ID I2DT64_9BURK Unreviewed; 659 AA. AC I2DT64; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 24-JAN-2024, entry version 39. 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=MYA_3481 {ECO:0000313|EMBL:AFJ87840.1}; OS Burkholderia sp. KJ006. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ87840.1, ECO:0000313|Proteomes:UP000010108}; RN [1] {ECO:0000313|EMBL:AFJ87840.1, ECO:0000313|Proteomes:UP000010108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KJ006 {ECO:0000313|EMBL:AFJ87840.1, RC ECO:0000313|Proteomes:UP000010108}; RX PubMed=22843575; DOI=10.1128/JB.00821-12; RA Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K., RA Lee C.H., Yu D.S., Park S.H., Kim J.F.; RT "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp. RT Strain KJ006."; RL J. Bacteriol. 194:4432-4433(2012). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP003515; AFJ87840.1; -; Genomic_DNA. DR RefSeq; WP_014724277.1; NC_017921.1. DR AlphaFoldDB; I2DT64; -. DR KEGG; buk:MYA_3481; -. DR PATRIC; fig|416344.3.peg.3538; -. DR HOGENOM; CLU_012430_1_0_4; -. DR Proteomes; UP000010108; 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..389 FT /note="Glycoside hydrolase family 42 N-terminal" FT /evidence="ECO:0000259|Pfam:PF02449" FT DOMAIN 402..601 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 659 AA; 73771 MW; DC105922D156155C CRC64; MRLGVCYYPE HWPESMWADD ARRMKALGIV QVRIGEFAWS RIEPSPGEYA WGWLDRAIDA LGAAGLEIVM CTPTATPPKW LVDRHPDILA IGADGLPRKF GSRRHYDFSS PTYLEASRRI CTAVAERYGR HPAVRYWQTD NELGCHQTVV SYSPAALLRF RAWLKARYGT IDALNRAWGT VFWSMEYRHF DEVDAPVGTV TEAHPSHRLD YRRFASDELA RYHRMQVDVI RAHSPGRPVA HNFMQLFTEF DHYAVARDLD VATWDSYPLG ALEELWFAPD VKARWLRTGH PDFASFNHDL YRGMSKQPFW VMEQQPGPVN WAHWNPAPLP GMVRLWSWEA FAHGAGCVSY FRWRQAPFAQ EQMHAGLHTP DDRLDEGGRE AQRVAGEIAA VLDADADGAV RAPVALVFDY EAKWLLEVQP QGADFHYPRF AFEYYSALRA LGLDVDIVSA HAPLDGYRLV VVPPLPVVPD DFAARLAASG AHAVFGPRTG SKTVDLQIPP ALPPGPLASL LPLRVWRVES LRPNVTERID GALRDGSPLS GDARHWRDLV ELHDDARSVV HARFADGHPA WVSHGAFHYW AALFDDATTL RGFADVAAEA GLTPTPLGDD VRVSRRGGLT YVFNYGSTPH TIDAVAPSAF VVGAAQVEPQ GVAVYRSRP //