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Database: UniProt
Entry: D7BPZ6_STRBB
LinkDB: D7BPZ6_STRBB
Original site: D7BPZ6_STRBB 
ID   D7BPZ6_STRBB            Unreviewed;       680 AA.
AC   D7BPZ6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
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   Name=bga6 {ECO:0000313|EMBL:ADI05003.1};
GN   OrderedLocusNames=SBI_01882 {ECO:0000313|EMBL:ADI05003.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI05003.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI05003.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI05003.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI05003.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7BPZ6; -.
DR   STRING; 749414.SBI_01882; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
DR   KEGG; sbh:SBI_01882; -.
DR   PATRIC; fig|749414.3.peg.1947; -.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_012430_1_1_11; -.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006012; P:galactose 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; IPR013739; Beta_galactosidase_C.
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:SF1; BETA-GALACTOSIDASE GANA; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08533; Glyco_hydro_42C; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377}.
FT   DOMAIN          22..386
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          398..602
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          615..671
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        158
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        310
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   680 AA;  76121 MW;  5BA61B07564A957B CRC64;
     MTVNSRMDAF RARLGGFAFG GDYNPEQWDR AVWDEDIQLM RRAGVNLVTL GVFAWASLEP
     EPGRFTFEWM DEVMDLLHAG GISVDLATPT MAPPVWLTHE HPEVLPVMED GERFGFGNRL
     QFDPASPRYR EHAARITTAL AERYSHHPAL AMWHISNEYG QPSYGEASAV AFRGWLQRKY
     GSLDALNDAW YTRFWSQVYT SWDQINPPEV PRSWSNPTRR LDFKRFVSDA LLECFVMERD
     IVRSYRDDIP VLTNYMRFYK NADYWTWAPE QDAVALDIYP NPGHDDAHIS AALNFDLMRS
     LRGEPWVLME QAASSVSQWK VNNVKRPGHM RLGSYQAIAH GADSVLYFQW RASRGGHERF
     HSAMLPHSGT ASRTWQEIEA LGGELPRIAE AVGARSSAEI AVLFDWNAWW GLTETHGLPR
     NDFDYTQIAT DHYQPLLEAH HAVDMVHFGS DLSPYKVVVV PNAYLVDDRF TDALTRFVEG
     GGTLVCSFFS GVVDANNQVR QPAYPGAFRG LIGAYIDEYW PARGDETFAV TFADGTTRTA
     DWWQDSIHPE TARVLATYAS GHLEGRPAIL DNAVGRGRVV YLGTRLEPGA LRDTLLEAGA
     AAGVSPLVAA APGHLEAVRR VGDDAEFLFL LNHSETQPAE VRLAADGLDL ISGAKTGATL
     EVAPLSVSVV RFENTERVQE
//
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