ID A0A1Y1T1J5_9FLAO Unreviewed; 1193 AA.
AC A0A1Y1T1J5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=IIF7_13807 {ECO:0000313|EMBL:ORL44886.1};
OS Zunongwangia atlantica 22II14-10F7.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=1185767 {ECO:0000313|EMBL:ORL44886.1, ECO:0000313|Proteomes:UP000192746};
RN [1] {ECO:0000313|EMBL:ORL44886.1, ECO:0000313|Proteomes:UP000192746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II14-10F7 {ECO:0000313|EMBL:ORL44886.1,
RC ECO:0000313|Proteomes:UP000192746};
RA Lai Q., Shao Z.;
RT "Zunongwangia sp. 22II14-10F7 Genome Sequencing.";
RL Submitted (APR-2013) 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:ORL44886.1}.
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DR EMBL; ARYN01000012; ORL44886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1T1J5; -.
DR STRING; 1185767.IIF7_13807; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000192746; 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 CDD; cd00161; RICIN; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.80.10.50; -; 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; 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 InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
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 Pfam; PF14200; RicinB_lectin_2; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SMART; SM00458; RICIN; 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 SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ORL44886.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192746}.
FT DOMAIN 27..160
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT DOMAIN 917..1191
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1193 AA; 137465 MW; 042E7E0BBCFD1846 CRC64;
MDFKKLSIFF LFLSISILGV AQELSEDRYY RIKSKEGLVL STKNNDQNDA LIWLDKENKE
SKDQLWQITA IGNGLYNIRN SYSKKSLDNR GILNGSGNQI IQWDTEPFNN NQQWKIQQTG
TGAYIITHKK SQMVLDFQQN ENGNFGVYQK PNSAQTWEII PTEIAAEVAN KKKRGEHEWE
NETIFAINKE EGHVTFFPYP NSAALKKDAF FNKPWLTPNS DYYKSLNGDW KFNWVTNPED
RPKEFYKENF DVSKWETIEV PSNWEMKGYG TPIYTNITYP FKNNPPFIQS QKGYTNEHKP
NPVGSYRREF SLPNNWDGKE VFIHFDGVYS GMFLWINGNK IGYSQGSNND AEFNITKFLK
AGKNTLAVQV FRWTDGSYIE DQDMFRLSGI HRDVYLYATP KLSVRDFIIS ADFKNEDLSK
VDFSVNSIIK NFDSKSIKNA SLQIQLFDPA GKEVAKIQQK LDKIKSETEQ EILLKTEVNN
PELWSAEIPH LYNVLISLEQ DGKEIFATSN KYGFRKIEVK DNRVFINNKQ IFFKGVNRHD
THPTLGKAIP VSSMIQDITM MKQNNINTIR TSHYPNSQKM YALLDYYGLY TMDEADLENH
GNGNISNNPS WIPAFNDRIK RAIQRDRNHA SVIFWSLGNE GGNGDNFDEM YALAKKMDPV
RPIHYQGKNE AADIDSHMYP SLSFMEKFDK NGTQKPYFLC EYGHAMGNAI GNLQEYWDYI
EDDSSRMIGG CIWDWVDQGL IKQTEDQNNY YFGGDFGDTP NDNDFCLNGI VTSDRKPTAK
LEEVKKVYQY IKISAEDLAN GQLKIKNTYD FLNLNQFEIK WEVLEDGIPT ENGLLDPVAL
NADEECVIEI PFKRNYPKNH EYLLNVYFQL KNEQTWAKAG HQLASAQFSL TDKVAISAVD
VKVLPKISVQ EKDSDLLISG KNFSSVFNIK DGMLRSLKYD EKEMIYAEEG LTFNWYRSVN
NDKYTDQNYY QTSEKVNSIK YEVSPDRKSV SIQLEKEVSI AHPEKPVQFN YAINYSIYSN
GVVDIAAEFM KPENQPIIRR LGLRLSLDES LENVSYYGKG PFENYSDRKT AAYLRAYEAT
VNDFENAEHY AKAQSMGNRE EVRWLSLSDK NGNGVKIEAK DVLSFTALHH TDETLWNTRH
DFELKDNASP QTFLSLDRIQ QGLGNASCGP LPLEQYLIPE NKTLSYSFRI SGL
//
