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Database: UniProt
Entry: A0A0R1UMN1_9LACO
LinkDB: A0A0R1UMN1_9LACO
Original site: A0A0R1UMN1_9LACO 
ID   A0A0R1UMN1_9LACO        Unreviewed;       626 AA.
AC   A0A0R1UMN1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=FC21_GL000220 {ECO:0000313|EMBL:KRL92627.1};
OS   Limosilactobacillus equigenerosi DSM 18793 = JCM 14505.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=1423742 {ECO:0000313|EMBL:KRL92627.1, ECO:0000313|Proteomes:UP000051084};
RN   [1] {ECO:0000313|EMBL:KRL92627.1, ECO:0000313|Proteomes:UP000051084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18793 {ECO:0000313|EMBL:KRL92627.1,
RC   ECO:0000313|Proteomes:UP000051084};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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   -!- 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:KRL92627.1}.
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DR   EMBL; AZGC01000053; KRL92627.1; -; Genomic_DNA.
DR   RefSeq; WP_056995781.1; NZ_AZGC01000053.1.
DR   AlphaFoldDB; A0A0R1UMN1; -.
DR   STRING; 417373.GCA_001570685_01135; -.
DR   PATRIC; fig|1423742.4.peg.232; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000051084; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; 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   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 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:UP000051084}.
FT   DOMAIN          43..227
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          229..329
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          337..623
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   626 AA;  71328 MW;  BB4C717DCD902D1B CRC64;
     MEAQLAWLDD PQVFRVNQLP AHSDHQFFAS TAAMEAGDNE LVQSLNGTWE FAFAPTPAQR
     PVGFWEPTFN RAGFTTITVP GEIELQGFSQ INYINTLYPW AGKTYRRPVG TAVADQVDPA
     TFANGNDNTV GAYVRHFELP NHWADREVHI MFEGVERAMY VWLNGHFVGY AEDSFTPSEF
     DLTPYLQPGD NLLAVEVFKH STASWLEDQD MFRFSGIFRD VNLVCLPTAH VTDLKVEALY
     DPVTHEGQFG ATLQLTNDQA VVSAQLTAPD GTIVWDGQTD QSQDFKFPVT EIGVVQAWDH
     HHPTLYQLTL TVQMGAKTVE VIPQVVGFRH VEITPEAVLQ LNGQRLVING VNRHEWNCHR
     GRAIEYQDML TDLELFHQNN INAVRTCHYP DQLAWYDLCD RHGIYMMAEN NLETHGTWQK
     MGAVEPSYNV PGSLNEWLEA CLDRARTNYE VLKNHPAILF WSLGNESYAG EVIAAMDQFY
     HTHDQTRLTH YEGVCYTPEY RDRISDFESR MYLAPDDVEA YLQNQPDKPF VECEYMHSMG
     NSVGGLGSYN RLVDEYPQYA GGFIWDFIDQ ALEITDPVTG QSVMRYGGDF DDRHADYEFA
     GDGLVFANRQ PKPAMQEVRY YYGLHE
//
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