ID A0A419S561_9SPHI Unreviewed; 1089 AA.
AC A0A419S561;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 21.
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=BCY91_06915 {ECO:0000313|EMBL:RKD15236.1};
OS Pelobium manganitolerans.
OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC Sphingobacteriales; Sphingobacteriaceae; Pelobium.
OX NCBI_TaxID=1842495 {ECO:0000313|EMBL:RKD15236.1, ECO:0000313|Proteomes:UP000283433};
RN [1] {ECO:0000313|EMBL:RKD15236.1, ECO:0000313|Proteomes:UP000283433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YS-25 {ECO:0000313|EMBL:RKD15236.1,
RC ECO:0000313|Proteomes:UP000283433};
RA Wu S., Wang G.;
RT "Genome of Pelobium manganitolerans.";
RL Submitted (JUL-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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:RKD15236.1}.
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DR EMBL; MBTA01000025; RKD15236.1; -; Genomic_DNA.
DR RefSeq; WP_120182188.1; NZ_MBTA01000025.1.
DR AlphaFoldDB; A0A419S561; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000283433; 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:0005990; P:lactose catabolic process; IEA:TreeGrafter.
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; IPR050347; Bact_Beta-galactosidase.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; GH.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR006102; Ig-like_GH2.
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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000283433};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1089
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019007211"
FT DOMAIN 807..1071
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1089 AA; 123160 MW; 001126175F2CCA92 CRC64;
MKALKISLAL LFSATFGLAQ TVDGLPAAIP MVPGIYNTPP WEVPQITEIN RDKARSTSYS
YASVEDALNG DRSKSRMLLL NGDWDFKFAF KPADAPQDFY KQKVSGWDKI EVPSNWELKG
YDIPIYKSAV FPFRPVNPPF VPQDYNGVGS YQRSFTLPAN WKDMNITLHF GGVSSAFRVW
LNGKFLGYGE DSCLPSEFNA TAYLKEGENV VSVQVIRWND GSYLEDQDHW RMSGIQREVM
LLAEPKIRIA DFHYQTKLDK QYKDAIFSLR PRLDNFTGKF IPEGYEVKAQ LYDDSNRAVF
AKPLQRSAES IVNEIYPRLD NVKFGLLETE VKNPKKWSDE APNLYTLVIS LVDDKGNLLE
AKSCKVGFRS IEFSKENGKM LINGKVTYIY GVNRHDHDPV KGKALSRADI ERDVKTLKQF
NFNLIRTSHY PNDPYFYELC DKYGMMVMDE ANYETHGLGG KLSNDPSWTG AFMERTSRMV
LRDKNHPSVV IWSLGNEAGR GPNNAAMAAW IHDFDITRPV HYEPAMGSPK EEGYIDPSDP
RYPKSVDHAH RLQNPVDQYY VDMVSRFYPG IFTPDLLLNQ ANGDKRPILF VEYSHSMGNS
TGNMKEFWDI FRSRDRLIGG CIWDFKDQGL LKKDSAGKEF FAYGGDFGDK PNDGNFCING
IVASDGRPKA AIYECKHVYQ PAETQWKNQQ AGVLEIENRH ASKNLEDYDL FLSFLENGKV
IKSLQIPSVA VAAGEKKELN IRKYYPNLKT GNEYLLNISF KLKNNLPWAA KGHEVAYNQL
PLTSVLEGIK ISEKPVTVAQ KSASGLSLKG TDFQITFTNG ALSSYIKNGK ELVKSPFLPH
FTRPQTDNDR KGWKPAKKLK QWYNAVPELT DFKEIKAGSV YQANYQIIKD SASVSLTYHI
DADGGLKVDY ALTANQALPN IPKVGMQGAI ANDLQNIAFY GKGPQENYID RAFGFDAGLY
QLDIKNFVEP YVYPQENGNR TDVRWMAFTN KQNGIMVVAD SLLSMSAWPW TEANINKAKH
TNELSEAGFV TLNVDLKQMG IGGNDTWSDV SQPLPQYQIK AGNYKYSFYI KPVASAQTEK
LMAIYKKLK
//
