ID   A0A0P0R8F9_9BURK        Unreviewed;       648 AA.
AC   A0A0P0R8F9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE            Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN   ORFNames=K788_0008429 {ECO:0000313|EMBL:ALL64297.1};
OS   Paraburkholderia caribensis MBA4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1323664 {ECO:0000313|EMBL:ALL64297.1, ECO:0000313|Proteomes:UP000019146};
RN   [1] {ECO:0000313|EMBL:ALL64297.1, ECO:0000313|Proteomes:UP000019146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBA4 {ECO:0000313|EMBL:ALL64297.1,
RC   ECO:0000313|Proteomes:UP000019146};
RX   PubMed=24558235;
RA   Pan Y., Kong K.F., Tsang J.S.;
RT   "Draft Genome Sequence of the Haloacid-Degrading Burkholderia caribensis
RT   Strain MBA4.";
RL   Genome Announc. 2:e00047-e00014(2014).
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|PIRNR:PIRNR001084};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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DR   EMBL; CP012746; ALL64297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P0R8F9; -.
DR   KEGG; bcai:K788_0008429; -.
DR   Proteomes; UP000019146; Chromosome 1.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR   PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ALL64297.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ALL64297.1}.
FT   DOMAIN          2..375
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          390..589
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        127
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        298
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   648 AA;  73115 MW;  D50BF940F1DD4FD9 CRC64;
     MWKDDARRMK ALGIEQVRIA EFAWSRIEPS PGEYDWGWLD RAIDVLGDAG LQVVMCTPTA
     TPPKWLIDRH PDILPVGADG RPRAFGSRRH YDFSSPSYFD ASRKICEAVA ERYGKHPAVA
     YWQTDNEFGC HNTVVSYSPA AVARFRVWLK ERYQNIDALN RAWGTVFWSM EYRSFDEIDA
     PVATVTEAHP SHRLDYRRFA SDEVARYNRM QVEIIRAHSP GRRVAHNFMQ LFTEFDHYKV
     ARDLDVATWD SYPLGALEEQ WYAPEIKAKF LRTGHPDFAS FNHDVYRGMS KLPFWVMEQQ
     PGPVNWAHWN PAPLPGMVRL WSWEAFAHGA GCVSYFRWRQ APFAQEQMHA GLNTPDNRLD
     IGGSEAEQVA HEIAKVSAAD ADANANVRSK VALIYDYEAK WLFEIHPQGA DFHYPRFAFE
     YYSALRSLGF DVDVIPADAP LDGYAMIVVP PLPVVPGDFA VRLAASGAQI VLGPRTGSKT
     PDLQIPANLP PGALASLLPI RVWRVESMRP NVTEPVQING AGDGLREGQA RHWRDLIDAA
     DERSFGVRAR FADGHPAYVQ HGSVHYFASL FDDRLTESLF ARIATEAGLT PTPLGDSVRI
     SRRGKLTYVF NYTNARHVIE GVDASRFVIG AHEVEPQGVA AYRTEDTE
//