BGAL_ECO24
ID BGAL_ECO24 Reviewed; 1024 AA.
AC A7ZI91;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Beta-galactosidase {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};
GN OrderedLocusNames=EcE24377A_0368;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV16715.1; -; Genomic_DNA.
DR RefSeq; WP_000177919.1; NC_009801.1.
DR AlphaFoldDB; A7ZI91; -.
DR SMR; A7ZI91; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PRIDE; A7ZI91; -.
DR EnsemblBacteria; ABV16715; ABV16715; EcE24377A_0368.
DR KEGG; ecw:EcE24377A_0368; -.
DR HOGENOM; CLU_002346_0_2_6; -.
DR OMA; SNWQLQG; -.
DR Proteomes; UP000001122; 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: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..1024
FT /note="Beta-galactosidase"
FT /id="PRO_0000366992"
FT ACT_SITE 462
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 538
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 202
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 419
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 462
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 538..541
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 598
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 602
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 605
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 605
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1000
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 358
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 392
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1024 AA; 116462 MW; 5B313DCAAC93B53F CRC64;
MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR
FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP
TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA
GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV
LEAEVQMCGE LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGSYADRV TLRLNVENPK
LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD
PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA
HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN ELLHWMVALD
GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ
WRLAENLSVT LPSASHIIPQ LTTSETDFCI ELGNKRWQFN RQSGLLSQMW IGDEKQLLTP
LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCSADT LADAVLITTA
HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLTCQLA QVAERVNWLG
LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGSH QWRGDFQFNI
SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV
WCQK
