BGAL_LACDA
ID BGAL_LACDA Reviewed; 1008 AA.
AC Q1G9Z4; P20043;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Beta-galactosidase;
DE Short=Beta-gal;
DE EC=3.2.1.23;
DE AltName: Full=Lactase;
GN Name=lacZ; OrderedLocusNames=Ldb1201;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1705929; DOI=10.1128/jb.173.6.1951-1957.1991;
RA Leong-Morgenthaler P.M., Zwahlen M.-C., Hottinger H.;
RT "Lactose metabolism in Lactobacillus bulgaricus: analysis of the primary
RT structure and expression of the genes involved.";
RL J. Bacteriol. 173:1951-1957(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR EMBL; M55068; AAA25244.1; -; Genomic_DNA.
DR EMBL; CR954253; CAI98003.1; -; Genomic_DNA.
DR RefSeq; WP_003619632.1; NZ_JQAV01000039.1.
DR AlphaFoldDB; Q1G9Z4; -.
DR SMR; Q1G9Z4; -.
DR STRING; 390333.Ldb1201; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; CAI98003; CAI98003; Ldb1201.
DR KEGG; ldb:Ldb1201; -.
DR PATRIC; fig|390333.13.peg.1439; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_9; -.
DR OMA; WCDHGIL; -.
DR BioCyc; LDEL390333:LDB_RS05145-MON; -.
DR BRENDA; 3.2.1.23; 2861.
DR SABIO-RK; Q1G9Z4; -.
DR Proteomes; UP000001259; Chromosome.
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:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.70.98.10; -; 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; 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 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; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..1008
FT /note="Beta-galactosidase"
FT /id="PRO_0000250751"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 465
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 532
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1008 AA; 114160 MW; 4681BFCA448F731F CRC64;
MSNKLVKEKR VDQADLAWLT DPEVYEVNTI PPHSDHESFQ SQEELEEGKS SLVQSLDGDW
LIDYAENGQG PVNFYAEDFD DSNFKSVKVP GNLELQGFGQ PQYVNVQYPW DGSEEIFPPQ
IPSKNPLASY VRYFDLDEAF WDKEVSLKFD GAATAIYVWL NGHFVGYGED SFTPSEFMVT
KFLKKENNRL AVALYKYSSA SWLEDQDFWR MSGLFRSVTL QAKPRLHLED LKLTASLTDN
YQKGKLEVEA NIAYRLPNAS FKLEVRDSEG DLVAEKLGPI RSEQLEFTLA DLPVAAWSAE
KPNLYQVRLY LYQAGSLLEV SRQEVGFRNF ELKDGIMYLN GQRIVFKGAN RHEFDSKLGR
AITEEDMIWD IKTMKRSNIN AVRCSHYPNQ SLFYRLCDKY GLYVIDEANL ESHGTWEKVG
GHEDPSFNVP GDDQHWLGAS LSRVKNMMAR DKNHASILIW SLGNESYAGT VFAQMADYVR
KADPTRVQHY EGVTHNRKFD DATQIESRMY APAKVIEEYL TNKPAKPFIS VEYAHAMGNS
VGDLAAYTAL EKYPHYQGGF IWDWIDQGLE KDGHLLYGGD FDDRPTDYEF CGNGLVFADR
TESPKLANVK ALYANLKLEV KDGQLFLKND NLFTNSSSYY FLTSLLVDGK LTYQSRPLTF
GLEPGESGTF ALPWPEVADE KGEVVYRVTA HLKEDLPWAD EGFTVAEAEE VAQKLPEFKP
EGRPDLVDSD YNLGLKGNNF QILFSKVKGW PVSLKYAGRE YLKRLPEFTF WRALTDNDRG
AGYGYDLARW ENAGKYARLK DISCEVKEDS VLVKTAFTLP VALKGDLTVT YEVDGRGKIA
VTADFPGAEE AGLLPAFGLN LALPKELTDY RYYGLGPNES YPDRLEGNYL GIYQGAVKKN
FSPYLRPQET GNRSKVRWYQ LFDEKGGLEF TANGADLNLS ALPYSAAQIE AADHAFELTN
NYTWVRALSA QMGVGGDDSW GQKVHPEFCL DAQKARQLRL VIQPLLLK
