ID A0A2G0CAV2_9BACT Unreviewed; 1044 AA.
AC A0A2G0CAV2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CGL56_17585 {ECO:0000313|EMBL:PHK97093.1};
OS Neolewinella marina.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC Neolewinella.
OX NCBI_TaxID=438751 {ECO:0000313|EMBL:PHK97093.1, ECO:0000313|Proteomes:UP000226437};
RN [1] {ECO:0000313|EMBL:PHK97093.1, ECO:0000313|Proteomes:UP000226437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKG-38 {ECO:0000313|EMBL:PHK97093.1,
RC ECO:0000313|Proteomes:UP000226437};
RA Wang K.;
RT "The draft genome sequence of Lewinella marina KCTC 32374.";
RL Submitted (OCT-2017) 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 -!- 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:PHK97093.1}.
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DR EMBL; PDLO01000013; PHK97093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G0CAV2; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000226437; 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; 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.
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:UP000226437}.
FT DOMAIN 765..1041
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1044 AA; 117919 MW; 2D4C10726D2FB907 CRC64;
MRLVFSVLVC LVLLPIVLSA QTLREWEDPE VYQINREYPH AAFYRYASPE AARAQVPYEQ
SPFYRSLNGS WKFNWVPTPS DRPVYFYQPD FDVSAWADIP VPANWELEGH GTPIYTNITY
PFPANPPFID HDHNPVGSYR RNFTVPADWA GQEIYLHFGG VSSAFYVWVN GERVGYSEGS
KTPAEFRITH YLRPGENTLA VEVYRWSDGS YLEDQDFWRL SGIDRDVYLY ATPKVTLRDF
RVVASLDTIA YRDGDFHLEL EYRNTTGTVS DAYRVEATLL EGERPVLEFN RPLRVPVGGG
AVEFSGTVPA ARPWTAETPN LYTLVITLRD SVGRAVESTS SRVGFRTIEI RDNQFLVNGV
PVYLKGVNLH DHDPATGHVI SEELTRQDMQ RMKEFNINAI RCSHYPKNEF FYRMCDEYGF
YVVDEANIET HGMGTTNQGL DDDFQRQAIH PAYLPEWRAA HLDRTVRMYE RDKNFPSIVT
WSLGNEAGNG ENFYVTYQWL KKVDPTRPVQ YEGATQYENT DIQAPMYARI PDLIAYAEDD
PQRPLILCEY AHAMGNSVGN LQDYWDVIER YDVLQGGFIW DWVDQGLDAT TPDGVTYYAY
GGDLGGQYLQ NDRNFNLNGL VSPDRSPHPA LHEVKQVYQY IKFPDYDPVA GRLTLYNGYD
FISLDRFALS WSLLADGEEV ASGDLPPTAL AARRDTTLAL ELPARETGQE YYLRVQARLK
EAEPLLASGH VVARAEFPLS KPHFARLTAT PGNSPEVEEG PETVTLSGED FTAAFDKETG
LLYRLDYGAG NLLVSPLKPN FWRAPTDNDY GYGMPREAKV WKKASQEPVL KSFTVDPAEN
GLQCLTAEYD LPGTGGTVKV SYTFNARGEL RVSNQLRGVN KELAAIPRLG NTFALQPAYD
AVTYYGRGPV ENYQDRNTAA LVGRYSSSVG DLGYAYTRPQ ENGYRTGVRE VQFLDGNGRG
IAVRAESALL GFNAHHQLNS DYDEGPEKVQ RHTYDIPVRP LVTVNVDYKQ SGVGGDDSWG
ARPHAQYTLP AGDYTYSFLL SPVR
//
