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
//