ID A0A0S8JW37_9BACE Unreviewed; 1050 AA.
AC A0A0S8JW37;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AMS26_12530 {ECO:0000313|EMBL:KPL13940.1};
OS Bacteroides sp. SM23_62.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL13940.1, ECO:0000313|Proteomes:UP000050819};
RN [1] {ECO:0000313|EMBL:KPL13940.1, ECO:0000313|Proteomes:UP000050819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62 {ECO:0000313|EMBL:KPL13940.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL13940.1}.
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; LJUP01000114; KPL13940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8JW37; -.
DR PATRIC; fig|1703352.3.peg.4878; -.
DR Proteomes; UP000050819; 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; IPR023232; Glyco_hydro_2_AS.
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.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 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}.
FT DOMAIN 742..1025
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1050 AA; 120038 MW; 881DEE1A69FAB431 CRC64;
MPDWEDPEMI GQNKEPPHCT LIPFPNSKLA VLGDRKDSPY FKLLNGVWKF NWVKKPGHRP
RDFFNVGYDV SHWMDIQVPG NWELYGHGIP IYTNVIYPFS PENPNPPFIP HEYNPVGSYR
TEFTIPGEWE GRQIFIHFDG VKSACYLWIN GLKVGYSQGS MTPAEFDITD FVHDGKNVLA
AEVYRWCDGS YLEDQDTWRL SGIYRDVYLI SRPQIYIRDF FICCDLDSQC KNAQLHVTAK
VHNCSSSTAE HHEIDVIMMD INGNVVGDDP LISGDVKGIA AGEEDVLKIS ALAQNPNKWS
AEIPNLYIIL LVLKNSAGEV LEVLRCNFGF REIEIKDSQL FINGVSLKLK GVNRHEHDPD
YGFTVPVSRM IQDIKLIKQA NMNTVRTSHY PNMPIWYDLC DKYGLYLIDE ANMETHGVSY
GQNRLPGSDP RWEKAAIDRM ASVVERDKNH PSVIFWSLGN EAGHGENIRK MAEYARRADP
TRPLHYRQMN SVVDTDNLSY QTVEWIINRA KEYPDRPFLM EEYAYARGNA VGNLEEYQDA
IESHRQLIGA LIWDWADKAL RKYSQDGEMY WAYGGDYGPP GTPSDGTMVC NGIVGPDRDP
EPEYYEVKKV YQFVKVKAID LIKGKICIEN NYNFLNLAHF DVLWEMTVKG VKVQEGKIPE
LTLAPKDTQM VLIPFDAPVL TAGSECFLTI KFVLAQEELW ADRGHIVAWD QFKMPFEAPS
KVEDSLADMA HLTLNDSGDL YSIVGKNFSI KIGKASGVIE SFIYKNNQFI EAPLIPNFWR
VPTDNDIENK WDHTTEKPIG GMPVRLGVWK HAGRDRKIIS IDTKQITPQL VCINTHMILP
PGDTNYIINY DIYGSGDIIV SVALRPENLK IPEMPRIGMQ MILQSEFNIV TWYGRGPHES
YWDRKTGAAI GIYSGRVEEL IHNYVRPQEN GNRTDVRWIA LTNETGTGLL AVGMPLLDFS
AWPYTMQDLD SAKHIHELPR GDITTLNLDY KQMGVGGDDG WTEKARPHPE YRLPLKNYKY
CFRLQPYSKE MGKIAFNARR ILPQFEIHKK
//