ID A0A224XBX5_9LACT Unreviewed; 616 AA.
AC A0A224XBX5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN ORFNames=RsY01_725 {ECO:0000313|EMBL:GAX47143.1};
OS Lactococcus reticulitermitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=2025039 {ECO:0000313|EMBL:GAX47143.1, ECO:0000313|Proteomes:UP000218689};
RN [1] {ECO:0000313|Proteomes:UP000218689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs-Y01 {ECO:0000313|Proteomes:UP000218689};
RA Ohkuma M., Yuki M.;
RT "Draft genome sequence of Lactococcus sp. strain Rs-Y01, isolated from the
RT gut of the lower termite Reticulitermes speratus.";
RL Submitted (AUG-2017) 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|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:GAX47143.1}.
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DR EMBL; BEDT01000001; GAX47143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A224XBX5; -.
DR Proteomes; UP000218689; 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; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Reference proteome {ECO:0000313|Proteomes:UP000218689}.
FT DOMAIN 32..352
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 397..513
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 533..591
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 180
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 616 AA; 69823 MW; 8A1C5F8DECD86F7B CRC64;
MASCCVNSSL ILINIEVLDE EDVVKSFQIE EEFLLDGQPI KIISGAIHYF RIPTNQWEDS
LYNLKALGAN TVETYIPWNI HEPAEGIFDF SGMKDIVSFV KLAQSLGLMV ILRPSAYICA
EWEFGGLPAW LLKTPKIRLR STDKVFMAKV EAYFKELLPK LLPLQITQGG PVIMMQIENE
YGSYGMEKEY LRQTKQIMEK YGVVVPLFTS DGAWEAALEA GSLIEDDVLV TGNFGSHSKE
NVAALVQFMA KHGKKWPVMC MEYWDGWFNR WGEPIIKRDP KDLAQEVKEM LELGSLNLYM
FHGGTNFGFY NGCSARETGS MPQITSYDYD ALLTESGEPT EKYDLVQKAI KEVCPEVWQA
APRRKQVKYL GNFKVAQSVS LLNTKKTLTQ SIASSYPLAM EEVGTGYGYM LYSVALRNNQ
SEQKLKLVEA DDRIQIYLDG EYQATQYQSE IGQELLVGHE KATESITADF LVENLGRVNY
GFKFNHSSQS KGIKGGIMQD IHFHQGYQHY PLDFSKEQLA EIDYSAGRNV KQPSFYKVIF
ELPEVSDTFI DCSAYGKGVV IVNGVNLGRY WQEGPTYSLY CPKDFLRVGE NEVVIFETEG
VEVKKLVFSE IPIFKH
//
