ID A0A1B8TUR8_9FLAO Unreviewed; 951 AA.
AC A0A1B8TUR8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=LPB301_11370 {ECO:0000313|EMBL:OBY63413.1};
OS Polaribacter reichenbachii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=996801 {ECO:0000313|EMBL:OBY63413.1, ECO:0000313|Proteomes:UP000092612};
RN [1] {ECO:0000313|Proteomes:UP000092612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 23969 {ECO:0000313|Proteomes:UP000092612};
RA Shin S.-K., Yi H.;
RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL Submitted (FEB-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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:OBY63413.1}.
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DR EMBL; LSFL01000035; OBY63413.1; -; Genomic_DNA.
DR RefSeq; WP_068361785.1; NZ_VRMM01000054.1.
DR AlphaFoldDB; A0A1B8TUR8; -.
DR STRING; 996801.BW723_04340; -.
DR KEGG; prn:BW723_04340; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000092612; Unassembled WGS sequence.
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; 1.
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; IPR006103; Glyco_hydro_2_cat.
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 PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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 PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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:UP000092612};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..951
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008615591"
FT DOMAIN 66..196
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 209..301
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 307..523
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT REGION 921..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 951 AA; 108923 MW; AC2199166CB93C13 CRC64;
MQKFKNLLIA FVFTSSMPFY AQNAVIDANL KSDLQTEIQY LSGTDKDNLV DWDFWISEGR
KSGKWTTIGV PSCWEQQGFG AYNYGQDKED NRAQEYGLYK YTFNAPKNWK NKNINIVFEG
VMTDAEVKIN GKLAGEIHQG AFYEFKYAIT DLLKYGKQNI LEVKVHKVSA NESINHAERN
ADFWIFGGIY RPVYLEILPK ENIERVAIDA KANGIINADI FTTSKKVHAI AATLSNVNGQ
VIENLKIDKS FKEEGRWHIT TKANNVKTWN PEFPNLYVLH IKILDKQNKI LHKISETIGF
RTVEVLEGDG IYVNGKRIKF KGVNRHSFHP KSGRTTSKSW SLEQALQIKD MNMNAVRMAH
YPPDKHFLQV CDSLGLFVIN EICTWHNPTL DTKVARKIVK ETVVRDVNHP SIVLWANGNE
QGWNTEVDDD YAKWDIQKRE VIHPWSIYKK TNTIHYSHYH SLINDAYSKD KILFPTEFLH
GLYDGGHGAG LDDYWNIMWN LPLSAGGFLW DFADEGIERT DKNNEIDLDG NHAPDGIVGP
YGEKEGSYFT IKEVWSPIYI EDRFIKEDFN GIFRIENRYH YTNLDKCTMT AKWIKFNGPK
DNKNATILNT TKVDLPNLAP ITKGQFTVDK PKNWKEADAL YLTAVNQYGK EIFTWSYPVS
IPKKANSSQI DVAEKGSIST KTENEFIKVE ANGISYLFSE KTGLLQEVKK GNTTIPLKDG
PIILNQKDKI KSITVNSSEE KVEILVVFEE GKWSPGWSTL KEYRSDIIKW TVNANGLLDV
KVEFKGYRNL KGFRGITFSF PETQVAGMKW LGDGPYRVWR NRMKGTEFNV WENDYNNTIT
GHSGFVYPEF KGFFSNLYWA KIKGNNNNGF TVYCNSPQVY LRMLTPENAP DTRKGRLDPK
FPKGDISFVM NIPAIGTKFQ KPESTGPHGN PEHYFGNDDN PITIDLTFDF N
//