BGAL_KLEP3
ID BGAL_KLEP3 Reviewed; 1035 AA.
AC B5XQY2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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}; OrderedLocusNames=KPK_2776;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(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; CP000964; ACI08231.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XQY2; -.
DR SMR; B5XQY2; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; ACI08231; ACI08231; KPK_2776.
DR KEGG; kpe:KPK_2776; -.
DR HOGENOM; CLU_002346_0_2_6; -.
DR OMA; DYPQYTN; -.
DR OrthoDB; 245411at2; -.
DR Proteomes; UP000001734; 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..1035
FT /note="Beta-galactosidase"
FT /id="PRO_0000367000"
FT ACT_SITE 469
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 545
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 208
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 426
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 545..548
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 605
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 609
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 612
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 612
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1011
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 365
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 399
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1035 AA; 117917 MW; A44AC3C1E52DFCB5 CRC64;
MQISDTGHSH MPDFHAVLAR EDWQNQTITH LNRLPAHPAF ASWRDELAAR DNHLSTRRRQ
LDGEWQFVYA RSPFAVDAQW LTQDLPDSRG TPVPSNWQME GYDAPIYTNV RYPIDTTPPR
VPEDNPTGCY SLHFTVEDTW RENGQTQIIF DGVNSAFHLW CNGVWVGYSQ DSRLPAAFDL
SPFLRPGDNR LCVMVMRWSA GSWLEDQDMW RMSGIFRSVW LLNKPQQRLC DVQLTPALDA
LYRDGTLQVQ ATVEATEAAL AGLSVGVSLW RGEEQVAAGR QPLGTPAVDE RGHYAERVDF
ALAVTAPAHW SAETPNCYRA VVTLWRGDEL LEAEAWDIGF RRIEIADGLL RLNGKPLLIR
GVNRHEHHYL RGQVVTEADM VQDILLMKQN NFNAVRCSHY PNAPRWYELC NRYGLYVVDE
ANIETHGMVP MNRLSDDPAW LPAFSARVTR MVQSNRNHPC IIIWSLGNES GGGGNHEALY
HWLKRNDPSR PVQYEGGGAD TTATDIICPM YARVERDQPI PAVPKWGIKK WISLPGEQRP
LILCEYAHAM GNSLGNFADY WQAFREYPRL QGGFIWDWAD QAIRKIFDDG SVGWAYGGDF
GDKPNDRQFC MNGLVFPDRT PHPSLVEAKH AQQYFQFTLL STSPLRVRIT SEYLFRPTDN
EVVRWQVQSA GETLYHGNLT LALPPEGSDE ITLLDSLILP EGARAVWLTL EVTQPRATDW
SEADHRVAWQ QFPLPAPLAL PAPTVPAGAP DLIVSDEVWQ IRAGSQCWTI DRRTGLLSRW
SVGGQEQLLT PLRDQFIRAP LDNDIGVSEV ERIDPNAWVE RWKSAGLYDL EAHCVQCDAQ
RLANETLVDC RWHYLRGEEV VIVSHWRMHF TADGTLRLAV DGERAETLPP LPRVGLHFQV
ADQQAPVSWL GLGPHENYPD RRSSACFARW EQPLAAMTTP YIFPTENGLR CDTQALDWGR
WHVSGHFHFS VQPWSTRQLM ETDHWHKMQA EDGVWITLDG LHMGVGGDDS WTPSVLPQWL
LSQTRWQYEF FLRCL
