BGAL_CARML
ID BGAL_CARML Reviewed; 668 AA.
AC Q9RFN0;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Beta-galactosidase BgaB;
DE Short=Beta-gal {ECO:0000250|UniProtKB:P19668};
DE EC=3.2.1.23;
GN Name=bgaB {ECO:0000312|EMBL:AAF16519.1};
OS Carnobacterium maltaromaticum (Carnobacterium piscicola).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=2751;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF16519.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=BA {ECO:0000312|EMBL:AAF16519.1};
RX PubMed=10584002; DOI=10.1128/aem.65.12.5443-5450.1999;
RA Coombs J.M., Brenchley J.E.;
RT "Biochemical and phylogenetic analyses of a cold-active beta-galactosidase
RT from the lactic acid bacterium Carnobacterium piscicola BA.";
RL Appl. Environ. Microbiol. 65:5443-5450(1999).
CC -!- FUNCTION: Capable of hydrolyzing the chromogen 5-bromo-4-chloro-3-
CC indolyl-beta-D-galactopyranoside (X-Gal) at low temperatures. pNP-beta-
CC galactoside, pNP-beta-fucoside and pNP-beta-galacturonide are also
CC hydrolyzed, but not pNP-beta-galactosidase, pNP-alpha-galactoside, pNP-
CC beta-mannoside, pNP-beta-arabanoside, pNP-beta-xyloside, pNP-beta-
CC glucuronide nor pNP-betacellobioside at 20 degrees Celsius.
CC {ECO:0000269|PubMed:10584002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000269|PubMed:10584002};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for o-nitrophenyl-beta-D-galactopyranoside (ONPG) (at 30
CC degrees Celsius) {ECO:0000269|PubMed:10584002};
CC KM=1.04 mM for ONPG (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:10584002};
CC Vmax=450 umol/min/mg enzyme with ONPG as substrate (at 30 degrees
CC Celsius) {ECO:0000269|PubMed:10584002};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius for activity with ONPG as
CC substrate. Loses half of its activity at 30 degrees Celsius within 1
CC hour. Inactivated at 40 degrees Celsius in 10 minutes. In the absence
CC of glycerol, the enzyme is extremely unstable even at low-temperature
CC incubation, with an 85% loss of activity at 20 degrees Celsius after
CC 1 hour. {ECO:0000269|PubMed:10584002};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR EMBL; AF184246; AAF16519.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RFN0; -.
DR SMR; Q9RFN0; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR013739; Beta_galactosidase_C.
DR InterPro; IPR013738; Beta_galactosidase_Trimer.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR003476; Glyco_hydro_42.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; PTHR36447; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08533; Glyco_hydro_42C; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR PIRSF; PIRSF001084; B-galactosidase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..668
FT /note="Beta-galactosidase BgaB"
FT /id="PRO_0000407686"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT ACT_SITE 302
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
FT BINDING 350..353
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O69315"
SQ SEQUENCE 668 AA; 76789 MW; 6B256F81C06C4F17 CRC64;
MLQQKKLFYG GDYNPEQWSK AIILEDMRLM KKANVNYVSL NIFGWASIQP TEEGFDFSFL
DEMLDLLWEN GIGIDLANGT ASPPAWLVKK HPEILPVTSQ GTPLVHGSRQ HYCPSNKVYR
SYVIRLTEEV AKRYATHPGI VMWHVNNEYT CHISECYCES CEKSFRQWLQ MKYKKINTLN
ECWSTKFWSQ SYSQWDEIFL PKEMPTFKNP AHQLDYKRFI SDQNLTLFKA EKKAIRSYSK
DIPVMTNLMG LHKHVDGFAF AEEMDVVGWD SYPNPFEEKP YPQFLANDLT RSLKKKPFLV
MEQAPSAVNW RRANGAKSPG QMRLWSYEAL AHGADGILFF QWRQSQGGAE KFHSGMVSHN
QDTNSRIFKE VVQLGTEMSQ LDELVGTNYN AEVAIVFDWE NWWALELDAK PSGEINYIKQ
MRDLYTIFHE LNIGVDFIHP KEDLSNYKLV LSIAQYLVTD DFSAKVKRYI KAGGHFLTTF
FSGIVDEYDR VYLGGYPGAF KEVLGIYVEE FDPMPIGRKS QIKYGETYYT TELWKEVIHL
QGAETIATFT EGYLMGQPAL TKFGYGKGKT YYMGTKLAKD GNMKFIQTIL AESKIQPLNQ
VEIESENSKI SMTCRSNSSH DYIFLLNYGQ TSEKVKLKKG GQSLLDGSMV EGEVSVKAND
VKIIKLTK
