ID U4TK99_9LACO Unreviewed; 665 AA.
AC U4TK99;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=L248_2951 {ECO:0000313|EMBL:ERL65276.1};
OS Schleiferilactobacillus shenzhenensis LY-73.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1231336 {ECO:0000313|EMBL:ERL65276.1, ECO:0000313|Proteomes:UP000030647};
RN [1] {ECO:0000313|Proteomes:UP000030647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY-73 {ECO:0000313|Proteomes:UP000030647};
RX PubMed=24265500;
RA Lin Z., Liu Z., Yang R., Zou Y., Wan D., Chen J., Guo M., Zhao J., Fang C.,
RA Yang R., Liu F.;
RT "Whole-Genome Sequencing of Lactobacillus shenzhenensis Strain LY-73T.";
RL Genome Announc. 1:e00972-e00913(2013).
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; KI271588; ERL65276.1; -; Genomic_DNA.
DR RefSeq; WP_022529536.1; NZ_KI271588.1.
DR AlphaFoldDB; U4TK99; -.
DR SMR; U4TK99; -.
DR STRING; 1231336.L248_2951; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_0_9; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000030647; Unassembled WGS sequence.
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 {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 10..382
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 396..594
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 608..637
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 146
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 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 145
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 665 AA; 75325 MW; F8415605BBF85CBE CRC64;
MQPKIQFGVD YYPEHWPEER WDQDFAMMAE MGIDVVRLAE FSWFKLEPAD GQYDFGWLDK
VLDLAAAHGI RAVLGTPTAA PPAWLIAQHP DIQPVDREGR THYFGGRHHD CQSNPIYRDY
IGRFVRAYAQ HFGKNPTVVG WQVDNELGNS HGDLCYCRYC QRHFQKWLRA KYDTIENLNE
NWGTAFWSQG YQDFSQIQAP KMTASGDNPS ALLDWQQCHS DLINDFHAFQ AQIIRQYSPG
RFITHNMMGF SPVVCYYDLG EQLDFASQDQ YPTGHFLADQ TSFRGAQCAA ELDFIRSVKQ
QSFWVMEQQT TITGWEYMGR LPKPGQIPLW SMQSVAHGAD AIVYFRWRSS ALGTEQFWHG
ILPHSGIPGR AYREIRAFIH QTKPLLREIN GTTPRAKVGI VFSYPQDYAL NIQPQHPDMA
YTQTLMTYYG ALYRRNVAVD FIRDTADFSQ YDLVIAPLQY LMTSALADRY AAYVQGGGQL
VLTMRTGVKH PNNLCMTDAA LPGKTLSQVL GLTVPEYDCL RDVDVVVDWA GQSFTGTHWA
DLIAPTTATP LATYGSEFYD GTPAITQNRF GAGTAYYVGT ELTDALADQF VGQLPAVAAE
TITAPPRVEI THRDSATKRY YFVLNHTGET QTVPIPAAWT PYFSEAQPGQ IAPYHYQVFT
EAIHS
//