BGAL1_KLEPN
ID BGAL1_KLEPN Reviewed; 1034 AA.
AC P06219;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 103.
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};
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3897196; DOI=10.1128/jb.163.3.850-857.1985;
RA Buvinger W.E., Riley M.;
RT "Nucleotide sequence of Klebsiella pneumoniae lac genes.";
RL J. Bacteriol. 163:850-857(1985).
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.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01687}.
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DR EMBL; M11441; AAA25082.1; -; Genomic_DNA.
DR PIR; A24925; A24925.
DR AlphaFoldDB; P06219; -.
DR SMR; P06219; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
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..1034
FT /note="Beta-galactosidase"
FT /id="PRO_0000057662"
FT ACT_SITE 468
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 544
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 207
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 425
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 544..547
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 604
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 608
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 611
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 611
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1010
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 364
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 398
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1034 AA; 117517 MW; 8F8B9DC7521EF649 CRC64;
MQISDTGRSH TPDFHAVLAR EDWHNQTITH LNRLPAHPVF ASWRDELAAR DNLPSSRRRQ
LDGSGSSLTP AARLPSMRVV TQDLPDCRGT PVPSNWQMEG YDAPIYTNVR YPIDTTPPRV
PEDNPTGCYS LHFTVEDTWR ENGQTQIIFD GVNSAFHLWC NGVWVGYSQD SRLPAAFDLS
PFLRPGDNRL CVMVMRWSAG SWLEDQDMWR MSGIFRSVWL LNKPQQRLCD VQLTPALDAL
YRDGTLQVQA TIEATEAALA GLSVGVSLWR GEEQFAAGRQ PLGTPTVDER GHYAERVDFS
LAVATPAHWS AETPNCYRAV VTLWRGDELL EAEAWDIGFR RIEIADGLLR LNGKPLLIRG
VNRHEHHHLR GQVVTEADMV QDILLMKQNN FNAVRCSHYP NAPRWYELCN RYGLYVVDEA
NIETHGMVPM NRLSDDPAWL PAFSARVTRM VQSNRNHPCI IIWSLGNESG GGGNHEALYH
WLKRNDPSRP VQYEGGGADT TATDIICPMY ARVERDQPIP AVPKWGIKKW ISLPGEQRPL
ILCEYAHAMG NSLGNFADYW QAFREYPRLQ GGFIWDWADQ AIRKTFADGS VGWAYGGDFG
DKPNDRQFCM NGLVFPDRTP HPSLVEAKHA QQYFQFTLLS TSPLRVRIIS EYLFRPTDNE
VVRWQVQAAG EPLYHGDLTL ALPPEGSDEI TLLDSLILPE GARAVWLTLE VTQPQATAWS
EAEHRVAWQQ FPLPAPLGCR RPPCLPALPD LIVSDEVWQI RAGSQCWTID RRTGLLSRWS
VGGQEQLLTP LRDQFIRAPL DNDIGVSEVE RIDPNAWVER WRSAGLYDLE AHCVQCDAQR
LANETLVDCR WHYLRGEEVV IVSHWRMHFT ADGTLRLAVD GERAETLPPL PRVGLHFQVA
DQQAPVSWLG LGPHENYPDR RSSACFARWE QPLAAMTTPY IFPTENGLRC DTQALDWGRW
HISGHFHFSV QPWSTRQLME TDHWHKMQAE DGVWITLDGL HMGVGGDDSW TPSVLPQWLL
SQTRWQYEVS LRSL
