ID BGAL_VIBC3 Reviewed; 1024 AA. AC A5F5U6; C3M461; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 2. DT 27-MAR-2024, entry version 87. 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=VC0395_A1917, VC395_2453; OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / OS O395). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=345073; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395; RA Heidelberg J.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395; RX PubMed=19115014; DOI=10.1371/journal.pone.0004053; RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., RA Wang W., Wang J., Qian W., Li D., Wang L.; RT "A recalibrated molecular clock and independent origins for the cholera RT pandemic clones."; RL PLoS ONE 3:E4053-E4053(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; Evidence={ECO:0000255|HAMAP- CC 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; Evidence={ECO:0000255|HAMAP- CC 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 -!- SEQUENCE CAUTION: CC Sequence=ABQ20296.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=ACP10443.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CP000627; ABQ20296.1; ALT_INIT; Genomic_DNA. DR EMBL; CP001235; ACP10443.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_001243585.1; NZ_JAACZH010000008.1. DR AlphaFoldDB; A5F5U6; -. DR SMR; A5F5U6; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR KEGG; vco:VC0395_A1917; -. DR KEGG; vcr:VC395_2453; -. DR PATRIC; fig|345073.21.peg.2357; -. DR eggNOG; COG3250; Bacteria. DR HOGENOM; CLU_002346_0_2_6; -. DR OrthoDB; 9758603at2; -. DR Proteomes; UP000000249; Chromosome 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:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt. DR Gene3D; 2.70.98.10; -; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. 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 PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1. DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1. DR Pfam; PF02929; Bgal_small_N; 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 Pfam; PF16353; LacZ_4; 1. DR PRINTS; PR00132; GLHYDRLASE2. DR SMART; SM01038; Bgal_small_N; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 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_0000367011" FT ACT_SITE 459 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT ACT_SITE 535 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 100 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 198 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 198 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 414 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 416 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 459 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 459 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 535..538 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 595 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 599 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" 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 602 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 995 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 355 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 389 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" SQ SEQUENCE 1024 AA; 118176 MW; 204F11E6188E33D8 CRC64; MRNFSDILLS QDWQNPHIVK WHCRTPHVPL HSYRTEQEAR LDVGGNRQSL NGQWRFALFE KPEAVEPAVI DPDFDDSAWA HIPVPSNWQM QGFDKPIYTN IQYPFADRPP YVPQDNPTGC YRHRFTLEKQ ALTESIRIVF DGVNSAFHLW CNGHWVGYSQ DSRLPAEFEL TPYLQEGENL LVAMVLRWSD GSYLEDQDMW WLSGIFRDVY LYRKPILAIE DFFIRTELDA LYQHAELRVE TRLSQVTRHH QVQVALFDAQ GECVARSQAL HTGQRVVDEK GAWHDKTEHS LAICSPTLWS DEAPYLYRCV ICLLDEDGAP IEFESAAVGF RKVEITQGLL KLNGQPLLIR GVNRHEHHPE LGHVMDEASM RRDIELMKQH NFNAVRTAHY PNHPRWYELC DEYGLYVVDE ANLETHGQFP MSRLSNDPQW VNAYLQRMIG MVERDKNHPC VIIWSLGNES GIGTNHHAMY QWTKQRDPSR PVQYEGGGAN TAATDIVCPM YARVDQHQPH PAVPKYALKN WISLPQENRP LILCEYAHAM GNSLGAFYKY WQAFREFPRL QGGFIWDWVD QGISKWDSEG RHYWGYGGDF GDTINDRQFC INGLLFPDRT PHPALHEVKK VQQPYQFSLS YPKLTIHNER LFAALPLELV VSVLCDGQEI KQERLPLDIA PRGTITLDLA SLPMLPEHEY HLNAVLLCRE DQPWSNAGHC IASEQWCLQP RRSMLPKITH APLPQWQQDG DKVRIEAANQ QWQFNRQTGL LEQWWQNGQP VLSEPLRDNF YRAVLDNDIG TSEAQHLDPN SWIARWHAAG LDKLRVECDD LRVTTLNESV EVVIDVAHYH QQALALRTRW RYQIFGDARV ELNVEVMLCS DLPPLPRVGL TLALPVAENP VSWFGRGPHE NYPDRLQSAH VGRYTATVDE LHTPYIFPSE NGLRCDTRQL QVGALVVEGH FHFSLSRYSQ TMLDKAKHSN ELVAGDKWYL NLDAQHMGVG GDDSWSQSVH PEFLLTQPHY QYQLTLRVKA SSPQ //