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
//