ID A0A1U9L9Q3_9FLAO Unreviewed; 1067 AA.
AC A0A1U9L9Q3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=BXQ17_12325 {ECO:0000313|EMBL:AQS94815.1};
OS Polaribacter sp. BM10.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1529069 {ECO:0000313|EMBL:AQS94815.1, ECO:0000313|Proteomes:UP000189235};
RN [1] {ECO:0000313|EMBL:AQS94815.1, ECO:0000313|Proteomes:UP000189235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BM10 {ECO:0000313|EMBL:AQS94815.1,
RC ECO:0000313|Proteomes:UP000189235};
RA Lee J.-Y., Bae J.-W.;
RT "Polaribacter aureus sp. nov., isolated from the gut of a blood cockle,
RT tegillarca granosa.";
RL Submitted (FEB-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}.
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DR EMBL; CP019704; AQS94815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9L9Q3; -.
DR STRING; 1529069.BXQ17_12325; -.
DR KEGG; pola:BXQ17_12325; -.
DR Proteomes; UP000189235; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 776..1065
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1067 AA; 122830 MW; FE0EDC853FD45276 CRC64;
MMKFFLKTFL FVFLIGSCNQ ETKFKPKYIA KVWENPEWEN SEIFQVNREA PKATFYNYDN
LDNAILGKNW KSSSYYKSLN GTWNFYYADS VKARPESFYK EDFNVDGWDT ISVPSNWELQ
GFGLPIYTNV VYVFPKNPPF IPHNINNNGS YKRDFQIPKN WKNNDIYLHF AGVSGAMYVY
INGKKVGYSE GSKTPAEFNI TKYIKSGKNQ IAVQVLRWSD ASYIEDQDFW RLSGIERDVY
LRADKPIAIN DFKVGSDLVN NYKDGAFSID IELKNTKLSV EKRKLEVTLL DDKKQQIFSK
TKIVAISKSK SNITFKENIK NVKPWTAETP NLYTAVLSLS NLDGEFLQIT SVKVGFRNIK
IKNNQFLVNG KPVLIKGVNL HDHDETKGHV VDEVLTIKDL RLMKQNNVNA IRCSHYPKNT
FFYDLCDTYG FYVIDEANIE THGMGTTNQG LDKKPEMKKI HPAYREDWKA AHLDRTIRMF
ERDKNHPSIV TWSLGNEAGN GDNFFATYNW LKENDATRPT QYEGATKYKN TDIQAPMYDR
IPQLIEYAEN KPKRPLILCE YSHAMGNSLG NFKDYWDVIR KYDVLQGGFI WDWVDQGLVT
KTEDGKKYWG YGGDFGAAHL QHDGNFCLNG IVNPDRTPHP GLQELKKVYQ NIQFSDVNFK
TGQVKIFNEY FFTNLNNFKI DWELFKEGEK ITSGSLGVLD IAPQKSKMVQ LNLPKLDNKK
HEYQLNFLAT THKDLPLLSK GFPLAKAQFV TGTFIPKFKE NATEHLMLSS TENEVVLKSE
NFTASFDVQT GELSKLDYGN GNIIQKGISA NFWRATTDND YGFNMPKHFG IWKKATENQK
LTSMLLKDKK STLDLLSADK ISFNGNAVHL EMIYKLPENI ATIKMQYVID ASGQITIKTS
LLNVKTALPN LPRFGTNFIV NKDLNQVNWY GRGPLENYQD RKTSQFVGSY QASVSELYFP
YIRPQENGYR TDVRWVTFTN RQGQGIKVLG PKNIGFSAHH QYNSDFDAGE TKKQRHTVDI
VERDFTNINI DNEQMGVGGD TSWWTRPLEQ YQIKAQNQSF SYSIFPI
//
