ID A0A103EEG6_9BURK Unreviewed; 660 AA.
AC A0A103EEG6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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=WS68_13090 {ECO:0000313|EMBL:KVE33330.1};
OS Burkholderia sp. TSV86.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1385594 {ECO:0000313|EMBL:KVE33330.1, ECO:0000313|Proteomes:UP000066043};
RN [1] {ECO:0000313|EMBL:KVE33330.1, ECO:0000313|Proteomes:UP000066043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSV86 {ECO:0000313|EMBL:KVE33330.1,
RC ECO:0000313|Proteomes:UP000066043};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
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:KVE33330.1}.
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DR EMBL; LOWB01000109; KVE33330.1; -; Genomic_DNA.
DR RefSeq; WP_059572427.1; NZ_LOWB01000109.1.
DR AlphaFoldDB; A0A103EEG6; -.
DR Proteomes; UP000066043; 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:0005975; P:carbohydrate 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; 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:SF2; BETA-GALACTOSIDASE YESZ; 1.
DR Pfam; PF02449; Glyco_hydro_42; 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.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084}.
FT DOMAIN 6..390
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 405..605
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 142
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 313
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 321
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 660 AA; 73958 MW; A20BE22A27A056D6 CRC64;
MRIGVCYYPE HWPESMWADD ARRMKALGIE QVRIGEFAWS RIEPSPGEYD WDWLDRAINV
LGAAQLDVVM CTPTATPPKW LIDRHPDILP IGADGRPRGF GSRRHYDFSS PAYYGESKRI
CTAIAERYGR HPAVRCWQTD NELGCHLTVV NYSSAALARF REWLKARYGT VDALNRAWGT
VFWSMEYRSF DEIDAPIGTV TEAHPSHRLD YRRFASDELA RYHRMQVDVI RAHSPGRAIT
HNFMQLFTEF DHYQVARDLD FAAWDSYPLG ALEEQWFAPQ VKARWLRTGH PDFASFNHDV
YRGMSKRPFW VMEQQPGPVN WASWNPAPLP GMVRLWSWEA FAHGAGCVSY FRWRQAPFAQ
EQMHAGLNTP DNQLDAGGRE AAQLAQEIAA LRAATDGSAD GAVRAPVALI YDYEAKWLFD
VHPQGADFHY PRIAFEYYSA LRALGLDVDV IPADAPLDGY RLVIVPPLPI VPDDFAARLA
ASSAHVVLGP RTGSKTRDLQ IPPTLPPGPL APLMPIRVWR VESLRPNVAE RVAGTAHDGS
AFTGSARCWR DLVELRDEAR ADVRARFADG HPACIASGRL QYWAALFDDT TTERLLADAA
AEAGLAPVPL GDSVRMSRRG GLTYVFNYGD APYALDSVAP GAFVLGTAQV EPRGVAVFRH
//
