ID   GMUD_BACSU              Reviewed;         465 AA.
AC   O05508; Q797D9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=6-phospho-beta-glucosidase GmuD;
DE            EC=3.2.1.86;
DE   AltName: Full=Aryl-phospho-beta-D-glucosidase BglD;
DE   AltName: Full=Glucomannan utilization protein D;
GN   Name=gmuD; Synonyms=bglD, ydhP; OrderedLocusNames=BSU05840;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA   Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA   Ogasawara N.;
RT   "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT   Bacillus subtilis chromosome.";
RL   Microbiology 143:1861-1866(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION AS AN ARYL-PHOSPHO-BETA-D-GLUCOSIDASE, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RC   STRAIN=168 / PS832;
RX   PubMed=14652714; DOI=10.1007/s00203-003-0628-2;
RA   Setlow B., Cabrera-Hernandez A., Cabrera-Martinez R.M., Setlow P.;
RT   "Identification of aryl-phospho-beta-D-glucosidases in Bacillus subtilis.";
RL   Arch. Microbiol. 181:60-67(2004).
RN   [4]
RP   INDUCTION BY GLUCOMANNAN, AND FUNCTION IN GLUCOMANNAN UTILIZATION.
RC   STRAIN=168;
RX   PubMed=18177310; DOI=10.1111/j.1574-6968.2007.01018.x;
RA   Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.;
RT   "Glucomannan utilization operon of Bacillus subtilis.";
RL   FEMS Microbiol. Lett. 279:103-109(2008).
CC   -!- FUNCTION: Phospho-beta-D-glucosidase that seems to be involved in the
CC       degradation of glucomannan. Is also capable of hydrolyzing aryl-
CC       phospho-beta-D-glucosides, although very weakly, and plays only a minor
CC       role, if any, in the degradation of these substrates in vivo.
CC       {ECO:0000269|PubMed:14652714, ECO:0000269|PubMed:18177310}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose +
CC         D-glucose 6-phosphate; Xref=Rhea:RHEA:10772, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:58312, ChEBI:CHEBI:61548; EC=3.2.1.86;
CC   -!- DEVELOPMENTAL STAGE: Expressed at only a very low level in exponential-
CC       phase cells and germinating spores, but is expressed at a higher levels
CC       upon entry into the stationary phase of growth.
CC       {ECO:0000269|PubMed:14652714}.
CC   -!- INDUCTION: Up-regulated by konjac glucomannan and by cellobiose and
CC       mannobiose, the possible degradation products of glucomannan. Repressed
CC       by glucose via the carbon catabolite repression system. Also repressed
CC       by GmuR. Is not induced by aryl-beta-D-glucosides such as arbutin or
CC       salicin. {ECO:0000269|PubMed:14652714, ECO:0000269|PubMed:18177310}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; D88802; BAA19708.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12403.1; -; Genomic_DNA.
DR   PIR; D69785; D69785.
DR   RefSeq; NP_388465.1; NC_000964.3.
DR   RefSeq; WP_003243625.1; NZ_JNCM01000031.1.
DR   AlphaFoldDB; O05508; -.
DR   SMR; O05508; -.
DR   STRING; 224308.BSU05840; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   PaxDb; 224308-BSU05840; -.
DR   EnsemblBacteria; CAB12403; CAB12403; BSU_05840.
DR   GeneID; 939872; -.
DR   KEGG; bsu:BSU05840; -.
DR   PATRIC; fig|224308.179.peg.628; -.
DR   eggNOG; COG2723; Bacteria.
DR   InParanoid; O05508; -.
DR   OrthoDB; 9765195at2; -.
DR   PhylomeDB; O05508; -.
DR   BioCyc; BSUB:BSU05840-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome.
FT   CHAIN           1..465
FT                   /note="6-phospho-beta-glucosidase GmuD"
FT                   /id="PRO_0000371418"
FT   ACT_SITE        170
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        368
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   465 AA;  54334 MW;  9DD069BF2151D590 CRC64;
     MAHTEQYRFP KDFWWGSSAS ATQMEGAADR DGKGQNIWDY WFEKEPHRFF DHVGPADTSQ
     FYDNYKEDIR LMKELGHNSF RMSISWSRLI PNGTGEINDK AADFYNNVID ELIANGIEPF
     VNLFHFDMPM ALQKIGGWVN RETVDAYENY ARTCFRLFGG RVKKWFTHNE PIVPVEGGYL
     YDFHYPNKVD FKEAVQVGFH TMLSSARAIQ AYREMKQDGK IGIILNLTPS YPRSSHPADV
     KAGEIADAFF NRSFLDPSVK GEFPKELVDI LKHEGFMPDY NAEDLDIIKK NTVDLLGVNY
     YQPRRVKAKE HLPNPDAPFL PDRYFDPYVM PGRKMNPHRG WEIYEKGVYD ILINLKENYG
     NIECFISENG MGVEGEERFR DEQGIIQDDY RIEFIKEHLK WIHRAIQEGS NVKGYHLWTF
     MDNWSWTNAY KNRYGFVSVN LEKDGERTVK KSGKWFKEVA EHSGF
//