BGAL_CROS8
ID BGAL_CROS8 Reviewed; 1043 AA.
AC A7MN76;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=ESA_02977;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU78206.1; -; Genomic_DNA.
DR RefSeq; WP_012125561.1; NC_009778.1.
DR AlphaFoldDB; A7MN76; -.
DR SMR; A7MN76; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PRIDE; A7MN76; -.
DR EnsemblBacteria; ABU78206; ABU78206; ESA_02977.
DR KEGG; esa:ESA_02977; -.
DR PATRIC; fig|290339.8.peg.2666; -.
DR HOGENOM; CLU_002346_0_2_6; -.
DR OMA; DYPQYTN; -.
DR OrthoDB; 245411at2; -.
DR Proteomes; UP000000260; 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; 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; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Magnesium; Metal-binding; Sodium.
FT CHAIN 1..1043
FT /note="Beta-galactosidase"
FT /id="PRO_0000366984"
FT REGION 33..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 471
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 547
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 212
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 212
FT /ligand="substrate"
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 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 547..550
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 607
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 614
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 614
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1017
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 367
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 401
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1043 AA; 117662 MW; 269BB0FA74F2772F CRC64;
MTENPTTTAF NELQTRPLAT ILARNDWQNP AITSVNRLPS HTPLHGWRDA DRARRGEPSD
AVLSLDGEWQ FSFFASPHQV PEVWLAADLS DARATPVPSN WQMEGYDTPI YTNVRYPIPV
NPPFVPDDNP TGCYSRDIEV PQAWLETGRT RIIFGGVNSA FYLWCNGQWV GYSQDSRLPA
EFDLTGVLHA GRNRLCVLVL RWSDGTYLED QDMWRMSGIF RPVSLLHLPE QALADVRVHT
ELAPSLRHAT LFSEVEVTPA ACGLSVTLAL WHGENEIASQ TLPLGSAPID ERGNYAERVT
LSLDVDNPLL WSAETPHLYR AVVTLLDADG MPLVSEAHDV GFRRVEINNG LLTLNGQPLL
IRGVNRHEHH PEKGQAVDEA AMVQDILLMK QNNFNAVRCS HYPNQPRWYE LCSRYGLYVV
DEANIETHGM EPMSRLSDDP VWLGAYSERV TRMVKCNRNH PSIIIWSLGN ESGNGATHTA
LYNWIKHQDP TRPVQYEGGG ADTRATDIIC PMYARVETDQ LIPAVPKWSI KKWISMPGET
RPLILCEYAH AMGNSLGNFA DYWAAFRQYP RLQGGFIWDW ADQAITRVEP DGSRWWAYGG
DFGDTPNDRQ FCMNGLVFPD RTPHPALFEA KHQQQFFQFR LVSENPLQIE VTSEYLFRES
DNERLLWSIE VRGETRLSGE LTLELGPQAS RVLTLSDTGF SARAGDEEIW LHVRVEQPQA
TPWSPEGHLS AWAQWPLAAP LALPEPVAAG DAPQLEITDA EFVIRHGCQT WRVSRASGQL
IQWSDDGVDQ ILTPLADQFI RAPIDNDIGV SEVERIDPNA WVERWKAAGL YNTEHRCLAC
DAQTTRDGVE IVAQHAYFVK GVADGPAILS RWRMVVDNQG ALHCDIDIAR SAALPPLPRV
GVVCQLRGGE ETASWLGLGP HENYPDRLSS ACFSRWTLPL SELTTPYIFP GENGLRCNTR
ELNWNGWQAE GEFHFSLSPY GTRQLMETSH WHKLQPEAGI WLTIDGFHMG VGGDDSWTPS
VHPEYLLTAR EYRYRFTLRR RQG
