ID Q74KL4_LACJO Unreviewed; 678 AA.
AC Q74KL4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 116.
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 OrderedLocusNames=LJ_0738 {ECO:0000313|EMBL:AAS08556.1};
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314 {ECO:0000313|EMBL:AAS08556.1, ECO:0000313|Proteomes:UP000000581};
RN [1] {ECO:0000313|EMBL:AAS08556.1, ECO:0000313|Proteomes:UP000000581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533
RC {ECO:0000313|Proteomes:UP000000581};
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS08556.1; -; Genomic_DNA.
DR RefSeq; WP_011161683.1; NC_005362.1.
DR AlphaFoldDB; Q74KL4; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR KEGG; ljo:LJ_0738; -.
DR PATRIC; fig|257314.6.peg.593; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_9; -.
DR Proteomes; UP000000581; 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 15..395
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 406..607
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 621..677
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 316
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 158
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 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 678 AA; 78941 MW; E6A94C3B1843B1A2 CRC64;
MKRALDINQF LHGGDYNPEQ WWDEPDVINQ DFALFKQAKI NTVTVGIFSW AKLEPQEGNY
DFSWLDEIFD RVEEMNGHVI LATPSGARPA WLAQKYPEVL RTDNRGNKRG FGGRHNHCLT
SPIYRKKVYE INTKLAEHFG QRKSLVLWHI SNEYSGECYC DLCKDAFRKW LKNKYGDLAT
LNHAWWNTFW SHTYNDWSQV NPPSPLSEMG NKGMNLDWKR FITDQTISFI DNETAPLKKI
TPNIPVTTNM MAGNPLMDPF AGFDYQKVAR HSDFISWDSY PAWSNDSQST EELGRNIGLI
HDFFRSLKHQ NFLVMENTPS RVNWHNFDRA KRPGMHELAS LQDVAHGSQG VLYFQLRASR
GSSEMFHGAV IEHRHPEKTR AFKDVTKVGK DLEKISPIVA TNYAKAKVAI VFSYDSYWAL
QDAESYSENK KVWQTIQKHY RYFYDHDIPV DFVSPEDEFS QYDLLIDPMH FLMSKSYLEK
IDNYVKNGGK IVGTYISGVV DENDLAYMNE WPKELQEIYG LEPLETDVLY PRQSNLINFE
GKEYPVHDYC ETLINCTGKV LATYSTDFYQ DTPAIVEHSY GAGKSYYLAC RTDYSFLEKF
YEKIASELVP EIPITKFNDR VSIQIRENKS EKYWFVQNFS DKEEKIELSC ELVNLLDNTK
ETGEVVLEPF ESKVYKNN
//
