LICH_BACSU
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 03-AUG-2022, entry version 137.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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 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 -!- 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; NZ_JNCM01000034.1.
DR AlphaFoldDB; P46320; -.
DR SMR; P46320; -.
DR STRING; 224308.BSU38560; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR jPOST; P46320; -.
DR PaxDb; P46320; -.
DR PRIDE; P46320; -.
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 OMA; NEHASHI; -.
DR PhylomeDB; P46320; -.
DR BioCyc; BSUB:BSU38560-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
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:UniProtKB-KW.
DR Gene3D; 3.90.110.10; -; 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; PTHR32092; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 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
