ID BGAL1_BACLD Reviewed; 663 AA. AC Q65KX8; Q62WC5; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 2. DT 24-JAN-2024, entry version 96. DE RecName: Full=Beta-galactosidase YesZ; DE Short=Beta-gal; DE EC=3.2.1.23; DE AltName: Full=Probable rhamnogalacturonan beta-galactosidase; GN Name=yesZ; OrderedLocusNames=BLi01382, BL03780; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism RT with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). CC -!- FUNCTION: May play a role in the degradation of rhamnogalacturonan CC derived from plant cell walls. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues CC in beta-D-galactosides.; EC=3.2.1.23; CC -!- SUBUNIT: Homotrimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017333; AAU40286.1; -; Genomic_DNA. DR EMBL; CP000002; AAU22933.1; -; Genomic_DNA. DR AlphaFoldDB; Q65KX8; -. DR SMR; Q65KX8; -. DR STRING; 279010.BL03780; -. DR CAZy; GH42; Glycoside Hydrolase Family 42. DR KEGG; bld:BLi01382; -. DR KEGG; bli:BL03780; -. DR eggNOG; COG1874; Bacteria. DR HOGENOM; CLU_012430_1_0_9; -. DR Proteomes; UP000000606; Chromosome. DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro. DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro. DR CDD; cd03143; A4_beta-galactosidase_middle_domain; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR013739; Beta_galactosidase_C. DR InterPro; IPR013738; Beta_galactosidase_Trimer. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR003476; Glyco_hydro_42. DR InterPro; IPR013529; Glyco_hydro_42_N. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1. DR PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1. DR Pfam; PF02449; Glyco_hydro_42; 1. DR Pfam; PF08533; Glyco_hydro_42C; 1. DR Pfam; PF08532; Glyco_hydro_42M; 1. DR PIRSF; PIRSF001084; B-galactosidase; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. PE 3: Inferred from homology; KW Glycosidase; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..663 FT /note="Beta-galactosidase YesZ" FT /id="PRO_0000367025" FT ACT_SITE 146 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 297 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT BINDING 107 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 145 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 154 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 156 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 159 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 346..349 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 663 AA; 74214 MW; C2044F388107C6C6 CRC64; MNGKLYHGAC FYPELWDEDV LDEDIRMMER IGINVVRIGE FAWSRMEPEK GRIDVGFFAD VIRKLRDNKI ETVMCTPTAT PPIWLTHGHP ERMHVNEKGE TMGHGSRQHA CTNHPYFRER ARLIIKHIAK EIGELPGLIG WQLDNEFKCH VAECICETCR TLWHKWLEDR YQTIDRLNEA WGTGVWSETY QCFEQVPQPG PTPFLHNSSL RTMYQLFSMD KISEFAREQA EVIRAYSDAP ITHNSSVMFG VDHEDLFKSL DFASFDTYAS QENSQAFLFN CDLWRNIKKG RPFWIMETSP SYSASLESYA APHQNGYLKA EAVSSYALGG AAFCYWLWRQ QRAGSEQPHG SVLSAWGEPD VGYENVLEAE RARREVEHIM LATAPLQAET AVVYSDRAKV FLKTEPHRGL HYRTLITEFY DRLLKMGIHR DVILEGSPLD GYKLLFTPFI HYLPPAFIKK AEAFAQSGGI WIAGPLTGGR TEHHTIHTDC GLGPLEKCSG VKTLFTFPMD ERNSSGTAFG VKAPLSLWSA VFEAGGTKAV GMIEKGPASG KAFITEHKCG KGKIVMLGSM PAGEAGDIMM KKLISHYAEE AGVEQKTDVT PGTVVAPRKG ADGLVWVVIN MDGKGGAVTL DGNGTDLLSG RPVTGRVTLG PHDYRVILLS ENK //