ID A0A0Q9L1S3_9MICO Unreviewed; 662 AA.
AC A0A0Q9L1S3;
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=ASG74_03160 {ECO:0000313|EMBL:KRE43849.1};
OS Knoellia sp. Soil729.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE43849.1, ECO:0000313|Proteomes:UP000051965};
RN [1] {ECO:0000313|Proteomes:UP000051965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil729 {ECO:0000313|Proteomes:UP000051965};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE43849.1, ECO:0000313|Proteomes:UP000051965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil729 {ECO:0000313|EMBL:KRE43849.1,
RC ECO:0000313|Proteomes:UP000051965};
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:KRE43849.1}.
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DR EMBL; LMSA01000001; KRE43849.1; -; Genomic_DNA.
DR RefSeq; WP_056138861.1; NZ_LMSA01000001.1.
DR AlphaFoldDB; A0A0Q9L1S3; -.
DR STRING; 1736394.ASG74_03160; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000051965; 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 Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 14..381
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 396..594
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 606..647
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 662 AA; 73152 MW; 4844ED6636C559E9 CRC64;
MRAWPKDGIA FGGDYNPEQW PRSVWDDDMR LMREAGVTFV TLGVFSWSWL EPTKGEYTFE
WLDEAMDLLH ANGIAVDLAT ATATPPPWLT SAYPEILPVD HDGHTLWPGS RQSWCPSSRL
YRELALSLTD RLAARYHDHP ALAMWHVSNE YACHNLPCYC DTCAIAFRAW LEQRYADLDT
LNDAWGTAFW SQRYTAWEDI LPPRRTTTFA NPTQVLDYHR FGSDTLLGFY REEYEVIRRH
SSQVPITTNF MTLSNFRLLD YHDWAPLQDV VSTDHYIVDS LEHPRAELSF HGDLTRGLAG
GRPWILMEHS TSAVNWQPVN PAKAPGQTVL DSLTHVAHGA DALGFFQWRQ SRSGSEKFHS
ALVPHAGEDS DRFREVCELG AISARLGELL GSTVEAEVAV LWDYEALWAM SGPCMPSSAI
DYATAPHTFH RILRERGITC DVVHPSADLS RYRVVIVPTL YVVSDENASA IASAAESGAH
VVVTYFSGIS DLDDHVRLGG YPGAFRDLLG VRVEEFFPLR PGEVVPLSGG GTGSQWSEDA
RAVDAEVLST YAAGPLQGRP ALTRRAVGEG TASYLGTLPD DATLGSVLDE VIALAAVTPA
AQTPPGVEVV RRSSSEGSWL FVLNHTTQEH EVTVTGHDLL TGRDVGPTHR LAGLCAAVVR
EA
//
