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Database: UniProt
Entry: A0A0L0BCE6_9MICC
LinkDB: A0A0L0BCE6_9MICC
Original site: A0A0L0BCE6_9MICC 
ID   A0A0L0BCE6_9MICC        Unreviewed;       658 AA.
AC   A0A0L0BCE6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=AC792_14015 {ECO:0000313|EMBL:KNC17745.1};
OS   Arthrobacter sp. RIT-PI-e.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1681197 {ECO:0000313|EMBL:KNC17745.1, ECO:0000313|Proteomes:UP000053253};
RN   [1] {ECO:0000313|Proteomes:UP000053253}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT-PI-e {ECO:0000313|Proteomes:UP000053253};
RA   Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT   "Whole genome sequencing of endophytes isolated from poison ivy
RT   (Toxicodendron radicans).";
RL   Submitted (JUL-2015) 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:KNC17745.1}.
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DR   EMBL; LGIU01000093; KNC17745.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0BCE6; -.
DR   STRING; 1681197.AC792_14015; -.
DR   PATRIC; fig|1681197.3.peg.696; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000053253; 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:UP000053253}.
FT   DOMAIN          6..375
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          389..591
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          603..650
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        142
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        299
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   658 AA;  72488 MW;  C2508ADD9DB9F458 CRC64;
     MGYGADYNPE QWPREVWDED VRLMREAGVN VVSLAIFSWA RLQPERDQWN FAWLDEVIDL
     LHANGIAVDL ATATASPPPW LATEHPEILP VTQDGSTLWP GARQHWRPTS PVFREHALKL
     VTAMAERYKD HPAICAWHVS NELGCHNIYD YSDDAAAAFR TWLTERYGSI DVLNDAWGTD
     FWSQRYTRFE QILPPRQAAS HPNPTQQLDF KRFSSDALKQ YLREERDILH RITPEIPVTT
     NFMVMGETKG MDYADWAAEV DFVSNDHYFV PGPQAVDELS FSANLTGNIA AGKPWFLMEH
     STSAVNWQPI NTPKKPGALR RDSLTHVAHG ADAVCYFQWR QSRAGAEKFH SAMVPHAGED
     SPIFRDVVAL GQELAGLSDV VGSRRSAAPA AILFDWDSWW ASEQDSHPTD RLRYKQEALD
     WYTAFLDLGI RADVVPSAAD LTGYGLVVAP ILHTVPAELR TRLEEYVSGG GNLVASYFSG
     ITDENDHIWL GGYPGALAEL LGIRIEEFGP LLDGESVSLD NGTSATTWAD RVHTRAGDVA
     TLVRYTSGEH AGAAAGTRRA VGAGSAAYVG ARLGSEGIAP VLADLAARAG VTSELPEELR
     GEVEQVLRTD GGTEYVFLIN RTDAPVDITG VEGETVTGED AKLAPRSVTV RTRAVRTA
//
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