ID I0BSU2_9BACL Unreviewed; 691 AA.
AC I0BSU2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN ORFNames=B2K_32840 {ECO:0000313|EMBL:AFH65439.1};
OS Paenibacillus mucilaginosus K02.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH65439.1, ECO:0000313|Proteomes:UP000007392};
RN [1] {ECO:0000313|EMBL:AFH65439.1, ECO:0000313|Proteomes:UP000007392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K02 {ECO:0000313|EMBL:AFH65439.1,
RC ECO:0000313|Proteomes:UP000007392};
RA Xiao B., Sun L., Xiao L., Lian B.;
RT "Complete genome sequence of Paenibacillus mucilaginosus K02.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|PIRNR:PIRNR001084};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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DR EMBL; CP003422; AFH65439.1; -; Genomic_DNA.
DR RefSeq; WP_014652721.1; NC_017672.3.
DR AlphaFoldDB; I0BSU2; -.
DR KEGG; pmw:B2K_32840; -.
DR PATRIC; fig|997761.3.peg.6597; -.
DR HOGENOM; CLU_012430_1_1_9; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000007392; 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:SF1; BETA-GALACTOSIDASE GANA; 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 {ECO:0000256|PIRNR:PIRNR001084};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 14..386
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 398..607
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 616..672
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 691 AA; 77944 MW; 2E580F5159B373D9 CRC64;
MINKKLPKMF YGGDYNPEQW DKPVWDEDMR MFQLAGIDVA TVNVFSWALL QPSENEYNFE
LLDEIMDKLH ENGLYACLAT STGAHPAWMA HRHPDVLRVD FQGRKRKFGG RHNSCPNSPT
YRKYARLLAG KLAERYKDHP ALLVWHVSNE YGGECYCDNC AAAFRVWLQQ RYGSLEAVNK
AWNTRFWGHT FYDWEEIVPP NELSEQWGPT RTNFQGISLD YTRFNSDSLL ECYKEEHEEL
KKHTPDIMVT TNLMGTFKPL DYFKWAKHMD IVSWDNYPAA DTPVSRTAMT HDLMRGLKDG
APFMLMEQTP SQQNWQPYNS LKRPGVMRLW SYQAVARGAD TVMFFQLRRS VGACEKYHGA
VIEHVGHEHT RVFRECAQLG AELQQLGDSL LDSRVPSRAA IVFDWENWWA VEFSSGPTVA
LQYVEEVHKY YDALYQANIQ VDMIGTDADL SGYDVVIAPV LYMVKSGYAK KVEEFVQGGG
TFLTTFFSGI VNENDIVTLG GYPGELRKVL GIWAEEIDAL LPGKQNRIVM KKELGSLQGE
YACEMLCDLI HSEGAEIIAE YGDDFYQGMP VVTANTFGQG QAWYLASSPE PSFLQGLLQQ
LCRDKGIEPL LETPAGVEVS RRRKDGKDYY FLLNHNAAPQ TVDAAALDAV DVLAGGKAGI
VELPAHGAVI LQAAASAEDT RSGSAQGVLS R
//