ID A0A085EHB1_9FLAO Unreviewed; 1103 AA.
AC A0A085EHB1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=FEM08_26190 {ECO:0000313|EMBL:KFC58606.1};
OS Flavobacterium gilvum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1492737 {ECO:0000313|EMBL:KFC58606.1, ECO:0000313|Proteomes:UP000028636};
RN [1] {ECO:0000313|EMBL:KFC58606.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1308 {ECO:0000313|EMBL:KFC58606.1};
RA Shin S.-K., Yi H.;
RT "Genome Sequence of Flavobacterium sp. EM1308.";
RL Submitted (MAY-2014) 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:KFC58606.1}.
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DR EMBL; JNCP01000087; KFC58606.1; -; Genomic_DNA.
DR RefSeq; WP_035638866.1; NZ_JNCP01000087.1.
DR AlphaFoldDB; A0A085EHB1; -.
DR STRING; 1492737.EM308_01465; -.
DR KEGG; fgl:EM308_01465; -.
DR PATRIC; fig|1492737.3.peg.2607; -.
DR eggNOG; COG3250; Bacteria.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000028636; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1103
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001788420"
FT DOMAIN 814..1085
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1103 AA; 126619 MW; DC880B1240E9ED0E CRC64;
MFKSIHIYHL SKFRFSIVFF LFSICVSQAQ SVTGEPAGVP ELHKKYEFAP WEDPTVTSIN
RQPSRATAYS YTNIEDALKG DRTKSRIQML NGDWNFKYAV NLKEASKDFY KTNVSGWDKI
EVPSNWEMKG YDNPIYKSAV YPFRPINPPY IPKDYNGIGS YQRSFTVPAN WKDMTVTLHF
GGVSSGFQVW LNGEFLGYGE DSCLPSEFDI TPYLKEGENV VSVQVIRWAD GSYLEDQDHW
RVSGIQREVF IMAEPKLRIQ DFFVQTKLDK EYKDAIFKLR PKVENLTGEK IKGYTFNVQL
YDDNNVAMFK EPLKRPVIDL INESYPRLDN VRFGFFQETI KNPKKWSSEE PNLYTLVVSI
KDKNGNITEA KSCKVGFRSI EFSKENGKML INGKETHVYG VNRHDHNPTR GKAVTREDIK
QDITTIKKFN FNFIRTSHYP NDPYFYELCD QYGIMVMDEA NQETHGIGGK LSNDPLWTNA
YMERMTRMVE RDKNHPSVVM WSLGNEGGKG PNHAAMSGWV HDFDITRPVH YEPAQGNAKL
DGYIDPLDPR YPKTIDHAYR YENPQDDSYV DMVSRFYPGV FTPKFLVDQK KDTRPIIFVE
YSHAMGNSVG NLKELWDEFR SLPRVIGGCI WEFKDQGLVK FDSRSGQQYF AHGGDFGEKY
HDGNFNTKGL VDSNGKPKGS IFENKWVYQP ATSTLKDGNQ LEIKNRQAVK SLEGYIPVIK
ILENGNVIKT QVLKPFNLEA GQSTTLNVNP YLPKMKSDAE YILNIEFQLS KEELWASKGY
VVAEDQFLLK KKEAVSLVSK KENLNVAETD ADFKIKGKTF DITIGKTNGA LTSYVFNGEE
QVFAPLLPNF VRPLTDNDKR GWKPQKNMKQ WYRAKPKLTN IKMDKSASEI KITSDYEIIK
DSANVSVVYN IKQDGTIKVD YSLKASNKLP NIPKIGMQMG VQRKFDQISW YGKGELENYS
DRSFGSFVGK YSLSINDFVE HYVKPQENGN RCDVRWMALT TPQKNKGFLV VNDNKVLSMS
AWPYTQENLA AAVHTFDLKD PGFLTVNIDL IQMGVGGNDS WTSVSQPLEK YQIKSGDYQY
SFYLVPFFGS KEELENSLKK FKY
//
