ID A0A1M6V7T6_9BACT Unreviewed; 957 AA.
AC A0A1M6V7T6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=SAMN02746009_01528 {ECO:0000313|EMBL:SHK77567.1};
OS Hymenobacter psychrotolerans DSM 18569.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1121959 {ECO:0000313|EMBL:SHK77567.1, ECO:0000313|Proteomes:UP000183947};
RN [1] {ECO:0000313|Proteomes:UP000183947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18569 {ECO:0000313|Proteomes:UP000183947};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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 -!- 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}.
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DR EMBL; FRAS01000006; SHK77567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6V7T6; -.
DR STRING; 1121959.SAMN02746009_01528; -.
DR OrthoDB; 1007335at2; -.
DR Proteomes; UP000183947; Unassembled WGS sequence.
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; 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 PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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 PRINTS; PR00132; GLHYDRLASE2.
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; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..957
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013042480"
FT DOMAIN 59..196
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 208..298
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 301..469
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 957 AA; 107031 MW; 5EC9792A6C80ED48 CRC64;
MKTRLIFRIA SLLLFCFGGE AAAQSAGRKQ VQYLSGPDNT RTATWDFFCT GGRRSGSWTT
IQVPSCWEQQ GFGSYNYGRD YKTYGKNFRF ADEKGLYRSQ FEVPAAWQEK EVFIVFEGSM
TDTEVKVNGQ LAGPIHQGAF YRFRYNITDK LKPGQPNLLE VTVSKMSADA SVNNAERLAD
YWVFGGIFRP VYLEAYPRQF IAHTAINAQA NGTFALQTAV RGLRQTTTVQ ADILDATGTV
VGTARGTAGP ADTLVTLKTT VPKPRQWTAE TPTLYRANVS LWAEGQVLYQ TQEKFGFRTI
EVRRGQGIFV NGTQVKLKGI NRHSFWPETG RTLNDSIHLL DVRLMKEMNM NAVRMAHYPP
DARFLDLCDS LGLYVLDELA GWQKAYRTPV GRKLVREMVT RDVNHPSILF WSNGNEGGTN
KELDGDFGKY DPSGRPVLHA HHRPGNAFNG IDTNHYEDYY STQKILADSL IYMPTEFLHC
QDDGGGGTAL HDLWELHWAA PRSGGGFLWA LVDEGLVRTD QRNIIDVNGV NAPDGVLGPH
REKEGSFYAI REVFSPIKIE LQELPAKFKG DIPVENRYHF TNLSQCFFQW ELLDFRKPGE
AFTGATAAQR GRLASPNVAP LGRGKLQLKL PKNWQQHDAL VLSAYDAQKN LVYKWTWKTG
SNAQLLRDIL PTSPDKLPPV AVAETDSTLT LQASGITVGF DKKTGQLRGI KGNNNSPLSF
GKGPVLVSGT ATFRGLRHFS ENGNEVVEAT YQGDLQQVRW TMQPTGWLRL DYDYRLHGDF
AFSGISFTYP ENYVIGAKWL GHGPYRVWKN RRQGVGLNVW ENAYNNTQTG AAPWLYPEFK
GYFADIAWLE MNTVEGKFLI ASPDKGLFVR LFDFYGLSGV VPHPALPVGN LSFLDAIPPL
GTKLALNIDT NTKNLGPSGE LNHLTGTTRR TLYFFFGLPK TTATPQPYTA PVKDDLF
//
