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Database: UniProt/TrEMBL
Entry: A0A1B4C2E5_9BURK
LinkDB: A0A1B4C2E5_9BURK
Original site: A0A1B4C2E5_9BURK 
ID   A0A1B4C2E5_9BURK        Unreviewed;       662 AA.
AC   A0A1B4C2E5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=WI26_26595 {ECO:0000313|EMBL:AOI61086.1};
OS   Burkholderia diffusa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=488732 {ECO:0000313|EMBL:AOI61086.1, ECO:0000313|Proteomes:UP000094588};
RN   [1] {ECO:0000313|EMBL:AOI61086.1, ECO:0000313|Proteomes:UP000094588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RF2-non-BP9 {ECO:0000313|EMBL:AOI61086.1,
RC   ECO:0000313|Proteomes:UP000094588};
RA   Sahl J., Wagner D., Keim P.;
RT   "Diversity of Burkholderia near neighbor genomes.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP013363; AOI61086.1; -; Genomic_DNA.
DR   RefSeq; WP_069227708.1; NZ_CP013363.1.
DR   AlphaFoldDB; A0A1B4C2E5; -.
DR   KEGG; bdf:WI26_26595; -.
DR   Proteomes; UP000094588; Chromosome 2.
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          404..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   662 AA;  74353 MW;  3745E305D63F8AD7 CRC64;
     MRLGVCYYPE HWPESMWADD ARRMKALGIA QVRIAEFAWS RIEPSPGEYD WGWLDRAVDV
     LGAAGLEIVM CTPTATPPKW LVDRHPDILA IGADGRPRTF GSRRHYDFSS PTYLEASRRI
     CSAVAERYGR HPAVRYWQTD NELGCHQTVV SYSPAALVRF RAWLQARYGT IDALNRAWGT
     VFWSMEYRHF DEVDAPVGTV TEAHPSHRLD YRRFASDELA RYHRMQVAVI RTHSPGRPVA
     HNFMQLFTEF DHYEVARDLD VATWDSYPLG ALEEQWFAPD VKARWLRTGH PDFASFNHDL
     YRGMSKLPFW VMEQQPGPVN WAHWNPAPLP GMVRLWSWEA FAHGAGCVSY FRWRQAPFAQ
     EQMHAGLHTP DDRLDEGGRE AQRVAREIAA VLDAGADANG AVRAPVALVF DYEAKWLFEV
     QPQGADFHYP RFAFEYYSAL RSLGLDVDIV SAHAPLDGYR LVVVPPLPIV PDDFAARLAA
     SGAHAVFGPR TGSKTVDLRI PPALPPGPLA SILPVRVWRV ESLRPNVTER IDGTLHDGAP
     LTGDARHWRD LVELNDDDVH SVVRARFADG HPAWVSHGTL HYWAALFDDA TTARLFADVA
     VEAGLTPSPL GDGVRVSRRG GLTYVFNYGS TPHTIDAVQP SAFVVGAAQV ERQGVAVYRS
     RS
//
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