ID A0A1M6U9M2_9FLAO Unreviewed; 1039 AA.
AC A0A1M6U9M2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN05444371_3225 {ECO:0000313|EMBL:SHK65869.1};
OS Epilithonimonas mollis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=216903 {ECO:0000313|EMBL:SHK65869.1, ECO:0000313|Proteomes:UP000184498};
RN [1] {ECO:0000313|Proteomes:UP000184498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18016 {ECO:0000313|Proteomes:UP000184498};
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; FRAM01000004; SHK65869.1; -; Genomic_DNA.
DR RefSeq; WP_072999994.1; NZ_FRAM01000004.1.
DR AlphaFoldDB; A0A1M6U9M2; -.
DR STRING; 216903.SAMN05444371_3225; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000184498; 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; 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; 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1039
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012070697"
FT DOMAIN 759..1034
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1039 AA; 119091 MW; FB3B83D958A1CBD1 CRC64;
MNLKILAIVL SFFSVPVIAQ NNDWENPKIV DQGKEKPHVT FVSFDNQRDA LSDEYSKSSN
YKSLNGQWKF SYTDLYKDRP ADFYKTTMDD SGWANLTVPS NWELNGFGIP IYTNVTYPHP
RTPPFIGPNN PVGTYRKTFT IPEDWDQKEI LLHFGSISGC AFIYVNGNKV GMTKSSKTPA
EFDITKHLKK GENLLAVQVF RWHDGSYLED QDFWRLSGLE REVYLYALPK LAIWDYFLRA
DLDDKYKNGL LSADVDLRKF KENNLKSGSV TLSLLDKSGE TIYNKEEIFS VNEDSIQTLK
FQTAIKNPLK WNAETPNLYD CVLTLKDQNG KILSITASKV GFRKIEIRNA RLLVNGMPIS
VHGVNRHEHD DVTGHTTTRA LMLKDIKLMK ELNINAVRLS HYPNDPLWYK LCDQYGLYLV
DEANIETHGM GAELQGGFDK TIHPAYLPEW APAHTDRIVR MVERDKNHAS IIIWSLGNEC
GNGPVFHDNY KWIKSRDNSR PVQFEQAGQD WNTDIVAPMY PRIADMKRYA ADSTKTRPYI
MCEYSHAMGN SNGNMQTYFD IMRKSKNMQG GFIWDWVDQG IKTKDANGKS FWAYGGDLGS
FSWQNDENGV ADGIISSDRT PDPGAYEVKK MYQKVIFTAK DLNKGLINIE NVFDFTNLNQ
YSFKWLLLRN GEKINEGAFD VQLDPHQSKD VKLNIPQYKS IAGTEYYLNL YAYTKSATEM
LPSGSEIAKE QFSYAGSYFD RDETKTTKLV FTKDDKKLNF TADTVKGEFD LQKGKFILYS
KNDSNFNNFP EPYFWRAPTD NDFGNGMPSK LGLWRSAHDQ KKLKKITVGE QTDKGLAIQV
EWQLASIDVP YQINYFIHNN GDIQITTTMD MAGKELPELP RFGMRTTLPA SYNNLSYYGR
GPYENYTDRH SASFIGIYQD KVENQYYKGY IRPQESGNKT DVRWFKLTDK SGNGIKVEGL
QPIAFTAINH SVEDLDPGLT KKKQHPVDLP PRHQVFLSID LKQRGLGGDD SWGAYPHQEY
RLLDKKYSYS YTISLLSKK
//
