ID A0A0N1FRT3_9ACTN Unreviewed; 994 AA.
AC A0A0N1FRT3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=OK006_7840 {ECO:0000313|EMBL:KPI01992.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI01992.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI01992.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI01992.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-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:KPI01992.1}.
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DR EMBL; LJCU01000255; KPI01992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1FRT3; -.
DR PATRIC; fig|1592326.3.peg.9755; -.
DR Proteomes; UP000037912; 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 708..992
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 737..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 109419 MW; 9146FD34411CB7C5 CRC64;
MPSELSAYVS DPTPGRGALR PARSWLHSDA PSLSLNGAWR FRLSPTASTA QDFAAEEFDD
HAWESIPVPS HWVLEGDGTH GRPIYTNIQF PFPIDPPHVP DENPTGDYRR HFALPADWSD
AERIVLRFDG VESLFRVWVN GVDIGSAGGS RLAHEFDVTR AVRPGDNVVA VRVHQWSAAS
YVEDQDQWWL PGIFRDVTLT ARPLGGIEDV WLRTGFRDGR GRVEAEITAE ASAFPVTLRI
PELGVEQVWA TAADVTPVDA GEVEPWSAEG PHLYDATVST AAESIALRVG FRTVEIRGDR
FLVNGRRVVF HGVNRHEAHP VRGRVFDEEH AREDLARMKR FNVNAIRTSH YPPHPRLLDL
ADELGFWVVL ECDLETHGFE KLGWVGNPSD DPAWREAYLD RIRRTVERDK NHPSIVIWSL
GNESGTGSNL AAMSAWVHAR DAERPVHYEG DYTGEYTDVY SRMYASVQET ERIGTDGTDT
PLLNCTPAQS ARQRAKPFLL CEYAHAMGNG PGALDQYEAL VHEHPRLHGG FVWEWRDHGI
LATAPDGTAY QAYGGDFGEV VHDGNFVMDG MLLSDDVPTP SLYEYKAVVQ PVRFVFDGDK
VAVTNLRHSA DTSDLRFRWR VEQDGAPVDA GDLEAPVVAA GESGRGSLPP VPVAPEGETW
LTIDAVLATA APWAPEGHVV ATVQSDRSPH IPVPAVRHRT GWRPDTGTLT LGAAAFVDGR
LVSLAGRAVT GPRLELFRAP TDNDESPSDG VEESDASVPG VSNAELWRRD GLDRLTARRV
SVERPHDKAD ALRTLDKVSA ANSALFVMVE SVWSLEAGEL ELRVEIEPSR GWSTVWPRIG
IRFDLPDGGA PVDGAEWFGL GPSESYPDSL RAARTGRFSF GIDDLSVDYA RPQETGHRSG
LRRLTLTSSG AKVFRVEALP DTHGRRPGFT LSRHTPQELA RAGHPYELPA STTSRLTIDA
AQHGLGSRSC GPDVRPEFAL RPEARTIRLR ITAG
//
