BGAL_PHOPR
ID BGAL_PHOPR Reviewed; 1030 AA.
AC Q6LL68;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=PBPRB0034;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378675; CAG21907.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6LL68; -.
DR SMR; Q6LL68; -.
DR STRING; 298386.PBPRB0034; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PRIDE; Q6LL68; -.
DR EnsemblBacteria; CAG21907; CAG21907; PBPRB0034.
DR KEGG; ppr:PBPRB0034; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_6; -.
DR OMA; SNWQLQG; -.
DR Proteomes; UP000000593; 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; Reference proteome;
KW Sodium.
FT CHAIN 1..1030
FT /note="Beta-galactosidase"
FT /id="PRO_0000367005"
FT ACT_SITE 456
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT ACT_SITE 532
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 197
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 411
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
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 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 532..535
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 596
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
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 599
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT BINDING 1004
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 352
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
FT SITE 386
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687"
SQ SEQUENCE 1030 AA; 117266 MW; 6A859CAEA1AF7939 CRC64;
MALSDIIQRR DWENPQSVNI HCLKAHSPLA SYRDINHARD GIHAQRQSLN GQWKFKLFDA
PEQVEGEFID VQFNDSAWGD ITVPSNWQLQ GYDKPIYANV KYPFEVNPPY VPADNPTGCY
RTRLTLTEAD LESTQRIIFD GVNSAFHLWC NGDWVGYSQD SRLPAEFDLS QYLTAGENTL
AVMVIRWSDG SYLEDQDMWW LSGIFRDVTL LSKPKQCIED VFITPDLDAC YRDGSLSIVT
HISAPETSQV HVQLFDGSQA VTEPSIARPH NRRIDERGSY DDVVFQTLHV REPQQWTAET
PNLYRVVVSL LDAEGNHLES EAYQVGFRKV EVKDGQLQLN GKPLLIRGVN RHEHHPELGH
VMTEEDMVRD ICLMKQYNFN AVRTAHYPNH PRWYELCDQY GLYVCDEANI ETHGMIPMNR
LSADPQWAHA YMSRYTQMVM RDKNHPSIII WSLGNESGHG SSHNAMYAWS KQFDPSRPVQ
YEGGGANTTA TDIICPMYAR VNTTVEDEAV PKWPIKQWIS LPNEQRPLIL CEYAHAMGNS
LGNFNEYWDA FREFPRLQGG FIWDWVDQGL SQWDNDGKHF WAYGGDFGDT INDRQFCING
LIFPDRTPHP TLEEVKFCQR MITVALTQQD KQQCHLTVTN EYVFRSTDNE QLHWSVLENG
VEVQSGQCTL AIDAGSQQTV DIALDFQPKA DAKYHLNTDI CLISATPWAQ AGHVSATEQF
TLSNTSSLTL PKISILSAPQ LSEQGRDILV SNLDKKHQWQ WNVESGLLTS WMVDGQSQLL
HAPEDNFFRA PLDNDIGVSE IDNIDPNAWV CRWDAAGIGR WERECVSCTS ESLSQAVKVT
STFAYHHNGG VQAITVWTYT LDNQGEMHID VDVTLADHLP PMPRIGLELA LPLPSDNTTV
TWQGLGPFEN YPDRLAAARF GQHTQSLDAM HTPYIFPTDS GLRSGTQWLN VGNLECTGDF
LFSVSRFSQQ QLTEAKHTNE LTLEDKIYLR IDHQHMGVGG DDSWSPSVHE EFQLTDNTYR
FSIMLKPRHN
