 - GLVA_BACSU

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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

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
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. 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 – 116Combined sources
Beta strandi15 – 173Combined sources
Helixi18 – 2710Combined sources
Turni28 – 314Combined sources
Beta strandi34 – 407Combined sources
Helixi44 – 6118Combined sources
Beta strandi65 – 717Combined sources
Helixi73 – 775Combined sources
Beta strandi81 – 855Combined sources
Helixi91 – 10313Combined sources
Turni104 – 1063Combined sources
Beta strandi111 – 1133Combined sources
Helixi114 – 13825Combined sources
Beta strandi143 – 1464Combined sources
Helixi151 – 16111Combined sources
Beta strandi167 – 1693Combined sources
Helixi173 – 18513Combined sources
Helixi190 – 1923Combined sources
Beta strandi193 – 2008Combined sources
Beta strandi203 – 2119Combined sources
Helixi218 – 22811Combined sources
Helixi246 – 25510Combined sources
Beta strandi260 – 2623Combined sources
Helixi264 – 2663Combined sources
Helixi267 – 2704Combined sources
Helixi272 – 2765Combined sources
Beta strandi281 – 2833Combined sources
Helixi285 – 2928Combined sources
Turni293 – 3008Combined sources
Helixi301 – 3077Combined sources
Turni319 – 3213Combined sources
Helixi322 – 33312Combined sources
Beta strandi337 – 3448Combined sources
Beta strandi356 – 36510Combined sources
Beta strandi368 – 3714Combined sources
Helixi379 – 40123Combined sources
Helixi404 – 41310Combined sources
Helixi420 – 43314Combined sources
Turni434 – 4374Combined sources

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

        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:
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

« Hide 'large scale' publications
  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 29, 2014
This is version 116 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