ID   A0A1C5DK50_9ACTN        Unreviewed;       683 AA.
AC   A0A1C5DK50;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=GA0115254_118561 {ECO:0000313|EMBL:SCF83219.1};
OS   Streptomyces sp. Ncost-T10-10d.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839774 {ECO:0000313|EMBL:SCF83219.1, ECO:0000313|Proteomes:UP000198750};
RN   [1] {ECO:0000313|Proteomes:UP000198750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ncost-T10-10d {ECO:0000313|Proteomes:UP000198750};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-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         ECO:0000256|PIRNR:PIRNR001084};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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; FMDF01000157; SCF83219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5DK50; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000198750; 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: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:UP000198750}.
FT   DOMAIN          26..398
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          411..614
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          626..680
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        162
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        321
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   683 AA;  75266 MW;  B88C1D0BCB59EF75 CRC64;
     MTSPRISRFP YPAGSDGRRR LGYGADYNPE QWPREVWEED VRLMREAGVN IVSLAIFSWA
     RIQPTADTWD FEWLDEVMDL LHAGGIGVDL ATATASPPPW LTTAHPDILP VTATGETLWP
     GARQHWRPTS PVFRTHALRL VRELATRYAG HPALVAWHVN NELGCHNVYD YSDDAAHAFR
     TWLLRRYTTL EALNHAWGTA FWSQRYSDWD QILPPRLAAS HPNPTQQLDF KRFSSAALKD
     HLLAEREVLR ELTPDVPVTT NFMVMGGTKG MDYADWADSG AIDFVANDHY VTPGPQDRDE
     LSFAANLTSG IAGHRPWFLM EHSTSGVNWQ PVNLAKKPGE LARDSLLHVA HGADAVCFFQ
     WRQSAAGAEK YHSAMVPHAG SDSELFRSVA ELGRTLEALA PIAGAGREPG RVAVLFDWDS
     WWTSEHDSHP TSRLDYHREA LDWYSALLRL GIRADVVPAH RTDLSSYDVV IAPVLHVVPQ
     PFGKALTRYV EGGGHLVTTY FSGVVDENDH IWLGGYPGAL RELLGIRIEE FGPLLDGATV
     DLDNETTGSL WTDRITVTGP DVEVLARYRS GTYASRPAIT RCTTGHGSAA YVSTRLGAEG
     LAALLPDLLA PAGVTSELPD EARGAVELTV RRDADSRYLF LVNRSDVPVP LPGVTGELLV
     GPATEGGLVL PPRDVAVLRQ PAP
//