ID A0A0J0Y2F0_9SPHI Unreviewed; 922 AA.
AC A0A0J0Y2F0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=AB669_17860 {ECO:0000313|EMBL:KLT64411.1};
OS Pedobacter sp. BMA.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT64411.1, ECO:0000313|Proteomes:UP000036014};
RN [1] {ECO:0000313|EMBL:KLT64411.1, ECO:0000313|Proteomes:UP000036014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMA {ECO:0000313|EMBL:KLT64411.1,
RC ECO:0000313|Proteomes:UP000036014};
RA Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT "Pedobacter sp. BMA.";
RL Submitted (JUN-2015) 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:KLT64411.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LECU01000007; KLT64411.1; -; Genomic_DNA.
DR RefSeq; WP_047800692.1; NZ_LECU01000007.1.
DR AlphaFoldDB; A0A0J0Y2F0; -.
DR STRING; 1663685.AB669_17860; -.
DR PATRIC; fig|1663685.3.peg.3734; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000036014; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000036014};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:KLT64411.1}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..922
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005245750"
FT DOMAIN 53..186
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 196..284
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 286..412
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 922 AA; 105025 MW; 2CD87F0F6A63B305 CRC64;
MRLRFILFFC LLIMFDALKA QQTEKLYLSG TGNDQTVNWE FFCTEGANSG KWTTIPVPSN
WELQGFGKYN YGFNKEANKG KEQGLYKYRF KVPGDWKSKI IRIVFEGSMT DTEVKINGKL
AGAVHQGSFY VFNYDISGLI KYDTDNLLEV KVSKHSANQS VNEAERKADF WIFGGIFRPV
YLEALPQTHM ERIQADAKAN GIFSANVLTA GSADEISVEL KDQNGKKFGN TFSVKTTSAS
TQILYTFKNP QLWSSEFPNL YTATFTLIKK GKEVHQLTKK IGFRTVEVKE RDGVYVNGVK
MKFKGVNRHS FYPSSGRTTS KRISIDDVQL MKGMNMNAVR MSHYPPDGHF LDVCDSLGLF
VMDELAGWHG TYDTPTGTKL MKEMMRNDEN HPSIIFWANG NEGGHNRELD HLFPEEDIQK
RPLIHPWEVF GGFETTHYRE FNYGIGNYDH GHNILMPTEF LHGMWDGGHG AGIEDYWNAM
WHNPLSAGGF LWDFADQAVV RTDKNGELDT DGNHGPDGIV GPYHEKEGSF FTIKEVWSPV
FIEKREMTPG FDGSFLVENR YAFTNLNQCT FEWKLKHLKS AGDAEFKAGK TDAPDVKPFE
KGKLQINLPA DWRTFDALYL TAKDVYGKVL FTWSFPINLP KDDAERIVAK AGGSKVALEE
SALAYLVAAN GIKFSFDKTT GLLQGVENAK GIIPFSKGPV LQEGVNNFKK FKVKREGDTL
IISSTFDKKE SYNTLEWTVY PSGWLKMQVK YFPSDYFTTF AGLNFSYPET EIKGVEYKGN
GPYRVWKNRM KGTEFGIWKK DYNDSATGEP AWQYPEFKGY YSNMYWCEFI GRQQSFKVLT
DREDVFLRLF TPKKSKDTEY DNMSPTFPNG DISFMNAISA IGTKTQKPET TGPMGMKNIY
YDFDKDPSRA LDMTLYFDFS GK
//
