ID A0A0U3PI18_9ACTN Unreviewed; 972 AA.
AC A0A0U3PI18;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AS200_09940 {ECO:0000313|EMBL:ALV32322.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV32322.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV32322.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV32322.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-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}.
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DR EMBL; CP013743; ALV32322.1; -; Genomic_DNA.
DR RefSeq; WP_058922004.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3PI18; -.
DR STRING; 1725411.AS200_09940; -.
DR KEGG; scx:AS200_09940; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000068029; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT DOMAIN 716..970
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 972 AA; 106963 MW; FE790E0049240C2C CRC64;
MSDPLLALRP WEAPEVTSWG RLPMNAVDRR AGALCLDGDW RFQLLPAPGA PADGAWSSSY
VPGAWTMQGT DDLPQYTNVR MPFDDIPPHS PAAGPTGVYE RDVDVPAEWA GRRIVLQAGA
AESVLLVHVD GRPVGLSKDS HLAAEFDLTG VVRPGGRSVL RLTVVKWSDA SHIEDQDQWW
HGGLTRSVLL YATDPLHLAD VTVRARRDGE LRVDCRVRDA RGPLPDGWYV SAELDGRLLT
QDAEFDRVNA EDDRVSGFLG EARVHGFVPE VRTWNAETPE LYALTVRLHR ADGTLADASH
HRVGFRDVET AGRDLLVNGE RVYIRGVNRH DFHPLTGRTV SYDDMRADLV LLKRFGFNAI
RTSHYPNDPA LYDLADELGF YVVDEADIES HDHAHEIADD PRYLNAFVDR VSRMVLRDKN
HPSVIIWSLG NESDYGAHHD AAAGWVRRHD PTRPLQYEGA AKLDWAATDY CSDIACPMYA
PLEDCVAHAL SGRQTRPLIQ CEYSHAMGNS NGTLADHWAA IESTPGLQGG FIWEFWDHGI
LQRVNDGRPA GRGGAGLYDN GVAAPGHRWA YGGDFGETIH DGAFIADGVV FPDRTPKPAL
YEHREIAAPV RIECYRHEGI VLGNHQHFRG LDWLAGTWEL SLADGRTLTA PADLPDLRPG
ETAAVPLPFE LPRDGGEAWL TLRVTTAEDQ PWAPRGTEVC LPQVRLRGPS VAEDAVVDGS
VEVDGEGLFV HPSLTAAPTL SLWRAPTDND ELGGMAPRWR TWGLDSLVRK LVSVRADGGR
VTVDAEYAGT AGVVRHRQVF TPVEGGIRIE EEAELPEEFD DVARVGTVFE TAPGPDLLEW
FGQGPWESYP DRCAGAPVGH HSLPVDATFT PYLRPQESGG RHGVRRFTLS APDGTGLAVV
LDAPRQVSVT RYRAEDLTAA RHHDELVPRP GCVVHIDAAH RGLGTASCGP DTFPSYRVPP
GVHRWSWTLR VR
//
