ID A0A1Y4U9E8_9BACT Unreviewed; 1038 AA.
AC A0A1Y4U9E8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=B5E60_07465 {ECO:0000313|EMBL:OUQ53466.1};
OS Alistipes sp. An116.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1965546 {ECO:0000313|EMBL:OUQ53466.1, ECO:0000313|Proteomes:UP000195395};
RN [1] {ECO:0000313|Proteomes:UP000195395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An116 {ECO:0000313|Proteomes:UP000195395};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-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:OUQ53466.1}.
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DR EMBL; NFLR01000008; OUQ53466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4U9E8; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000195395; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1038
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012418461"
FT DOMAIN 754..1032
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1038 AA; 118701 MW; 5D6B06BCC6DE0EB1 CRC64;
MKKLLFILLF AASSVSAKAP AERWLDPTCF GVNRAPMRTS FIVYPTAGEA SPENTPERSP
FYRSLNGVWT FLRVDRPGAE PEGFFRPGFD DSSWGEMPVP GLWEMNGYGD PVYTNKPYPW
HKFFPVKAPL VPYEQNYTGI YRRTVTLPEE WKGKELFIHI GSATSNLTLW VNGHEVGYSE
DSKLEAEWEI TRYTKPGQEN LIVMRINRWC DGSYLEDQDF WRMTGIGRDC YLYARDKRRL
ADVRITPDLT SDYRDGELQI RIATTPGIGA VRLVLRDEAG EELLRRTVTP RQNRIETSFE
VSNPRKWSAE SPALYTLTAE ALTRDGSVIE AAAFPVGFRK VEIRGGQLLV NGQPILIKGV
NRHEMEPNTG YYVTREEMIR DIREMKRLNI NAVRTCHYPD APIWYDLCDR YGLYVVDEAN
IESHGYFYHD KSKNLAGNPD FAQAHLDRNQ RMVHRDFNHP SIIIWSTGNE AGNGPNFERC
YDWIKAFDPS RPVQYEQASY HGDYNTDITC PMYWDYNTCQ RYLDRNPDKP LIQCEYAHAM
GNSLGGLKEY WEMIRREPRY QGGFIWDFAD QALAWRSPEG RLTFRYGGDY NDRDASDSTF
CCNGILASDR SWHPHAYEVK HLHQPVHTTL RDAKKGIVAL YNENFFTDLS PYRLLWEVSA
DGKPVTSGVI ERIEVAPQQT KEITLGYDPA RIEALDGELL LTVRYQLRET TDLLEAGYEV
AADQLVLRAD DPARRFASLE AGASREKLRL DGDSVTGEDF TLRFDPETGC LISYRLRGVE
LLSGALRPNF YRAATDNDLG VRQAGKVPDS RIWAEITPRL EKFDLTKENQ QVRATAHYLL
PQVGGRLTLS YRIAEDGTIR VRETLKADST RTGVADLMRF GMMFEAPGMF NTLSYYGRGP
MENYADRASA AFVGRYDQRV ADQFHAKYAS PQESGTRSGL RWWRLTDETG LGLEICSDRH
FSASAIPYSI PQLDNGTPEY RRHPSELVSD GRTHVCFDLI QSGLGCVNSW GKQARPEYRI
PYADLQFDFL LRPVGVSH
//
