ID A0A1D2IJJ0_9ACTN Unreviewed; 967 AA.
AC A0A1D2IJJ0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN Name=lacZ {ECO:0000313|EMBL:ODA74678.1};
GN ORFNames=APS67_000867 {ECO:0000313|EMBL:ODA74678.1};
OS Streptomyces sp. AVP053U2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1737066 {ECO:0000313|EMBL:ODA74678.1, ECO:0000313|Proteomes:UP000054731};
RN [1] {ECO:0000313|EMBL:ODA74678.1, ECO:0000313|Proteomes:UP000054731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AVP053U2 {ECO:0000313|EMBL:ODA74678.1,
RC ECO:0000313|Proteomes:UP000054731};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-2016) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:ODA74678.1}.
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DR EMBL; LMTQ02000004; ODA74678.1; -; Genomic_DNA.
DR RefSeq; WP_062192542.1; NZ_LMTQ02000004.1.
DR AlphaFoldDB; A0A1D2IJJ0; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000054731; 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; 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; 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:0000313|EMBL:ODA74678.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ODA74678.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054731}.
FT DOMAIN 701..961
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 106043 MW; 6819D3C7FCE8A7EA CRC64;
MSLHTRTTAT DYVEDVSPGR GTLPPRARHA SSDAASLSLN GRWRLRLSAT ADAEDDAFGV
PGYDAGDWAE VTVPGHWVLQ GDGAFGAPAY TNHLYPFPVD PPYVPTENPT GDHLRVFDLP
KGWPARAEGD EAVLRFDGVE SCARVWLNGT DIGEFKGSRL PHEFAVGALL KPAGNVLAVR
VHQWSAGSYL EDQDQWWLPG IFRDVTLLHR PAGCVGDFFV HASYDHVTGE GTLRVDVDTD
SGAGGRVTVP ELGVDIATGE SVTLPVDPWS AEIPRLYEGV LATSGERVPL RVGFRTVALE
DGLLKVNGRA VLFKGVNRHE WHPERGRALD VDTMREDVLL MKRHNINAVR TSHYPPHPAF
LDLCDEYGLW VVDECDLETH GFVEQGWRDN PTDDERWTPA LLDRAARMVE RDKNHPSVVM
WSLGNEAGTG RGLTAMADWI RSRDPARPVH YEGDVDCRDT DVYSRMYPPH AEVERIARGL
DGGSRRRRRL PLILCEYAHA MGNGPGGLAD YQSLFERYDR LQGGFVWEWI DHGVRHPELG
YAYGGDFGEE LHDGNFVCDG LLFPDRTPSP GLVEYKKVIE PVRIEAGEAD GTVRVTNRYD
FAGLSHLEFE SSYLVDGRPA GACRLTVPAL APGRSAEVEL PGAPDGKGEE VQWTVRALLA
DDTAWADRGH EVAWAQRTVA PRAPAAAAAG VRPAVGGDGI TLGPASFDAR TGVVRTIAGV
PVSGLRLDVW RATTDNDDGA PWQPDTRYGP LWRELGLHRM RHRTVAVGTD GDALVVRTRV
ASAGRETGLR AAYRWTSDGR HVRLTVSVVP EGDWRVPLPR LGIRFGLEGS PEDAVSWFGG
GGEAYPDTRA ASRDLRWDAS VEDLQTPYVR PQENGARADV RWVELGGLRI EGEPGFWFTA
RPWTTEQLDA ARHLTDLVPG GTVWVNLDHA QHGIGSQSCG PGPLPRYVLR AEPAEFSFVF
SAQPGSG
//
