ID A0A0R1X3L3_9LACO Unreviewed; 649 AA.
AC A0A0R1X3L3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=FD32_GL001203 {ECO:0000313|EMBL:KRM24847.1};
OS Limosilactobacillus panis DSM 6035.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423782 {ECO:0000313|EMBL:KRM24847.1, ECO:0000313|Proteomes:UP000051412};
RN [1] {ECO:0000313|EMBL:KRM24847.1, ECO:0000313|Proteomes:UP000051412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6035 {ECO:0000313|EMBL:KRM24847.1,
RC ECO:0000313|Proteomes:UP000051412};
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:KRM24847.1}.
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DR EMBL; AZGM01000142; KRM24847.1; -; Genomic_DNA.
DR RefSeq; WP_047768171.1; NZ_LDPB01000054.1.
DR AlphaFoldDB; A0A0R1X3L3; -.
DR STRING; 1423782.FD32_GL001203; -.
DR PATRIC; fig|1423782.4.peg.1254; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000051412; 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:UP000051412}.
FT DOMAIN 45..227
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 229..331
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 338..646
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 649 AA; 75349 MW; 50C72D7592BE26CA CRC64;
MDADIKWLDD PETFRVNQLP AHSDHHYYGN YAEWGQGQSR FAQLLNGQWQ FKFAQNPHER
QKNFYQVDLD CADFAQIEVP SEIELSDYAQ NNYINTLIPW EGKIYRRPAY AVDGKNKEEG
SFSTGEDNTV GMYRKEFDLA PELRGKEVRV HFEGVERSMY LWLNGHFVGY AEDSFTPSEF
DLTPYIQDEG NVMAVEVFKH STASWIEDQD MFRFSGIFRS VELLAQPVTH LEDMTIRPTV
DDGYQNGRLN LDLQLAGEQE GTVHVLVKDE DGNVVVDQTK SVAEQVAIDD VALKNVHLWD
NHHPYLYQLF VEIRNEAGQL VELVPYRFGF RRIEINANHV VLLNGQRLII NGVNRHEWDD
QRGRSVTMAD MEKDIQTFKE NNINAVRTCH YPDQLPWYQL CDEHGIYMMA ENSLESHATW
QKMGKVDPSY NVPGSVPQWK KVVVDRARTN YETFKNHPAI LFWSLGNESF AGDNIAAMGR
FYKEHDDSRL VHYEGVCHTH DYSKQIPSLK KESYLPAGGT KDYRDQISDV ESWMYLPPKQ
VEEYLQNNPD KPFMECEYMH DMGNSDGGMG SYIKLLDKYP QYFGGFIWDF IDQALQVKDP
VSGKMVMRYG GDFDDRHSDY EFSGDGLMFA DRTPKPAMQE VRYYYGLHK
//
