BGAL1_BACLD
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 03-AUG-2022, entry version 92.
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; Firmicutes; 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 9375
RC / 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 9375
RC / 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}.
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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 EnsemblBacteria; AAU22933; AAU22933; BL03780.
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 Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.40.50.880; -; 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; PTHR36447; 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; SSF51445; 1.
DR SUPFAM; SSF52317; SSF52317; 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
