ID A0A0Q7KDS1_9ACTN Unreviewed; 663 AA.
AC A0A0Q7KDS1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=ASD06_03210 {ECO:0000313|EMBL:KQX70011.1};
OS Angustibacter sp. Root456.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae.
OX NCBI_TaxID=1736539 {ECO:0000313|EMBL:KQX70011.1, ECO:0000313|Proteomes:UP000051170};
RN [1] {ECO:0000313|EMBL:KQX70011.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX70011.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX70011.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX70011.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQX70011.1}.
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DR EMBL; LMER01000001; KQX70011.1; -; Genomic_DNA.
DR RefSeq; WP_056672816.1; NZ_LMER01000001.1.
DR AlphaFoldDB; A0A0Q7KDS1; -.
DR STRING; 1736539.ASD06_03210; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000051170; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000051170};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 14..384
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 396..597
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 606..661
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 663 AA; 72902 MW; 244D590AD3D74DA5 CRC64;
MRSWPTRSLA LGGDYNPEQW PEEVWRDDIR LMREAGVTFA TVGVFSWSLL EPEPGRFDTG
WLDRVLDLLH EADVAVDLAT ATASPPPWML QLDGDLLPMR VDGSRLWPGG RQAYCPSNST
YRERALHLVE HLASQYHDHP ALALWHVNNE YACHNAPCYC DQCGARFRAW LERRYGDVET
LNEAWGTAFW SQHYTAFEQI LPPRQAPTVS NPTQVLDFRR FTSDNILELF VAERDVLHRL
SPGVPVTTNF MTLNHFRHLD YFAWGPEQDV VSTDHYLVAA ERDPDAELSF SGDLTRGIAG
GRPWVLMEHS TSAVNWQPVN LPKAPGQLLR NSLAHVAHGA DTLGFFQWRA SRAGAEKFHS
GLVPHAGTDT RLWREVVQLG EVCERLAEVV GTTVQADVAV LWDYQAGWAC DEDSHPSSLV
RYGTDAHAVH RALRERGVAA DVVHPSADLS RYRLVVVPTL YSCTDEAAAA VRAAAERGAS
VLVTFFSGIV DQDDHIRLGG YPGAFRDLLG VRVEEFHPLA PDTTVALDDG AVATTWAEHL
HLAGAEAVAS YADGALVGVP AITRRSVGTG AAWYLATRVD DEHLGALVDR LLAEAGVEPP
VAAPRGVELV RRTGDGRSYL FALNHTEAEA ALAVNGRDLV ADTDTGGNLR LAPGGVAVVR
EDR
//
