ID E3G1U6_ENTLS Unreviewed; 1030 AA.
AC E3G1U6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN OrderedLocusNames=Entcl_0624 {ECO:0000313|EMBL:ADO46901.1};
OS Enterobacter lignolyticus (strain SCF1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=701347 {ECO:0000313|EMBL:ADO46901.1, ECO:0000313|Proteomes:UP000006872};
RN [1] {ECO:0000313|Proteomes:UP000006872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1 {ECO:0000313|Proteomes:UP000006872};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA Hazen T.C., Woyke T.;
RT "Complete sequence of Enterobacter cloacae SCF1.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO46901.1, ECO:0000313|Proteomes:UP000006872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1 {ECO:0000313|EMBL:ADO46901.1,
RC ECO:0000313|Proteomes:UP000006872};
RX PubMed=22180812; DOI=10.4056/sigs.2104875;
RA Deangelis K.M., D'Haeseleer P., Chivian D., Fortney J.L., Khudyakov J.,
RA Simmons B., Woo H., Arkin A.P., Davenport K.W., Goodwin L., Chen A.,
RA Ivanova N., Kyrpides N.C., Mavromatis K., Woyke T., Hazen T.C.;
RT "Complete genome sequence of "Enterobacter lignolyticus" SCF1.";
RL Stand. Genomic Sci. 5:69-85(2011).
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:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU361154};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; CP002272; ADO46901.1; -; Genomic_DNA.
DR RefSeq; WP_013364654.1; NC_014618.1.
DR AlphaFoldDB; E3G1U6; -.
DR STRING; 701347.Entcl_0624; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; esc:Entcl_0624; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_6; -.
DR Proteomes; UP000006872; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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 PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 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 Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000006872}.
FT DOMAIN 727..998
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1030 AA; 117663 MW; FD8D39E561A41E1A CRC64;
MNRWENLQLT HENRLPPRAY FFSYDSTAQA RTFARETSSR FLSLSGQWNF RFFSNPLLVP
EAFTSQYISG WEPITVPGMW QMEGHGQLQY TDEGFPFPID VPYVPTDNPT GAYQRTFTLS
EGWQGKQTLI KFDGVETYFE VYVNGQYIGF SKGSRLTAEF DISAAVKTGD NLLCVRVMQW
ADSTYIEDQD MWWSAGIFRD VYLVGKTPLH VQDFTVRTDF NDDYRDATLS CQLQLENLAA
RPDAATLEYV LFDGEQALYQ GKTGSIAVDQ TAHAHFAIDV KAPQQWSAEN PYLYHLVMTL
KNAAGEVLEI IPQRVGFRDI KVRDGLFYIN NRYVMLHGVN RHDNDHLKGR AVGMERVEKD
LQLMKQHNIN SVRTAHYPND PRFYELCDIY GLFVMAETDV ESHGFANVGN LSAITDDPAW
EHIYVERIVR HVHAQKNHPS IVIWSLGNES GYGCNIRAMY HATRALDDTR LVHYEEDRDA
EVVDIISTMY TRVPLMNEFG EYPHAKPRII CEYAHAMGNG PGGLTEYQNV FYQHDSIQGH
YVWEWCDHGI QATDDSGAVW YKYGGDYGDY PNNYNFCLDG LIFSDQTPGP GLREYKQVIA
PVKVQATDLA RGELRVDNKL WFSTLDDYTL RVEVRAEGET LSSEVLKVRD LAPNSGREVR
ITMPALDERE AFVNVMVTKD SRTPYSDANH AIAVYQFPLK ARTAVKTPLI NASATPLSVA
DDRLSYTISG HNFRAVFSKV SGKLTHWQVN GVDQVTREPK INFFKPMIDN HKQEYEGLWQ
PAHLQIMQEH LREFHTERQG DTVIVTTRSI IAPPVFDFGM RCTYRWQITP QGHINVELQG
ERYGDYPHIV PCIGFMLGIN GEFEQVNYYG RGPGENYADS QQCNIIDIWR TTVDEMFVNY
PFPQNNGNRQ HVRWASFTSR HGNGLLVVPR RPINVSAWHY TAENIHAAQH CNELQRSDDI
TLNLDDQLLG LGSNSWGSEV LDSWRVWLKP FNYGFTLLPL EGGCSTSQVL ANHAFGADFF
SPVSHSEAEK
//