ID A0A4R5MJK1_9SPHI Unreviewed; 1045 AA.
AC A0A4R5MJK1;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 21.
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 ORFNames=EZJ43_13765 {ECO:0000313|EMBL:TDG35365.1};
OS Pedobacter changchengzhani.
OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC Sphingobacteriales; Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=2529274 {ECO:0000313|EMBL:TDG35365.1, ECO:0000313|Proteomes:UP000295668};
RN [1] {ECO:0000313|EMBL:TDG35365.1, ECO:0000313|Proteomes:UP000295668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E01020 {ECO:0000313|EMBL:TDG35365.1,
RC ECO:0000313|Proteomes:UP000295668};
RA He R.-H.;
RT "Pedobacter sp. nov., a novel speices isolated from soil of pinguins
RT habitat in Antarcitica.";
RL Submitted (FEB-2019) 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 -!- 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}.
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:TDG35365.1}.
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DR EMBL; SJCY01000010; TDG35365.1; -; Genomic_DNA.
DR RefSeq; WP_133263295.1; NZ_SJCY01000010.1.
DR AlphaFoldDB; A0A4R5MJK1; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000295668; 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 FunFam; 3.20.20.80:FF:000121; Beta-galactosidase; 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; 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; 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; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000295668};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1045
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020292619"
FT DOMAIN 759..1034
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1045 AA; 119149 MW; 5460F5B4A858FF41 CRC64;
MKIKLVLVVL FANILSLNAQ VNDWENPSLV SIGMENAHVT FMPFDNQKDA ISNDYARSKD
FKSLNGNWKF NYVDQYKDRP TTFASADFDD SGWADLKVPS NWELNGFGVP IYTNIVYPFP
KNPPFIGPNN PVGTYRKSFI IPENWNQKEV ILHFGSITGA AFVYLNGKKI GLSKASKTPI
EFNITKHLKK GENKLSVQVF RWHDGSYLED QDFWRLSGIE RDTYLFALPK LSIWDFFLKG
DLDVAYKNGL FSAAIDIRKF VGNDIKNASV SVSLTNKVGK TIYDKTQNFT VNKDSIQTLN
FSGTINNPLK WNAENPNLYD CVITLKDHAG KVLFITSNKV GFRKVEIKNA RLLVNGVPIS
VHGVNRHEHD EVTGHTTTKE LMLKDIKLMK EFNINSVRLS HYPNDPLWYK LCDEYGLYLV
DEANIETHGM GAEFQGRIDK SRHPAYLPEW APAHLNRTVR MVERDKNHPS IIIWSLGNEC
GNGPVFHDNY KWIKNRDNTR PVQFEQAGDD WNTDIVAPMY PSIDNMKKYA ADESKTRPYI
MCEYAHAMGN SSGNFKTYFE IMRKSKNMQG GFIWDWVDQG IKTKDANNKS FWAYGGDLGG
FYLQNDENFC ANGLISADRT PHPGAYEVKN VYQPIIITAK DLNKGILEIE NIYDFTNLKA
CNFKWELLKN GEKVNEGTFE VNLNPHQIKD VQLNLPKYKS IAGTEIYLNI YATTKNETPL
LPANFEVAKA QFKYAGDYFA KDEAIVTSLI INQLNDQIKF TAGNVKGEFN IKTGRISGYS
NGENKFSNFL EPYFWRAPTD NDFGNEMPSK LGVWRSAHLN KQLKDVKVGV QNAQGLSIDV
TWLLANINVP YHINYLILND GSIKVTGSMD FSNTQLPELP RFGMRTTLSN WYTDLNYYGR
GPFENYIDRQ DASFIGIYKD KIENQYFKDY IRPQESGNKT DVRWLTLTNN KGMGIKIEGA
QPLGFSAINH STEDLDPGLT KKQQHPTDLK PRDEVFLNVD LKQRGLGGDD SWGALPHQEF
QLLDKKYSYS YTISLIDGTA DKKEK
//
