BGAL2_ENTCL
ID BGAL2_ENTCL Reviewed; 1029 AA.
AC Q2XQU3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Beta-galactosidase 2 {ECO:0000255|HAMAP-Rule:MF_01687};
DE Short=Beta-gal {ECO:0000255|HAMAP-Rule:MF_01687};
DE EC=3.2.1.23 {ECO:0000255|HAMAP-Rule:MF_01687};
DE AltName: Full=Lactase {ECO:0000255|HAMAP-Rule:MF_01687};
GN Name=lacZ {ECO:0000255|HAMAP-Rule:MF_01687}; Synonyms=bga;
OS Enterobacter cloacae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B5;
RA Lu L.L., Xiao M.;
RT "Purification, characterization, and molecular cloning of a beta-
RT galactosidase with transglycosylation activity from Enterobacter cloacae.";
RL Submitted (OCT-2005) 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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01687};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01687};
CC Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC Rule:MF_01687};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01687};
CC Note=Binds 1 sodium ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01687};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01687}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01687}.
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DR EMBL; DQ266449; ABB73039.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2XQU3; -.
DR SMR; Q2XQU3; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PRIDE; Q2XQU3; -.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.70.98.10; -; 1.
DR HAMAP; MF_01687; Beta_gal; 1.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF16353; DUF4981; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF49303; SSF49303; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Magnesium; Metal-binding; Sodium.
FT CHAIN 1..1029
FT /note="Beta-galactosidase 2"
FT /id="PRO_0000366983"
FT ACT_SITE 463
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 539
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 203
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 539..542
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 599
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 603
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 606
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 606
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1004
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 393
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1029 AA; 116816 MW; C96F1A32A29E2241 CRC64;
MPNTLSLTLS AILARRDWEN PGVTQWNRLE AHAPLHSWRL EQPALDDAAS ASRRSLNGVW
RFNYFPAPEQ IPEAWVTEDC ADAVPMPVPS NWQMQGFDTP IYTNVTYPIP VNPPFVPQEN
PTGCYSLTFD VDDAWLQSGQ TRIIFDGVNS AFHLWCNGRW MGYSQDSRLP AEFNLSTVLR
PGENRLAVMV LRWCDGSYLE DQDMWRMSGI FRDVTLLHKP ETQIADYRVV TDLNAELDRA
VLKADVALAG AGFADCEVVF TLWRKGEKCA SVSRRPGSAV VDERGSWDER LTVAIPIDRP
ALWSAETPEL YRLTMALLGP QGEVLEVEAC DVGFRRVDIS NGLLKLNGKP LLIRGVNRLE
HHPENGQVMD EATMRRDIEI MKQHNFNAVR CSHYPNHPLW YRLCDRYGLY VVDEANIETH
GMVPMSRLAD DPRWLPAMSE RVTRMVQRDR NHPSIIIWSL GNESGHGANH DALYRWLKTT
DPTRPVQYEG GGANTAATDI VCPMYARVDW DQPFPAVPKW SIKKWIGMPD ETRPLILCEY
AHAMGNSFGG FAKYWQAFRS HPRLQGGFVW DWVDQALTKK DEKGNAFWAY GGDFGDTPND
RQFCLNGLVF PDRTPHPALY EAQRAQQFFT FTLVSTSPLM IEVQSGYLFR PTDNEVLSWT
VARDGKVLAS GEVTLAIAPE GVQRLEIALP ELKAGPGEIW LNVEVRQPRA TPWSPAGHRC
AWEQWPLPAP LFIAPPASTG EPPVLTQNDR ILEVTHRQQR WQFDRASGYL TQWWRNGVET
LLSPVTDNVS RAPLDNDIGV SEATRIDPNA WVERWKAAGM YDLTSRMLHC EAEQHAREVV
VTTLNVLEHR GRALFLSRKI WRLDEQGVLH GDIQVDIASD IPKPARIGLS VHLAETPEKV
DWLGLGPHEN YPDRKLAAQQ GRWTLPLADM HTPYIFPTEN GLRCDTRKLV LGAHQLNGAF
HFSVGRYSQQ QLRETTHHHL LREEPGGWLN LDAFHMGVGG DDSWSPSVSP EFILQTRQLR
YTFSWQQNP
