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Maltose-6'-phosphate glucosidase (EC 3.2.1.122) (6-phospho-alpha-D-glucosidase) (6-phosphoryl-O-alpha-D-glucopyranosyl:phosphoglucohydrolase)

 GLVA_BACSU              Reviewed;         449 AA.
P54716;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-JUN-2017, entry version 133.
RecName: Full=Maltose-6'-phosphate glucosidase;
EC=3.2.1.122;
AltName: Full=6-phospho-alpha-D-glucosidase;
AltName: Full=6-phosphoryl-O-alpha-D-glucopyranosyl:phosphoglucohydrolase;
Name=glvA; Synonyms=glv-1, glvG, malA; OrderedLocusNames=BSU08180;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8704981; DOI=10.1099/13500872-142-6-1417;
Yamamoto H., Uchiyama S., Fajar A.N., Ogasawara N., Sekiguchi J.;
"Determination of a 12 kb nucleotide sequence around the 76 degrees
region of the Bacillus subtilis chromosome.";
Microbiology 142:1417-1421(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
PROTEIN SEQUENCE OF 1-37, CHARACTERIZATION, MASS SPECTROMETRY, AND
MUTAGENESIS.
PubMed=9765262; DOI=10.1074/jbc.273.42.27347;
Thompson J., Pikis A., Ruvinov S.B., Henrissat B., Yamamoto H.,
Sekiguchi J.;
"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.";
J. Biol. Chem. 273:27347-27356(1998).
[4]
INDUCTION.
PubMed=11489864; DOI=10.1128/JB.183.17.5110-5121.2001;
Yamamoto H., Serizawa M., Thompson J., Sekiguchi J.;
"Regulation of the glv operon in Bacillus subtilis: YfiA (GlvR) is a
positive regulator of the operon that is repressed through CcpA and
cre.";
J. Bacteriol. 183:5110-5121(2001).
[5]
CRYSTALLIZATION.
PubMed=10329789; DOI=10.1107/S0907444999003790;
Varrot A., Yamamoto H., Sekiguchi J., Thompson J., Davies G.J.;
"Crystallization and preliminary X-ray analysis of the 6-phospho-
alpha-glucosidase from Bacillus subtilis.";
Acta Crystallogr. D 55:1212-1214(1999).
[6]
REACTION MECHANISM, CHARACTERIZATION, COFACTOR, SUBSTRATE SPECIFICITY,
ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17676871; DOI=10.1021/bi700536p;
Yip V.L.Y., Thompson J., Withers S.G.;
"Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis
of a 6-phospho-alpha-glucosidase from glycoside hydrolase family 4.";
Biochemistry 46:9840-9852(2007).
[7]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF COMPLEX WITH NAD(H) AND
ALPHA-D-GLUCOSE-6-PHOSPHATE, AND REACTION MECHANISM.
PubMed=15341727; DOI=10.1016/j.str.2004.06.020;
Rajan S.S., Yang X., Collart F., Yip V.L.Y., Withers S.G., Varrot A.,
Thompson J., Davies G.J., Anderson W.F.;
"Novel catalytic mechanism of glycoside hydrolysis based on the
structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from
Bacillus subtilis.";
Structure 12:1619-1629(2004).
-!- FUNCTION: 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 ACTIVITY: Alpha-maltose 6'-phosphate + H(2)O = D-glucose
+ D-glucose 6-phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:17676871};
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:17676871};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:17676871};
Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
Evidence={ECO:0000269|PubMed:17676871};
Note=Binds 1 divalent metal cation per subunit. Manganese, iron,
cobalt or nickel enhance activity. {ECO:0000269|PubMed:17676871};
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540;
Evidence={ECO:0000269|PubMed:17676871};
Note=Binds 1 NAD(+) per subunit. Is only active with NAD(+), not
NADH. {ECO:0000269|PubMed:17676871};
-!- ENZYME REGULATION: Cellobiose-6'-phosphate and 6-phospho-beta-D-
glucopyranoside are not substrates but competitive inhibitors of
GlvA. {ECO:0000269|PubMed:17676871}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=400 uM for maltose-6'-phosphate (at pH 7.5 and 37 degrees
Celsius) {ECO:0000269|PubMed:17676871};
KM=360 uM for maltose-6'-phosphate (at pH 8.4 and 37 degrees
Celsius) {ECO:0000269|PubMed:17676871};
KM=610 uM for methyl 6-phospho-alpha-D-glucoside (at pH 7.5 and
37 degrees Celsius) {ECO:0000269|PubMed:17676871};
KM=69 uM for phenyl 6-phospho-alpha-D-glucoside (at pH 7.5 and
37 degrees Celsius) {ECO:0000269|PubMed:17676871};
KM=52 uM for 4-nitrophenyl 6-phospho-alpha-D-glucoside (at pH
7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:17676871};
KM=12 uM for 3,4-dinitrophenyl 6-phospho-alpha-D-glucoside (at
pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:17676871};
KM=2.9 uM for 3,4-dinitrophenyl 6-phospho-beta-D-glucoside (at
pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:17676871};
KM=27 uM for 3,5-dichlorophenyl 6-phospho-beta-D-glucoside (at
pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:17676871};
KM=34 uM for 3-nitrophenyl 6-phospho-beta-D-glucoside (at pH 7.5
and 37 degrees Celsius) {ECO:0000269|PubMed:17676871};
pH dependence:
Optimum pH is about 7.6-8.4. Stable from pH 4.0 to 10.0.
{ECO:0000269|PubMed:17676871};
-!- SUBUNIT: Homotetramer.
-!- INDUCTION: By maltose; repressed by glucose.
{ECO:0000269|PubMed:11489864}.
-!- MASS SPECTROMETRY: Mass=50510; Method=Electrospray; Range=1-449;
Evidence={ECO:0000269|PubMed:9765262};
-!- 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
Mn(2+).
-!- MISCELLANEOUS: 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.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
{ECO:0000305}.
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EMBL; D50543; BAA09103.1; -; Genomic_DNA.
EMBL; AL009126; CAB12647.1; -; Genomic_DNA.
PIR; F69635; F69635.
RefSeq; NP_388699.1; NC_000964.3.
RefSeq; WP_003244008.1; NZ_JNCM01000032.1.
PDB; 1U8X; X-ray; 2.05 A; X=1-449.
PDBsum; 1U8X; -.
ProteinModelPortal; P54716; -.
SMR; P54716; -.
STRING; 224308.Bsubs1_010100004548; -.
DrugBank; DB02007; alpha-D-glucose 6-phosphate.
CAZy; GH4; Glycoside Hydrolase Family 4.
PaxDb; P54716; -.
PRIDE; P54716; -.
EnsemblBacteria; CAB12647; CAB12647; BSU08180.
GeneID; 936161; -.
KEGG; bsu:BSU08180; -.
PATRIC; fig|224308.179.peg.884; -.
eggNOG; ENOG4105F8D; Bacteria.
eggNOG; COG1486; LUCA.
HOGENOM; HOG000239810; -.
KO; K01232; -.
OMA; METYSPD; -.
PhylomeDB; P54716; -.
BioCyc; BSUB:BSU08180-MONOMER; -.
BRENDA; 3.2.1.122; 658.
SABIO-RK; P54716; -.
EvolutionaryTrace; P54716; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0050081; F:maltose-6'-phosphate glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
InterPro; IPR019802; GlycHydrolase_4_CS.
InterPro; IPR001088; Glyco_hydro_4.
InterPro; IPR022616; Glyco_hydro_4_C.
InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
InterPro; IPR016040; NAD(P)-bd_dom.
PANTHER; PTHR32092; PTHR32092; 1.
Pfam; PF02056; Glyco_hydro_4; 1.
Pfam; PF11975; Glyco_hydro_4C; 1.
PRINTS; PR00732; GLHYDRLASE4.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF56327; SSF56327; 1.
PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Cobalt; Complete proteome;
Direct protein sequencing; Glycosidase; Hydrolase; Iron; Manganese;
Metal-binding; NAD; Nickel; Reference proteome.
CHAIN 1 449 Maltose-6'-phosphate glucosidase.
/FTId=PRO_0000169859.
NP_BIND 6 72 NAD.
ACT_SITE 172 172 Proton donor.
ACT_SITE 265 265 Proton acceptor.
METAL 171 171 Manganese.
METAL 202 202 Manganese.
BINDING 95 95 Substrate.
BINDING 149 149 Substrate.
BINDING 285 285 Substrate.
SITE 111 111 Increases basicity of active site Tyr.
MUTAGEN 41 41 D->E,G: Loss of activity.
{ECO:0000269|PubMed:9765262}.
MUTAGEN 111 111 E->D,G: Loss of activity.
{ECO:0000269|PubMed:9765262}.
MUTAGEN 359 359 E->D,G: Loss of activity.
{ECO:0000269|PubMed:9765262}.
STRAND 6 11 {ECO:0000244|PDB:1U8X}.
STRAND 15 17 {ECO:0000244|PDB:1U8X}.
HELIX 18 27 {ECO:0000244|PDB:1U8X}.
TURN 28 31 {ECO:0000244|PDB:1U8X}.
STRAND 34 40 {ECO:0000244|PDB:1U8X}.
HELIX 44 61 {ECO:0000244|PDB:1U8X}.
STRAND 65 71 {ECO:0000244|PDB:1U8X}.
HELIX 73 77 {ECO:0000244|PDB:1U8X}.
STRAND 81 85 {ECO:0000244|PDB:1U8X}.
HELIX 91 103 {ECO:0000244|PDB:1U8X}.
TURN 104 106 {ECO:0000244|PDB:1U8X}.
STRAND 111 113 {ECO:0000244|PDB:1U8X}.
HELIX 114 138 {ECO:0000244|PDB:1U8X}.
STRAND 143 146 {ECO:0000244|PDB:1U8X}.
HELIX 151 161 {ECO:0000244|PDB:1U8X}.
STRAND 167 169 {ECO:0000244|PDB:1U8X}.
HELIX 173 185 {ECO:0000244|PDB:1U8X}.
HELIX 190 192 {ECO:0000244|PDB:1U8X}.
STRAND 193 200 {ECO:0000244|PDB:1U8X}.
STRAND 203 211 {ECO:0000244|PDB:1U8X}.
HELIX 218 228 {ECO:0000244|PDB:1U8X}.
HELIX 246 255 {ECO:0000244|PDB:1U8X}.
STRAND 260 262 {ECO:0000244|PDB:1U8X}.
HELIX 264 266 {ECO:0000244|PDB:1U8X}.
HELIX 267 270 {ECO:0000244|PDB:1U8X}.
HELIX 272 276 {ECO:0000244|PDB:1U8X}.
STRAND 281 283 {ECO:0000244|PDB:1U8X}.
HELIX 285 292 {ECO:0000244|PDB:1U8X}.
TURN 293 300 {ECO:0000244|PDB:1U8X}.
HELIX 301 307 {ECO:0000244|PDB:1U8X}.
TURN 319 321 {ECO:0000244|PDB:1U8X}.
HELIX 322 333 {ECO:0000244|PDB:1U8X}.
STRAND 337 344 {ECO:0000244|PDB:1U8X}.
STRAND 356 365 {ECO:0000244|PDB:1U8X}.
STRAND 368 371 {ECO:0000244|PDB:1U8X}.
HELIX 379 401 {ECO:0000244|PDB:1U8X}.
HELIX 404 413 {ECO:0000244|PDB:1U8X}.
HELIX 420 433 {ECO:0000244|PDB:1U8X}.
TURN 434 437 {ECO:0000244|PDB:1U8X}.
SEQUENCE 449 AA; 50514 MW; A903F7E41CFEF7AB CRC64;
MKKKSFSIVI AGGGSTFTPG IVLMLLDHLE EFPIRKLKLY DNDKERQDRI AGACDVFIRE
KAPDIEFAAT TDPEEAFTDV DFVMAHIRVG KYAMRALDEQ IPLKYGVVGQ ETCGPGGIAY
GMRSIGGVLE ILDYMEKYSP DAWMLNYSNP AAIVAEATRR LRPNSKILNI CDMPVGIEDR
MAQILGLSSR KEMKVRYYGL NHFGWWTSIQ DQEGNDLMPK LKEHVSQYGY IPKTEAEAVE
ASWNDTFAKA RDVQAADPDT LPNTYLQYYL FPDDMVKKSN PNHTRANEVM EGREAFIFSQ
CDMITREQSS ENSEIKIDDH ASYIVDLARA IAYNTGERML LIVENNGAIA NFDPTAMVEV
PCIVGSNGPE PITVGTIPQF QKGLMEQQVS VEKLTVEAWA EKSFQKLWQA LILSKTVPNA
RVARLILEDL VEANKDFWPE LDQSPTRIS


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