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
//