ID A0A1I4YWD3_9ACTN Unreviewed; 1325 AA.
AC A0A1I4YWD3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN04487980_1019139 {ECO:0000313|EMBL:SFN42366.1};
OS Streptomyces sp. cf124.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFN42366.1, ECO:0000313|Proteomes:UP000198530};
RN [1] {ECO:0000313|EMBL:SFN42366.1, ECO:0000313|Proteomes:UP000198530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF124 {ECO:0000313|EMBL:SFN42366.1,
RC ECO:0000313|Proteomes:UP000198530};
RA de Groot N.N.;
RL Submitted (OCT-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 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; FOUV01000019; SFN42366.1; -; Genomic_DNA.
DR Proteomes; UP000198530; 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; 2.60.120.200; -; 1.
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; 2.
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; IPR013320; ConA-like_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 InterPro; IPR006558; LamG-like.
DR InterPro; IPR006311; TAT_signal.
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; 2.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
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.
DR PROSITE; PS51318; TAT; 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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 678..809
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 1032..1306
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 767..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 146465 MW; B7141BCA5A5096C1 CRC64;
MQHPHPQPPP QPHPGTPAVR PVVSRRRLLE GGAALLGALA LSGGDAYAAP RSGTADADSP
EWSGNMALFQ VGAEPPHTTL MPYADVRQAL AGDRTRSPYR LSLDGTWKFA YVDRPGDRDE
DFYRTDLDDS GWDTIPVPSN WQLHGYDFPI YINITYPWWG PNGLGEEAQP PTAPTRYNPV
GQYRRTFHLP KDWTAGDRRT FLHFEGVKSA HYVWINGQLV GYHEDSYDPA EYDITKHLKP
GKNRIAVEVY RYSDGDWLED QDMIRLSGIF RSVYLYSTPA VHLRDFRLDT PLGDGYTSAE
LSVTASVRAY AAGHAGAYSV ETQLYDARGH AVWSRPLVQS VAVGASTTGE DVTVQAKKSV
PSPELWSAEH PTLYTAVLRL RDPRGKVVET LSHRVGLREF ALKDGLMRIN GKPVSLRGTN
RHEMHPDRGM ALTRADLVKD MGIIKRLNMN TVRTSHYPNN PLWYELADEY GLYLVDETNL
ETHGIRDRFP GNDPDWSKAC VARAQAMVHR DKNHASVVIW SLGNEAGGGS TFVAMRDWIE
SYDKTRVIQY EGDDRPTISQ IRSEMYDSPQ RVEQRAKDTS DTRPYVMIEY SHSMGNSTGN
FKKYWDLIRR YPVLQGGWIW DFVDQSLTWP VPRLRVFTDA GPSALKGQLL TAAGTFSRSK
GLSGATGFTR DPALDLTGSL TLEAWITPHV TGGHQPLVAK GDTQYALKQT NNSVEFFIYG
GGQWVSVSWN LPADGWTGRE HHVAGVFDAE AGSLTLYVDG EAKATRTTTR RPSVNTAPLS
LGTDTDNPTR EFSGTIRRAG VYARALSGAE LASGGRGPGD DGVRFWFDAA TVEVGERKRE
GFAKERSFFA YGGDWGDNPN DGAFVADGIV KADRGHTGKA AEVKRIYQAI HATPATGAAT
DALTSRKITL TNEYLFTNLR EFDGSWTLVA DGKEIQRGRL TRAQLDVGPL STKDITVPFR
LPSSPAPGTE YFLELSFTTK ERTPWAKSGF EVARQQLPVD AGSPAVAPAP LATVPKLTYT
DGPKEIKVSG KGVKGRGFSV TVDRESGVLT SYKSAGTRLL TSGPVPNFWR APTDNDHGNG
QHTRNQTWRD AGANRKVTEV TVRALGDGRA VEIKVTGTLP TTTESSYSTT YTVFGNGEIK
VDNTLHPGAA SLPYIPEVGT LLHLPRRLDR LHYYGRGPEE NHWDRNNGTD VGLHSGGVAD
QWSGYIRPQE NGNKTDIRWA ALTDRDGEGL LISGDSLIEV NASFFTPEDL STGLRHDYHL
TPRDTVVLRV NHRQMGVGGD NSWGAHTHDE YKLFAGRDYA YTYRLRPLTD VDLATKLSRR
PTATE
//
