ID D5EYK4_PRER2 Unreviewed; 937 AA.
AC D5EYK4;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 Name=lacZ {ECO:0000313|EMBL:ADE82782.1};
GN OrderedLocusNames=PRU_0693 {ECO:0000313|EMBL:ADE82782.1};
OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Xylanibacter.
OX NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE82782.1, ECO:0000313|Proteomes:UP000000927};
RN [1] {ECO:0000313|EMBL:ADE82782.1, ECO:0000313|Proteomes:UP000000927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG North American Consortium for Rumen Bacteria;
RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA Coutinho P.M., Henrissat B., Nelson K.E.;
RT "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT bryantii: insights into their environmental niche.";
RL Microb. Ecol. 60:721-729(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 -!- 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}.
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DR EMBL; CP002006; ADE82782.1; -; Genomic_DNA.
DR RefSeq; WP_013064768.1; NC_014033.1.
DR AlphaFoldDB; D5EYK4; -.
DR STRING; 264731.PRU_0693; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; pru:PRU_0693; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_10; -.
DR Proteomes; UP000000927; 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; 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.
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:UP000000927}.
FT DOMAIN 707..935
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 937 AA; 107545 MW; D48447B36B72498B CRC64;
MKRIFFALML ALAVDGQAQT SRDWENPAVL GINKLPYHAT LQLPSRWHEC KEIVSLDGEW
FFHWSRKPEE RPVDFYAEHF DVSAWDKIKV PGNWQTQGFG TPIYTNIDYP FKRDRPSVTS
EPPRDWTAYE NRNPVGSYVT YINVTKAMLS QNLILHFGGV HSAMYVWLNG KQVGYSQNSM
SPAEFDVTRY LHEGENKLAV EVYRWCDGSY LEDQDMWRLS GIFREVQLWV RPLVHIADYH
VTAVPNRHFS QASVTADIAV CNSGRSVAKN MKAVLKLDGH TIDGALKTLG AGDTMHVKLS
HLIDHPRLWS AEKPHLYPFS VELVDKKGNV VEHFDYHLGV KRVETVGEVF KINGKNVKLR
GVNRHDHHPI TGRYVDDTTY ETDIRLMKQA NINFLRTSHY PDREYLYELC DRWGLYVMDE
ANQESHGYGY ANEEMGHDEA WKQAHVDRAE SLVKRDFNHP CVILWSLGNE GGVGPNIQAM
YDKVCEFDST RLPFYDCHPR YSALHDFGYP APDELRSEAI KETEKPLIAR EYAHAMGNSV
GNLQEYWDVI YADSSICGAA IWDWVDQGLV KKDGDKKFWA YGGDFGDKPN LDAFCINGLL
APDRTPHPHY YEVQHVYQPL QFVLQGDSIH IINRDSFTDV SEYDITCDTI VIDGERLLNV
AAHLRQDMPW AQKGFVVASE QFVLSPYVFP KPVVTPSDSL VAGNGITIRG NALTSWMIDG
REVLQAPLEP YFWKPENDNQ HAAGFAGRVA MWKEVKDVKV RYTVLNERSI LVDVDYQPTE
TNRPIIPKLG MRMRLAADMT NIAYYGRGPW ENYPDRKRSA FLGLYQMPLS QFETEYIRPQ
DNGCRTDVRW FSISNGSNTL RIDGLQPLCI RAWDYGEENL EAARHPYEIQ RGQFVNLNID
LNIHGVGGID TWGRRTLPQY TIDGNKPYHY AFILTCI
//
