BGAL1_KLEP7
ID BGAL1_KLEP7 Reviewed; 1035 AA.
AC A6T8X0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Beta-galactosidase 1 {ECO:0000255|HAMAP-Rule:MF_01687};
DE Short=Beta-gal 1 {ECO:0000255|HAMAP-Rule:MF_01687};
DE EC=3.2.1.23 {ECO:0000255|HAMAP-Rule:MF_01687};
DE AltName: Full=Lactase 1 {ECO:0000255|HAMAP-Rule:MF_01687};
GN Name=lacZ1 {ECO:0000255|HAMAP-Rule:MF_01687};
GN OrderedLocusNames=KPN78578_15800; ORFNames=KPN_01610;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000647; ABR77041.1; -; Genomic_DNA.
DR RefSeq; WP_015958381.1; NC_009648.1.
DR AlphaFoldDB; A6T8X0; -.
DR SMR; A6T8X0; -.
DR STRING; 272620.KPN_01610; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; ABR77041; ABR77041; KPN_01610.
DR KEGG; kpn:KPN_01610; -.
DR HOGENOM; CLU_002346_0_2_6; -.
DR OMA; DYPQYTN; -.
DR Proteomes; UP000000265; 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; Reference proteome;
KW Sodium.
FT CHAIN 1..1035
FT /note="Beta-galactosidase 1"
FT /id="PRO_0000367001"
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; 117758 MW; C18A68CF81E14A6A CRC64;
MQISDTGRSH TPDFHAVLAR EDWQNQTITH LNRLPAHPVF ASWRDELAAR DNLPSSRRRQ
LDGEWQFSYA RSPFAVDAQW LTQDLPDCRG TPVPSNWQME GYDAPIYTNV RYPIDTTPPR
VPEDNPTGCY SLHFTVEDTW RENGQTQIIF DGVNSAFHLW CNGVWVGYSQ DSRLPAAFDL
SPFLRPGDNR LCVMVMRWSA GSWLEDQDMW RMSGIFRSVW LLNKPQQRLC DVQLTPALDA
LYRDGTLQVQ ATIEATEAAL AGLSVGVSLW RGEEQIAAGR QPLGTPTVDE RGHYAERVDF
SLAVATPAHW SAETPNCYRA VVTLWRGDEL LEAEAWDIGF RRIEIADGLL RLNGKPLLIR
GVNRHEHHHL RGQVVTEADM VQDILLMKQN NFNAVRCSHY PNAPRWYELC NRYGLYVVDE
ANIETHGMVP MNRLSDDPAW LPAFSARVTR MVQSNRNHPC IIIWSLGNES GGGGNHEALY
HWLKRNDPSR PVQYEGGGAD TTATDIICPM YARVERDQPI PAVPKWGIKK WISLPGEQRP
LILCEYAHAM GNSLGNFADY WQAFREYPRL QGGFIWDWAD QAIRKTFADG SVGWAYGGDF
GDKPNDRQFC MNGLVFPDRT PHPSLVEAKH AQQYFQFTLL STSPLRVRII SEYLFRPTDN
EVLRWQVQAA GEPLYHGDLT LALPPEGSDE ITLLDSLILP EGARAVWLTL EVTQPQATAW
SEAEHRVAWQ QFPLPAPLAL PAPTVSAGAP DLIVSDEVWQ IRAGSQCWTI DRRTGLLSRW
SVGGQEQLLT PLRDQFIRAP LDNDIGVSEV ERIDPNAWVE RWRSAGLYDL EAHCVQCDAQ
RLANETLVDC RWHYLRGEEV VIVSHWRMHF TADGTLRLAV DGERAETLPP LPRVGLHFQV
ADQQAPVSWL GLGPHENYPD RRSSACFARW EQPLAAMTTP YIFPTENGLR CDTQALDWGR
WHISGHFHFS VQPWSTRQLM ETDHWHKMQA EDGVWITLDG LHMGVGGDDS WTPSVLPQWL
LSQTRWHYEV SLRCL
