ID   LICH_BACSU              Reviewed;         442 AA.
AC   P46320;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 152.
DE   RecName: Full=Probable 6-phospho-beta-glucosidase;
DE            EC=3.2.1.86;
GN   Name=licH; Synonyms=celD, celF; OrderedLocusNames=BSU38560;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8990303; DOI=10.1128/jb.179.2.496-506.1997;
RA   Tobisch S., Glaser P., Krueger S., Hecker M.;
RT   "Identification and characterization of a new beta-glucoside utilization
RT   system in Bacillus subtilis.";
RL   J. Bacteriol. 179:496-506(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-305.
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA   Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA   Fujita Y.;
RT   "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT   the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT   sacXY region.";
RL   Microbiology 142:3113-3123(1996).
CC   -!- FUNCTION: Hydrolyzes phospho-beta-glucosides. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose
CC         6-phosphate + D-glucose; Xref=Rhea:RHEA:10772, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:58312, ChEBI:CHEBI:61548; EC=3.2.1.86;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- INDUCTION: Induced by lichenan, lichenan hydrolysate and cellobiose.
CC       Subject to carbon catabolite repression.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
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DR   EMBL; Z49992; CAA90288.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15882.1; -; Genomic_DNA.
DR   EMBL; D83026; BAA11746.1; -; Genomic_DNA.
DR   PIR; S57762; S57762.
DR   RefSeq; NP_391735.1; NC_000964.3.
DR   RefSeq; WP_003244285.1; NC_000964.3.
DR   AlphaFoldDB; P46320; -.
DR   SMR; P46320; -.
DR   FunCoup; P46320; 125.
DR   STRING; 224308.BSU38560; -.
DR   jPOST; P46320; -.
DR   PaxDb; 224308-BSU38560; -.
DR   EnsemblBacteria; CAB15882; CAB15882; BSU_38560.
DR   GeneID; 937373; -.
DR   KEGG; bsu:BSU38560; -.
DR   PATRIC; fig|224308.179.peg.4175; -.
DR   eggNOG; COG1486; Bacteria.
DR   InParanoid; P46320; -.
DR   OrthoDB; 9808275at2; -.
DR   PhylomeDB; P46320; -.
DR   BioCyc; BSUB:BSU38560-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P46320; -.
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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05296; GH4_P_beta_glucosidase; 1.
DR   FunFam; 3.40.50.720:FF:000163; 6-phospho-beta-glucosidase; 1.
DR   FunFam; 3.90.110.10:FF:000008; 6-phospho-beta-glucosidase; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR019802; GlycHydrolase_4_CS.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR32092:SF5; 6-PHOSPHO-BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Manganese; Metal-binding;
KW   NAD; Reference proteome.
FT   CHAIN           1..442
FT                   /note="Probable 6-phospho-beta-glucosidase"
FT                   /id="PRO_0000169861"
FT   ACT_SITE        256
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         5..73
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   SITE            112
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   442 AA;  48711 MW;  91CB42C8BB93F567 CRC64;
     MTKGLKIVTI GGGSSYTPEL VEGFIKRYDE LPVRELWLVD IPEGEEKLNI VGTLAKRMVE
     KAGVPIDIHL TLDRRKALKD ADFVTTQFRV GLLQARAKDE RIPLKYGVIG QETNGPGGLF
     KGLRTIPVIL EIAKDIEELC PNAWLVNFTN PAGMVTEALL RYSNLKKVVG LCNVPIGIKM
     GVAKALDVDV DRVEVQFAGL NHMVFGLDVF LDGVSVKEQV IEAMGDPKNA MTMKNISGAE
     WEPDFLKALN VIPCGYHRYY FKTKEMLEHE LEASQTEGTR AEVVQKVEKE LFELYKDPNL
     AIKPPQLEKR GGAYYSDAAC NLISSIYNDK HDIQPVNTIN NGAIASIPDD SAVEVNCVMT
     KTGPKPIAVG DLPVSVRGLV QQIKSFERVA AEAAVTGDYQ TALLAMTINP LVPSDTVAKQ
     ILDEMLEAHK AYLPQFFNKI EA
//