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Database: UniProt
Entry: A0A370BBS4_9ACTN
LinkDB: A0A370BBS4_9ACTN
Original site: A0A370BBS4_9ACTN 
ID   A0A370BBS4_9ACTN        Unreviewed;       683 AA.
AC   A0A370BBS4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=DVH02_05410 {ECO:0000313|EMBL:RDG39091.1};
OS   Streptomyces corynorhini.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2282652 {ECO:0000313|EMBL:RDG39091.1, ECO:0000313|Proteomes:UP000253741};
RN   [1] {ECO:0000313|EMBL:RDG39091.1, ECO:0000313|Proteomes:UP000253741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC230 {ECO:0000313|EMBL:RDG39091.1,
RC   ECO:0000313|Proteomes:UP000253741};
RA   Dunlap C.;
RT   "Streptomyces species from bats.";
RL   Submitted (JUL-2018) 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   -!- 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:RDG39091.1}.
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DR   EMBL; QQNA01000031; RDG39091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370BBS4; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000253741; 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   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; 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:UP000253741}.
FT   DOMAIN          26..394
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          408..611
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          623..683
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        319
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         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   683 AA;  75496 MW;  88772A6EC3146C29 CRC64;
     MTRVPSPRWL RRPHDDRTPR FAYGADYNPE QWPREVWPED IRLMREAGVN IVSLAIFSWA
     RIQPAPDTWE FGWLDEIMDL LHEGGIAVDL ATATASPPPW LTTLHPEILP VTAAGETVWP
     GARQHWRPTS PVFRSYALKL ARKMAERYGD HPALTAWHIS NELGCHNIYD YSDDAAHAFR
     GWLTDRYGSI EALNHAWGTA FWAQRYTEWD QILPPRLAAS HPNPTQQLDF KRFSSDALKD
     YLRAERDLLY RLTPDTPVTT NFMVMGETKG MHYADWAREV DFVSNDHYTL PGPQRLDELS
     FSANLTGSIA GGHPWFLMEH STSAVNWQPV NVAKRPDELA RDSLLHVAHG ADAVCFFQWR
     QSAAGAEKYH SAMVPHAGPD SEVFRSVAAL GALLGELSEV VGSHGRPARA AVLFDWESWW
     ASEQDSHPTS LLRYRQEALD WYSAFLDLGV RADVVHRGAS LDGYDLVVAP VLHVVPRDLA
     KELTGYVEGG GHLVTTYFSG VVDENDHAWL GGYPGALREL LGIRIEEFGP LLDGQHVTLD
     DGSTGTLWTD RITVTDDAVE VLASYRTGDQ SGRPAITRRA VGGGSAAYVS TRLGAEGLRG
     VLAPLLARAG VAGELPEAAR GRVELVVRGD GDTAYWFLVN RTDEPVELAR LSGTLLAGTA
     GSTRHGAEGP LVLGPRGVAV VRR
//
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