ID I9AIH4_9BACE Unreviewed; 949 AA.
AC I9AIH4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=HMPREF1074_01503 {ECO:0000313|EMBL:EIY87132.1};
OS Bacteroides xylanisolvens CL03T12C04.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997892 {ECO:0000313|EMBL:EIY87132.1, ECO:0000313|Proteomes:UP000003566};
RN [1] {ECO:0000313|EMBL:EIY87132.1, ECO:0000313|Proteomes:UP000003566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL03T12C04 {ECO:0000313|EMBL:EIY87132.1,
RC ECO:0000313|Proteomes:UP000003566};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides xylanisolvens CL03T12C04.";
RL Submitted (FEB-2012) 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:EIY87132.1}.
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DR EMBL; AGXE01000008; EIY87132.1; -; Genomic_DNA.
DR RefSeq; WP_008022251.1; NZ_JH724294.1.
DR AlphaFoldDB; I9AIH4; -.
DR PATRIC; fig|997892.3.peg.1540; -.
DR HOGENOM; CLU_007798_0_0_10; -.
DR Proteomes; UP000003566; 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; 1.
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; 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; 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 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..949
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003718538"
FT DOMAIN 55..193
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 219..295
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 298..527
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 683..874
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|Pfam:PF02929"
SQ SEQUENCE 949 AA; 107903 MW; 1F7ED23BD9857987 CRC64;
MKKVTTLLST LALATTLTAQ NLPQTERQYL SGHGCDDMVE WDFFCTDGRN SGKWTKIGVP
SCWELQGFGT YQYGITFYGK PFPKGVADEK GMYKYEFEVP EKFRGKQVNL VFEASMTDTE
VKVNGRKVGS KHQGAFYRFS YNVTDFLKYG KKNLLEVTVA KESENASVNL AERRADYWNF
GGIFRPVFLE VKPAVNLRHI AIDAKMDGTF RANCYTNISN DGMSIRTQIL DKKGKKITET
TVPVKAGGDW TSLQLNVSNP ALWTAETPNL YKAQFSLLDK AGKVLHSETE NFGFRTIEVR
ESDGLYINGV RINVRGVNRH SFRPESGRTL SKEKNIEDVL LMKGMNMNSV RLSHYPADPE
FLEACDSLGL YVMDELGGWH GKYDTPTGVR LIEGMIERDV NHPSIIWWSN GNEKGWNTEL
DGEFHKYDPQ KRPVIHPQGN FSGFETMHYR SYGESQNYMR LPEIFMPTEF LHGLYDGGHG
AGLYDYWEMM RKHPRCIGGF LWVLADEGVK RVDMDGFIDN QGNFGADGIV GPHHEKEGSY
YTIKQLWSPV QIMNTSINKQ FDGKFSVENR YDYLNLNTCR FLWKQVKFPL ATDASNAAIQ
VLKEGEVQGS DVVAHSAGIL DIKTNILPNA DALFLTAIDP YGHELWRWTF PVNQLNQQTE
QLSPLSSRPA YTETENELTV KANKRTFIFS KKDGQLKGVS VDNRKISFAN GPRFIGARRA
DRSLDQFYNH DDEKAKEKDR TYSEFPDAAV FTKLDVKEDG GNLVVTANYK LGNLDKTQWT
INPSGELALD YTYNFSGVVD LMGIRFDYPE DQVISKRWLG AGPYRVWQNR IHGTQYDVWE
NDYNDPIPGE TFTYPEFKGY FGDVSWMNIQ TKEGTISLTN ETPDAYIGVY QPRDGRDRLL
YTLPESGISV LNVIPPVRNK VNSTDLCGPS SQPKWVNGPQ TGRVIFRFM
//
