ID A8LFM6_FRASN Unreviewed; 1017 AA.
AC A8LFM6;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 ORFNames=Franean1_3257 {ECO:0000313|EMBL:ABW12663.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW12663.1};
RN [1] {ECO:0000313|EMBL:ABW12663.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW12663.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT "Complete sequence of Frankia sp. EAN1pec.";
RL Submitted (AUG-2007) 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|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU361154};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; CP000820; ABW12663.1; -; Genomic_DNA.
DR AlphaFoldDB; A8LFM6; -.
DR STRING; 298653.Franean1_3257; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; fre:Franean1_3257; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_11; -.
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; 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 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.
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}.
FT DOMAIN 759..1008
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1017 AA; 111492 MW; 2B03392DD0F768C0 CRC64;
MTGTDFTAVP WEDSGFQALG RLPMHSIRRP AEVELDGVWD FQLLDSPTAP PGAEWKRADV
PGLWTMSEAG DPAHYTNVRM PFDETPPRIP ARNPTGVYRR SFELRPAAGR RAILHVGAAE
GLLRVFVNGR AIGVSTDSHL AAEFDITEAC VAGGRDRHTV ELVISKWSSV SYLEDQDHWW
QSGITRSVYV YTLPEIRLAD LAVVADFDPE ARRGTLRLEV STAGLDHLPE LAWTVRVDVL
GRRSTLPVTP CSPAPGLPPP WDDRSVRPEP RVPADFMSLV SQIAADAPIP PRWSAAVPSL
RRSLAPRRPA GTATLHLDGL EVEPWSAESP HLEDLVVALV SPGGEVVDET RTRIGFRRVR
IEGRDLLVNG GRILIQGVNR HDTDARTGRV LSARTMLAEL SLLKRFNVNA IRTSHYPNDP
RLLELCDELG FYVVDEADIE AHAFANAICD DPRYLPAFLD RVSRMTLRDR NHPSVIVWSL
GNETGYGANH DAAAGWLRRF DPTRPLHYEG AIALDWHGGR AATDIVCPMY PSFEALAAFS
ADPRADRPVI LCEYAYSQGN STGGLAEYWE MFETLPGLQG GFIWEFKDHS LDPAGDGGYR
YGGDFGDVPH DGATLVNGIV FPDLTPQPAL YEARGLFSPV RIVSDAAAAL AGAIGIRNRQ
SFNDLSAYVL ELQVENDRST DPVTVDVPDV APGATGTIEL PDPIRKLLGS APPLALTLTV
RTRQGARWAP AGTVVAAHQI TFPRPPVALL SAPVPDALRV DQDGSVVHPL LRRAPALCLW
RAVTDNDKSF SLDQRFVRSG FFRLTPGAVT AEADGGSLTI TTAYATAFGT EVTHRRVISA
LAEHDYRFDE HVQLPADTED ALRVGVEFEL TPGFDDARWV GLGPWENYPD RRSSALLGSW
RERIDDLAVP YLVPQENGGR GAVSELCLSG PAGTVRTFHP TPVQMAVGRH RVDQLEAAAH
WWELPPSDVT VVHLDVAHRG VGTAQLGPDT RPRHRLTDHE YTWTWRLRLE SAAGAAV
//
