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Database: UniProt
Entry: A0A1I2FHH6_9BACT
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ID   A0A1I2FHH6_9BACT        Unreviewed;      1050 AA.
AC   A0A1I2FHH6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=SAMN05444380_12911 {ECO:0000313|EMBL:SFF04187.1};
OS   Thermophagus xiamenensis.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Thermophagus.
OX   NCBI_TaxID=385682 {ECO:0000313|EMBL:SFF04187.1, ECO:0000313|Proteomes:UP000181976};
RN   [1] {ECO:0000313|EMBL:SFF04187.1, ECO:0000313|Proteomes:UP000181976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19012 {ECO:0000313|EMBL:SFF04187.1,
RC   ECO:0000313|Proteomes:UP000181976};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FONA01000029; SFF04187.1; -; Genomic_DNA.
DR   RefSeq; WP_044138675.1; NZ_FONA01000029.1.
DR   AlphaFoldDB; A0A1I2FHH6; -.
DR   STRING; 385682.SAMN05444380_12911; -.
DR   eggNOG; COG3250; Bacteria.
DR   InParanoid; A0A1I2FHH6; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000181976; 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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000181976}.
FT   DOMAIN          756..1047
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
FT   REGION          979..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1050 AA;  120645 MW;  7B94E58940C5F9F3 CRC64;
     MKRSILFLVM SLSLFSCTRY NDYSNVPFEE KSPPDWENPA VNEINKEEPR AWYVPFASEE
     EASKDDIWAS SLIKSLNGEW LFHLSENPSE RPKWFFKDDY DIRDWGTIKV PANFELEGYT
     YPIYTNSQYP HAKTPPTIQD HYNPVGSYKR TFTIPESWKG KEVYLHFGAV SSAMYVWVNE
     QLVGYSEDSK TPAEFNITSF LKPGENTLAV EVYKWCDGSY LEDQDFWRLG GITRDVFLMA
     REKQHIRDFK VTAGLADDYT TGIFSLETEL ENVSTTTPVT LEAILYDGTA VLDRFTAEVT
     EGTATFKSEY ANVKRWSAET PNLYQLVIKL KDPSGQVLEV LRQDVGFRRV EIKGNTLLVN
     GQYVYLKGVN LHEHHPVTGH VVDEATMIKD IQTMKMHNIN AVRTSHYPQP ERWYELCNRY
     GLYLIDEANI ESHGMGYGKA SLAKDTVWKS SHLYRTRNMY ERDKNHPSII IWSLGNEAGN
     GVNFDATYDY LKSQDSTRPV QYEQAHGGRN TDIFCPMYAK IEWMIKYAKE DGSKPLIQCE
     YAHAMGNSVG NLQDYWDVIE SYEVMQGGFI WDWVDQGLLT ENENGEQYWA YGGDFGPDTV
     PSDGNFCING VVNPDRVPHP ALQEVKKVYQ YIKFRPVDLQ KGSISIENKY AFISTDLFDF
     EWDIKGNGEL IKSGNFGKIS LLPDEKATVN ADLNFTVKPG TEYFLTVRAK LKEEYGLVPA
     GTVLAAEQFQ LPVYVPEKTP QELGKIKYEE QGDQLLITGE GFSVAFDMIK GVMTSFKSEE
     KELLLKGPEP DFWRAPTDND FGNNMPIRSR MWRKAGENRK VTKAEVEEKG EGQLMVKFEY
     DLLNSENGEK IATYHSTYLV KGNAEIEVDN HFAMAKDNLP EIPRMGMTLH MPREYDQMTW
     YGRGPHESYQ DRKTSAFVDL YSGSVADQYW PYIRPQENGN KTDVRWVMIT NSEGEGLRFE
     GKQLLEVSAH HNIMEDFESP RRTDGRWEKG EERPVQRHTT DVKPRDLTSV DIDLKQMGVG
     GDNSWGAWTH EQYRLTEKSY SYGFVIKLVK
//
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