ID R9I3U9_BACUN Unreviewed; 1243 AA.
AC R9I3U9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ORFNames=C801_00817 {ECO:0000313|EMBL:EOS10869.1};
OS Bacteroides uniformis dnLKV2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1235787 {ECO:0000313|EMBL:EOS10869.1, ECO:0000313|Proteomes:UP000014212};
RN [1] {ECO:0000313|EMBL:EOS10869.1, ECO:0000313|Proteomes:UP000014212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=dnLKV2 {ECO:0000313|Proteomes:UP000014212};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides uniformis dnLKV2.";
RL Submitted (APR-2013) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU361154};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOS10869.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASSO01000004; EOS10869.1; -; Genomic_DNA.
DR AlphaFoldDB; R9I3U9; -.
DR PATRIC; fig|1235787.3.peg.843; -.
DR HOGENOM; CLU_002346_0_2_10; -.
DR Proteomes; UP000014212; Unassembled WGS sequence.
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; 2.60.120.200; -; 1.
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; IPR013320; ConA-like_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 InterPro; IPR006558; LamG-like.
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 Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000014212};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1243
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004474060"
FT DOMAIN 626..760
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 939..1239
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1243 AA; 142440 MW; 35AC1888A866A77D CRC64;
MNLRKLFLPL CSVALCLQSY AQDKSFLKDM LWYIDNPSVF EKGQEEGHAW HMPEKSMLLN
GTWKFFWCDT PEGIPAHFFN PEFPDKQWGD IKVPSNWEMQ GYGDKLFRNV SAPFGVNPPH
APKEYNPTGL YRRTFKVPAS WAAKDQIFLR FEKVASASFV WVNGHEVGYN EGAQEPAEYN
ITPYLKLGEN TLAVCVLKYS DGYYLEGQDY WRLAGIFDDV WLYATPAVRI FDWQVITEFD
NTYTDSQLSI QVKIKDYQKK PSENYGLKAY LKDKNGKIIC NFSATPFEMD AAEKTIQLHT
LVQEPQKWTA ETPELYTLGL ELSNPTGLLK DKIETVIGFK KTEIKDGVFY LNGIPLKVNA
QNSHMQHPEE GHIMDEATIR KDFELLKQFN FNAVRTSHYP PVNKYLELAN EYGLYIIDEV
GDEAHASEWI SNLPEYEEMY RERCRRMVLR DRNHPCVLFW SAGNESGEGI NITHTIEEGK
SLDPTRFWMY GGNAFSHPAE DIIGPRYPTP MELEMQVGIG MGEDSRPSFM DEYLSVAGNA
GGALDDYWEA IYRHPRLMGG AIWDFVSPGL TERIRQMDDL SPFHTPAHLM GNARLVKEGK
NTVLDLNGHD QWVEVYRADN VEMNNNELTL TCRIYPRKLV SSCGSFITKG NYQFGLQQRG
KDKLEFYIYT DKKHSVCASL PTDWEYNWHQ VTCVYDGQKM SIYIDGAEKA STQASGNIRN
LPYPVNIGRN AETHGQETSV YICDAQMDEV GIFAKALTSS FHPEEAALWL NFEQETENGT
FYSYGIGART YGSIWPDRSV QPEMWQMKKT GQPLSFSMSD VTEGVVELWN RNHYTNASRY
AIRWELKEDD KVIQSGDLAL STAPLSRELV HIPYKKPALI PGKEYRLMLH AVLKKDELWA
KAGHEVAWEE LELPWSLPCS SEEKVQGIPS YSLSEKELIV SGEGFKYVFN RTDGQLTSMV
VQDMELLESP LRLNLWRAPL ANELDNWNAS SARSSNWKEG YGYTVATEMY SAGIDRLTHQ
PLSFSVSETT EGVHIHIIDA ELMGKGEKEK KDLYIEGVQN NGIINHYEYI INSEGTIEIR
HVLKPEGKMP LWFPRIGLTL TVSDALDQVK WYGRGPQENY PDRKTGYPTG IYASTVQAMY
EPYLMPQDYG LRTDVRWLQL TTDKGIGLQF KMNEWFNFNI YPYSTDNLTK AMYTYQLQKQ
KGMTLNLDYA TTGVGCTARG VFGAYKAMPQ EYRRTISIKP MMK
//
