ID E3D7N7_GARV3 Unreviewed; 1005 AA.
AC E3D7N7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=HMPREF0421_21247 {ECO:0000313|EMBL:ADP39329.1};
OS Gardnerella vaginalis (strain ATCC 14019 / 317).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP39329.1, ECO:0000313|Proteomes:UP000001453};
RN [1] {ECO:0000313|EMBL:ADP39329.1, ECO:0000313|Proteomes:UP000001453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA Wilson B.A.;
RT "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT differences in metabolic and virulence potential.";
RL PLoS ONE 5:E12411-E12411(2010).
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}.
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; CP002104; ADP39329.1; -; Genomic_DNA.
DR RefSeq; WP_009993823.1; NC_014644.1.
DR RefSeq; YP_003986352.1; NC_014644.1.
DR AlphaFoldDB; E3D7N7; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; gvg:HMPREF0421_21247; -.
DR PATRIC; fig|525284.18.peg.1228; -.
DR HOGENOM; CLU_002346_0_2_11; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000001453; 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 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 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}.
FT DOMAIN 719..996
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1005 AA; 115350 MW; 2008216FC4A13A3A CRC64;
MVESVNDWEN PSLTGKNRLP ARAYFLSYEC SSLAKTYKRE FAHGYVCLNG KWKFALLKSP
NSVRKYMKTE LQSNWDEVNV PHMWQFDGYG QLQYTDEAFP FPVDPPRVPT LTPTAVYQKE
IIISSIDDDE EIILRCDGIE SYGEVYLNGR YVGMTKGSRL SAEFDITEAV VEGTNLFSIV
VMQYCDGTYL EDQDMWWASG IFRDIYVYRR PKVHLKDFFA RTHLLDDGRA CLSFDATISG
TSSFSCSIED NGIVVSRIEQ KVPNGEVHTK MYIDNPHLWN PEDPYLYDMV ITVTSDTGSN
EVVSHRLGLV EISIKDGLMY LNGKYFVMHG VNRHDFDQNK GRAIDIADVK HELIMMKQHN
INAIRTSHYP NDPRFYQLCD ELGFMVVAET DLECHGFEHV GNISMISDDS DWQLAYVSRI
EREVFQERNH ACIVMWSLGN ESGFGCNFRA MYHRCKELDP TRPVHYEEDR FGEVVDVLST
MYSRVSQMND FGEHPTKKPR ILCEYAHSMG NGPGGLQEYQ KVIDCYPSIQ GHFVWEWCDH
GIAQVDSQGR SYNAYGGDFH DYPNDGNFSI DGLVFPWKAA SPGLLEYKQV LCPVHVDLDG
EYIVITNKRY FTDLDDIRID LSLSENGHAI YNTTISPGEL HPSNTIRVKL NIPKLGSNVG
ELLITAYVYS LHRYWWNDEH SPLGVYQYCY RAGNIELPCS QEKCSVFRPD IKVDEDYITI
TSKSQKYVFD RISGDLIHWY NASHDMIKTP IHFDIWRPLI DNYRQEYNEL WKPNFLDIMQ
LDTRSVNWKS CDDIAEVTVE QRFAPPVLSF GMKLNSRYVV NSSGVLNLEI CAEAYGSYKD
IIPRVGLTFA MPREYDNITW YGRGPGETYP DSCSSQVVGL WEASVDDMIT PYVRPQDYGN
HQNTRWVSVR NSSGVGILVT RLSSSSMTDG FSYSAWPFTS NTIEQAKHRN ELHEDDLVTI
NLNDQILGLG SNSWGSEVLD SHRIRFENCN FAFSFMPICD NATMD
//
