ID A0A101N723_9ACTN Unreviewed; 982 AA.
AC A0A101N723;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AQI94_16025 {ECO:0000313|EMBL:KUM87789.1};
OS Streptomyces pseudovenezuelae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM87789.1, ECO:0000313|Proteomes:UP000053039};
RN [1] {ECO:0000313|EMBL:KUM87789.1, ECO:0000313|Proteomes:UP000053039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM87789.1,
RC ECO:0000313|Proteomes:UP000053039};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT strain for the species Streptomyces pseudovenezuelae.";
RL Submitted (OCT-2015) 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}.
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:KUM87789.1}.
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DR EMBL; LMWM01000014; KUM87789.1; -; Genomic_DNA.
DR RefSeq; WP_031046395.1; NZ_KQ948146.1.
DR AlphaFoldDB; A0A101N723; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000053039; Unassembled WGS sequence.
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 725..980
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 982 AA; 108069 MW; C97EC4BE671BB073 CRC64;
MTDAPRGPRP TDPLLALRPW DAPEVTSWGR LPMNAVDRRS GALPLDGDWR FQLLPTPDAP
VGGSWSTIHV PGVWTMQGTD DLPQYLNVRM PFPEFPPHSP AANPTGVYER AVDVPADWAG
RRVVLQVGAA ESVLLVHVDG RPVGVSKDSH LAAEFDLTGL VRAGERAVVR LTVVKWSDAS
HIEDQDQWWH GGITRSVLLY ATDPLHLSDV TVRASFDGSL RVDCQVRDAG GALPEGWYVS
GELEGRPLGQ DTEFDRFNRE DDRVSDFLGE ARIRTTVEDV RTWNAETPEL YDLTVRLHRA
DGTVSDTSRH RIGFRDVEIA GRDLLVNGER VFVRGVNRHD FHPLTGRTVS YDDMRADLVT
LKRFGFNAIR TSHYPGDPSL YDLADELGLY VVDEADIESH DHAHEIADDP RYLNAFVDRL
SRMVLRDKNH PSVIVWSLGN ESDYGANHDA AAGWVRRHDP TRPVQYEGAA KLDWAAAGDA
TDIACPMYAS LEECVAHALS GRQTKPLIWC EYSHAMGNSN GTLADHWAAI ESTPGLQGGF
IWEFWDHGIL QRVNDGRPVG RGGVGLYDNG VAAPGHRWAY GGDFGEALHD GAFIADGVVL
PDRTPKPVMY EHREIAAPVR IECFRHEGIV LGNHQHFRGL AWLAGEWELS LADGRTLTAP
AELPDLRPGE TAAVPLPFDL PEDGGEAWLT LRVTTARDEP WAPRGTVVCV PQVRLREAAP
QTPAIVRNRS VKVDDDGLLV HPLLTAAPTL SLWRAPTDND ELGGMAARWR GWGLDVLVRK
VAHIRQTSGR VTVRAEYACE AGVVRHVQVL TAVEGGIHVE ESAELPDELD DVARVGSVFE
TVAGLDLMEW YGQGPWESYP DRGFGAPVGH HAVPVDELFT PYLRPQESGG RHGVRHFTLS
ARDATDLAVA LDEPRQVCVT RYRAADLTAV AHHDELVPGA GCVVHIDAAH RGLGTASCGP
DTFASYRVPP GVHRWSWTLR AL
//
