ID A0A2P8GVU7_9MICO Unreviewed; 687 AA.
AC A0A2P8GVU7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=CLV49_1696 {ECO:0000313|EMBL:PSL38084.1};
OS Labedella gwakjiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Labedella.
OX NCBI_TaxID=390269 {ECO:0000313|EMBL:PSL38084.1, ECO:0000313|Proteomes:UP000241203};
RN [1] {ECO:0000313|EMBL:PSL38084.1, ECO:0000313|Proteomes:UP000241203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21548 {ECO:0000313|EMBL:PSL38084.1,
RC ECO:0000313|Proteomes:UP000241203};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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:PSL38084.1}.
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DR EMBL; PYAU01000001; PSL38084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8GVU7; -.
DR Proteomes; UP000241203; 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:UP000241203};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 35..405
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 416..617
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 628..670
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 687 AA; 75320 MW; 9FC5C20D5CBACF32 CRC64;
METLDQEARA IVVTDERPSA TTQPSLREGI AFGCDYNPEQ WDRAVWREDV ALMREAGVDL
VALNIFGWSH IEPRPGEYDF DGLDEIIGLL HEAGIRINLG TGTSSAPPWL THRHPEILPE
AADGTTRFPG GRQAWCPSSA VFRRYALALV EKVAERYGQH PAVALWHVSN ELGCHNALCY
DDESAEAFRG WLRARYGTIE RLNSAWGTSF WSQTYSAFEE ILPPRLTLSS RNPGQVLDFH
RFSSDALLDH YRAETAVLRR HSDVPVTTNF MVTAHIRNLD YWTWAPEMDV VANDHYLDHR
LAEPAAELSF ASDLTRGLAG GEPWLLMEQS TGSVNWQPHN LAKAPGQLTR NSLSHVARGA
DAICFFQWRA SLQGSEKFHS ALVPHAGTDS DLWREVVDLS RTLDRLDELA GTRVQADVAL
LFSWENWWAA DGESRPTHAV DYLSQVHAMH ASLTRSGHTV DVVRPGASLE GYGLVVVPSL
YLVRDEEARV LSDFAEAGGH VVVTFFSGIV DEEDRVRPGG YPGAFRDLLG VSVEEFAPVL
PGQVLTLASG RSASLWSERT RARGAEVLDS FADGPSAGRP AITRRALPGG GAAWYIATHL
DAADLDGVLR EAAAGAGVVP IGDPREPGLE VVRRANEERS YLFLINHTDH AIDHPATGID
IVSGDPVEGA AHVPAGFVSV IREESAA
//
