ID Q5FJD5_LACAC Unreviewed; 680 AA.
AC Q5FJD5;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 Name=lacA {ECO:0000313|EMBL:AAV43189.1};
GN OrderedLocusNames=LBA1364 {ECO:0000313|EMBL:AAV43189.1};
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621 {ECO:0000313|Proteomes:UP000006381};
RN [1] {ECO:0000313|EMBL:AAV43189.1, ECO:0000313|Proteomes:UP000006381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM
RC {ECO:0000313|Proteomes:UP000006381};
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV43189.1; -; Genomic_DNA.
DR RefSeq; WP_011254434.1; NC_006814.3.
DR RefSeq; YP_194220.1; NC_006814.3.
DR AlphaFoldDB; Q5FJD5; -.
DR STRING; 272621.LBA1364; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR GeneID; 56942942; -.
DR KEGG; lac:LBA1364; -.
DR PATRIC; fig|272621.13.peg.1290; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_9; -.
DR OrthoDB; 9800974at2; -.
DR BioCyc; LACI272621:G1G49-1338-MONOMER; -.
DR Proteomes; UP000006381; 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, ECO:0000313|EMBL:AAV43189.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:AAV43189.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000006381};
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..610
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 623..679
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 680 AA; 79348 MW; 1D17E878BF3E51CE CRC64;
MKRELKSKVF LHGGDYNPEQ WLGEPEIINE DFALFKNAAI NTVTVGIFSW AKLEPEEGKY
DFAWLDDIFD RVEKMNGYVI LATPSGARPA WLARKYPEVL RTDFNNQKRG FGGRHNHCLT
SPIYRKKVRE INTKLAEHFG KRPSLILWHI SNEYSGECYC DLCQQAFRDW LKKKYRTLER
LNHSWWNTFW SHTFSDWNQI HAPSPLSEMG NKGMNLDWKR FVSDQAISFI DNEVEPLRKI
TSEIPVTTNM MAGNPLMDPF TGYNYQEMAK HLDVISWDSY PLWGNDFQST EKLGQNVGLI
HDFFRSLKHQ NFMIMENTPS RVNWADIDRA KRPGMHQLAS LQDIAHSSDS VLYFQLRASR
GSAEMFHGAV IEHRHPEKTR VFHDVKDVGH DLEKLESIYS TSYTKAKVGI VYDYNNIWAL
EDAEGYSKDK KIWQTIQSQY QYFYQNDIPV DFVSPNDNFT QYKLLIDPMH FLMTKEYMDK
LESFVKKCGY VVGTYISGVV DENGLAYMNE WPKQLQSIYG IEPLETDSLY PKQSNSIEFA
GHRYQAYDFC ETIFKHDAKV LAKYTTDFYS GTPALTAHKC GEGKGYYIAC RTDTDFLSAI
YGQIVKELDL LPNLPIKKET TKISLQVREN DDEKYLFVQN FSHEQQSILL KQKMKEMLSD
EFEENKVIVK PYGTKIYQMN
//
