ID I9E6Q1_9FLAO Unreviewed; 1035 AA.
AC I9E6Q1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=HMPREF1321_0229 {ECO:0000313|EMBL:EIW94345.1};
OS Capnocytophaga sp. oral taxon 412 str. F0487.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1125721 {ECO:0000313|EMBL:EIW94345.1, ECO:0000313|Proteomes:UP000003723};
RN [1] {ECO:0000313|EMBL:EIW94345.1, ECO:0000313|Proteomes:UP000003723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0487 {ECO:0000313|EMBL:EIW94345.1,
RC ECO:0000313|Proteomes:UP000003723};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (MAY-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 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:EIW94345.1}.
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DR EMBL; AJZR01000004; EIW94345.1; -; Genomic_DNA.
DR RefSeq; WP_009420906.1; NZ_AJZR01000004.1.
DR AlphaFoldDB; I9E6Q1; -.
DR PATRIC; fig|1125721.3.peg.119; -.
DR Proteomes; UP000003723; 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 756..1033
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1035 AA; 119719 MW; 8D51264AAE055611 CRC64;
MKNYLYIIIS FFLTIVSYAQ HLDSIFENPA LQEINRMPMR ASYFPFENIA KAKNGTIEQS
ARFLNLNGLW SFLWKEDYRQ LPKDFYKTNF NESQWTKIPI PSNWEVQGYG IPIYVNASYE
FNQKNPTPPD IPDSLQQNAG LYRKTFDLPT SWQGEKVYLH LGAVKSAFKL YINGKFVGMG
KDSKLASEFD ITPYITKGKN LIAIEVRRWT DASYLECQDM WRFSGISRDC YLYMRPKVHL
YDLSISASLD KNYTNGKLIT SVEVWNETPS NVSKYQVEVS LFDKEQLLYQ EQKETIGLKK
AFGKTELQFE AQLPQVRAWS AETPYLYRLQ MVLYDAEGKV KEVVSRPIGF RTIEIEGANI
LVNGKRILFK GVNRHETDPH TGQVVSQEQM ENDVKQMKAL NFNAVRTSHY PNDPYFYDLC
DKYGLYVMDE ANIESHGMHY EMDKTIGNDP VWEYAHLLRL ERMVKRDKNH PSVLFWSMGN
ESGNGWNFYK GYQHIKGLDP SRPIHYELAH YDWNTDIESR MYRRIPFLID YALSNHTKPF
LQCEYAHAMG NSVGNFQEYW DVYEHYPKLQ GGFIWDFIDQ GLYKTLPNGK KLVTYGGDYG
DKNTPSDNNF LINGVIASDR SWHPHAYEVR KVQQEIGFQY QNNQLMLRNK HFFKDLSNYE
IHWQLLKEGV PVQSGNITNL IVLPQSEATF LLPPLKTDDK AEYILQCTAR LKQDEGLLKK
GTELAFAEFP LTSYTPQKAI ADTTPLEVEE TTSHILLHNK HYTAKIDKQT GKWVSFQVKN
EELFAPEGLE VNLWRAGTDN DFGAGLPKKL QQLQEAEKKA DSVRISVEKL NSGQVKITLS
KRLVEGTIDY TQELLFDGKP SVTVSNHFKP LNNDKTLTFK IGNHLTLLPF QRIQWYGRGP
WESYWDRKTS AMVGLYEGAI ASQYYPYVRP QENGNKTDVR WAKLSKKKGV NIAIYSTGSL
LNINALPYSP AQLFPGIEKG QTHAGELTPD KYTHLDIDLQ QLGLGGDNSW GNLPMKQYLL
YLYQPYSYSY RIEAF
//
