BGAL_VIBVY
ID BGAL_VIBVY Reviewed; 1031 AA.
AC Q7MG04;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=VVA0165;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000038; BAC96191.1; -; Genomic_DNA.
DR RefSeq; WP_011151589.1; NC_005140.1.
DR AlphaFoldDB; Q7MG04; -.
DR SMR; Q7MG04; -.
DR STRING; 672.VV93_v1c31610; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; BAC96191; BAC96191; BAC96191.
DR KEGG; vvy:VVA0165; -.
DR PATRIC; fig|196600.6.peg.3382; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_6; -.
DR OMA; SNWQLQG; -.
DR OrthoDB; 245411at2; -.
DR Proteomes; UP000002675; Chromosome II.
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; Reference proteome;
KW Sodium.
FT CHAIN 1..1031
FT /note="Beta-galactosidase"
FT /id="PRO_0000367013"
FT ACT_SITE 457
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 533
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 412
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
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 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 457
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 533..536
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 593
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 597
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 600
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 600
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1005
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 353
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 387
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1031 AA; 117763 MW; 3A3E6A9AD4BC5560 CRC64;
MTAFSEILQR RDWENPQSVN IHCLKAHSPL ASFRDMAHAR DGIHAQRQSL NGQWKFKLFD
APEQVDGQFT QADFNDAEWD EIPVPSNWQL HGYDKPIYAN IKYPFDVNPP FVPRENPTGC
YRTRVSLSPE DLLNTQRIIF DGVNSAFHLW CNGTWVGYSQ DSRLPAEFDL TSHLVAGENT
LAVMVMRWCD GSYLEDQDMW WLSGIFRDVT LLSKPQHCIE DVFITPDLDA CYRDGSLSIV
TTIAAPETYQ VQVQLFEGTQ AVTEPNIDRP HNRRIDERGT WNDVVFQTLH LREPKKWTAE
TPNLYRLVVS LLDENGTHLE SEAYPVGFRK VEISEGQLKL NGKPLLIRGV NRHEHHPELG
HVMTEEDMIR DICLMKQYNF NAVRTAHYPN HPRWYELCDQ YGLYVCDEAN IETHGMQPMS
RLSSDPQWAH AYMSRYTQMV LRDKNHPSII IWSLGNESGH GSNHNAMYAW SKNFDPSRPV
QYEGGGSNTT ATDIIAPMYA RVNTLIADEA VPKWPIKKWI SLPNETRPLI LCEYAHAMGN
SLGSFDEYWA AFREFPRLQG GFIWDWVDQG LSQWDENGQH FWAYGGDFGD EINDRQFCIN
GLIFPDRTVH PTLQEAKYCQ RMITVSLQEQ TQKACTLLVT NENLFRATDN EQLNWSLLEN
GQVIQTGSLA LSVEADSQTR LEIALNFTPK AQAQYHLNTD ICLIEATSWA PAGHVVATEQ
MALRNHAGLA IPTLRTQPAP KLTQDGHAIV VSSLDEKHQW RWDSQSGLLM EWNVDGKAQM
LAAPQDNFFR APLDNDIGIS EVDNVDPNAW VCRWEMAGIG QWERHCVHCD SETLAHTVVV
TTTFAYHFGG DVQAITQWTH TLSNDGEMLL DVDVTLADTL PPMPRIGLEL QLPLYQADTP
ITWQGLGPFE NYPDRLAAAR FGLHTQTLAQ MHTPYIFPTD SGLRCGTQWL QVNELAISGD
FQFSVSQYAQ QQLAEAKHTH DLLAQERIYL RLDHQHMGVG GDDSWSPSVH KEFQLTEKHY
RYQLRFKPAS R
