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Database: UniProt
Entry: U4TK99_9LACO
LinkDB: U4TK99_9LACO
Original site: U4TK99_9LACO 
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
//
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