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Database: UniProt
Entry: A0A0R2A4D4_9LACO
LinkDB: A0A0R2A4D4_9LACO
Original site: A0A0R2A4D4_9LACO 
ID   A0A0R2A4D4_9LACO        Unreviewed;       641 AA.
AC   A0A0R2A4D4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=FC26_GL001594 {ECO:0000313|EMBL:KRM61519.1};
OS   Paucilactobacillus vaccinostercus DSM 20634.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Paucilactobacillus.
OX   NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM61519.1, ECO:0000313|Proteomes:UP000051733};
RN   [1] {ECO:0000313|EMBL:KRM61519.1, ECO:0000313|Proteomes:UP000051733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM61519.1,
RC   ECO:0000313|Proteomes:UP000051733};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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:KRM61519.1}.
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DR   EMBL; AYYY01000025; KRM61519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2A4D4; -.
DR   STRING; 1423813.FC26_GL001594; -.
DR   PATRIC; fig|1423813.3.peg.1621; -.
DR   Proteomes; UP000051733; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   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; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
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:UP000051733}.
FT   DOMAIN          56..240
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          243..345
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          349..638
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   641 AA;  73840 MW;  DC18842A6B112B63 CRC64;
     MYNVIVLDEG GTRLDADLTW LDDPETFRVN QVPAHSDHRG YATVAEADQQ HSSLVQSLDG
     PWQFAFAKDP MHRPRDFYQP DTDRSTFHDI EVPGHIELAG YGQIHYINTA YPWEGKHYRR
     PAYAMGAEKR ERGMFSTDPE NTVGAYVKHF ELNQTLVNHR IAIEFDGVEQ AMFVWLNGQF
     VGYAEDSFSR SEFDLTPYIH PGDNLLAVEV FKHSTAAFLE DQDMFRFSGI FRSVRLVAKP
     ALHVEDLTIR ATVDGTLKHG HLQVETTLSA LHHVTGHMRL QLLNAENESI WSQDQALART
     VTVQTTVAAP RLWSHQDPYL YRLQIELFDD HDQLVEVVPY VVGFRRLVLQ NRVMILNGQR
     LIINGVNRHE WDAHRGRAVT LADMHSDMQV FHKYHINAVR TCHYPDQVAW YTLCDRNGIY
     MMAENNLETH GTWQKMGVVE PSYNVPGSLP QWQAAVLDRA RSNYQMFKNH PAILFWSLGN
     ESYAGDDIAA MDRYYHDADP TRLTHYEGVC RNRAYEDRIS DMESMMYDPP AAIAAYLEND
     PQKPFINCEY MHDMGNSLGG MASYDALIDR YPMYQGGFIW DFIDQALWCQ DEVTGNQVLR
     YGGDFDDRHS DYEFSGDGLL FADRTPKPAL QEVSYYYGRR D
//
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