BGAL_VIBVU
ID BGAL_VIBVU Reviewed; 1032 AA.
AC Q8D4H3; Q9AEQ8; Q9AHK2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=VV2_1327;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kim S.Y., Lee S.E., Morris J.G. Jr., Chung S.S., Rhee J.H.;
RT "Beta-galactosidase of Vibrio vulnificus.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29307 / CDC A8694;
RA Baek C.H., Park D.K., Lee K.E., Kim Y.T., You K.H., Hwang W., Kim K.S.;
RT "Beta-galactosidase of Vibrio vulnificus ATCC 29307.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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}.
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DR EMBL; AF305636; AAK15465.1; -; Genomic_DNA.
DR EMBL; AY028965; AAK29750.1; -; Genomic_DNA.
DR EMBL; AE016796; AAO08215.2; -; Genomic_DNA.
DR RefSeq; WP_011082210.1; NC_004460.2.
DR AlphaFoldDB; Q8D4H3; -.
DR SMR; Q8D4H3; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; AAO08215; AAO08215; VV2_1327.
DR KEGG; vvu:VV2_1327; -.
DR HOGENOM; CLU_002346_0_2_6; -.
DR OMA; SNWQLQG; -.
DR Proteomes; UP000002275; 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: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..1032
FT /note="Beta-galactosidase"
FT /id="PRO_0000367012"
FT ACT_SITE 458
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 534
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 413
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 415
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 534..537
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 594
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 598
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 601
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 601
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1006
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 354
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 388
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT CONFLICT 91
FT /note="Q -> H (in Ref. 1; AAK15465 and 2; AAK29750)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="L -> F (in Ref. 1; AAK15465 and 2; AAK29750)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..133
FT /note="DLL -> ELA (in Ref. 1; AAK15465 and 2; AAK29750)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="E -> D (in Ref. 1; AAK15465 and 2; AAK29750)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="Missing (in Ref. 1; AAK15465 and 2; AAK29750)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="N -> K (in Ref. 1; AAK15465)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="N -> K (in Ref. 1; AAK15465)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="Y -> H (in Ref. 1; AAK15465 and 2; AAK29750)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="E -> Q (in Ref. 1; AAK15465 and 2; AAK29750)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="A -> T (in Ref. 1; AAK15465 and 2; AAK29750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1028
FT /note="S -> K (in Ref. 1; AAK15465 and 2; AAK29750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1032 AA; 117737 MW; C904A3944BDE0D8E CRC64;
MTAFSEILQR RDWENPQSVN IHCLKAHSPL ASFRDMAHAR DGIHAQRQSL NGQWKFKLFD
APEQVDGQFT QADFNDAEWD EIPVPSNWQL QGYDKPIYAN IKYPFDVNPP FVPSDNPTGC
YRTRVSLSPE DLLNTQRIIF DGVNSAFHLW CNGTWVGYSQ DSRLPAEFDL TSHLVAGENT
LAVMVMRWCD GSYLEDQDMW WLSGIFRDVT LLSKPQHCIE DVFITPELDA CYRDGSLSIV
TTIAAPETYQ VQVQLFEGTQ AVTEPNIARP HNRRIDERGT WNDDVVFQTL HLREPKKWTA
ETPNLYRLVV SLLDENGTHL ESEAYPVGFR KVEISEGQLK LNGKPLLIRG VNRHEHHPEL
GHVMTEEDMI RDICLMKQYN FNAVRTAHYP NHPRWYELCD QYGLYVCDEA NIETHGMQPM
SRLSSDPQWA HAYMSRYTQM VLRDKNHPSI IIWSLGNESG HGSNHNAMYA WSKNFDPSRP
VQYEGGGSNT TATDIIAPMY ARVNTLVADE AVPKWPIKKW ISLPNETRPL ILCEYAHAMG
NSLGSFDEYW AAFREFPRLQ GGFIWDWVDQ GLSQWDENGQ HFWAYGGDFG DEINDRQFCI
NGLIFPDRTV HPTLQEAKYC QRMITVSLQE QTQKACTLLV TNENLFRTTD NEQLNWSLLE
NGQVIQTGSQ VLSVEADSQT RLEIALNFTP KAQAQYYLNT DICLIEATSW APAGHVVATE
QMALRNHAGL AMPTLRTQPA PKLTENGHAI VVSSLDEKHQ WRWDSQSGLL MEWNVDGKAQ
MLAAPQDNFF RAPLDNDIGI SEVDNVDPNA WVCRWEMAGI GQWERHCVQC ESETLAHAVV
VTTTFAYHFG GDVQAITQWT HTLSNDGEML LDVDVTLADA LPPMPRIGLE LQLPLHQADT
PITWQGLGPF ENYPDRLAAA RFGLHTQTLA QMHTPYIFPT DSGLRCGTQW LQVNELAISG
DFQFSVSQYA QQQLAEAKHT HDLLAQERIY LRLDHQHMGV GGDDSWSPSV HKEFQLTEKH
YRYQLRFSPA SR
