ID A0A1D8ATJ3_9BACT Unreviewed; 867 AA.
AC A0A1D8ATJ3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN Name=lacZ_2 {ECO:0000313|EMBL:AOS44218.1};
GN ORFNames=Verru16b_01279 {ECO:0000313|EMBL:AOS44218.1};
OS Lacunisphaera limnophila.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Lacunisphaera.
OX NCBI_TaxID=1838286 {ECO:0000313|EMBL:AOS44218.1, ECO:0000313|Proteomes:UP000095228};
RN [1] {ECO:0000313|EMBL:AOS44218.1, ECO:0000313|Proteomes:UP000095228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IG16b {ECO:0000313|EMBL:AOS44218.1,
RC ECO:0000313|Proteomes:UP000095228};
RA Rast P., Gloeckner I., Jogler M., Boedeker C., Jeske O., Wiegand S.,
RA Reinhardt R., Schumann P., Rohde M., Spring S., Gloeckner F.O., Jogler C.;
RT "Three novel species with peptidoglycan cell walls form the new genus
RT Lacunisphaera gen. nov. in the family Opitutaceae of the verrucomicrobial
RT subdivision 4.";
RL Submitted (JUN-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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP016094; AOS44218.1; -; Genomic_DNA.
DR RefSeq; WP_069961494.1; NZ_CP016094.1.
DR AlphaFoldDB; A0A1D8ATJ3; -.
DR STRING; 1838286.Verru16b_01279; -.
DR KEGG; obg:Verru16b_01279; -.
DR PATRIC; fig|1838286.3.peg.1289; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000095228; Chromosome.
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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:AOS44218.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AOS44218.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095228}.
FT DOMAIN 53..194
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 249..297
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 305..517
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 867 AA; 96006 MW; 4D01AD3E1128E37F CRC64;
MSLRHFPLVL ALISGLAAGA RETEVRYLSG TGPENAVPWE FLCTGGRNSG IWTTIPVPSC
WEQQGFGTYN YGVHHRPSKD KPNPPPLADE EGHYRHTFRV PAEWRDRAVR LVFDGVMTDA
EVTVNGRSAG PVHQGSFYRF HHDITALLDF EGENRLEVVV RKKSANESVN RAERLGDYWL
FGGIFRPVWL EARPRAAIEW TGIDARADGT FTADIHFGAA AAVAGRVTGV LVDQYDHELS
PPLSAAIPAG AAKATLSGRF ENLALWTAET PNLHRMRFTY SPEGGEPHTV TERFGFRTFE
VRPQDGLYLN GTKIILKGVN RHCFNPDTGR TISRAQSYAD ARLIKEMNLN AVRMSHYQPD
KHFLEACDEL GLYVLNELAG WQGAYDTPTG TRLIGQLVRR DVNHPSILFW DNGNEGGWNT
EVDGEFAKWD IQQRAVLHPW AKFSGVDTDH YEVWDSHVKK SAGPMLYMPT EFLHGLYDGG
IGVGFRDYWD VMKKSPTVVG GFFWVFADEG IARTDQAGRI DNAGNLAPDG IVGPRGEKEG
SFYTVKEIWS PVQISLPAVL PPGWTGADIR NEYQFTDLAS ASFRWEWLRA GPEGETLIEA
ADQAGPVLAP GASGILPSPL VVPAGAEFLR LTAFAAGQVV TVASAWTGPV AAPPPAANAA
PAGAPDWLGE PTVLALRRQD RRFEPVPAAT NPVFRWTRQP DGALRLDYEF TYDGPADVLG
IRFPVAEARL QAKRWLGHGP YRVWQNRLEG GWLGVHAMAF NDATPGESWA YPEFKGCFRD
WRWLSLLTPE GWLQVTNLSG VPFFGLGRPR DGVNGLYAMP DLGLSFLEVI PAMRNKFHSP
EQLGPQSRTR EVAGIHRGSL LFRLDRP
//
