ID D9TCH8_MICAI Unreviewed; 666 AA. AC D9TCH8; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 60. 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 OrderedLocusNames=Micau_3147 {ECO:0000313|EMBL:ADL46676.1}; OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442). OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Micromonospora. OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL46676.1, ECO:0000313|Proteomes:UP000001908}; RN [1] {ECO:0000313|EMBL:ADL46676.1, ECO:0000313|Proteomes:UP000001908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442 RC {ECO:0000313|Proteomes:UP000001908}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., RA Hirsch A.M., Woyke T.; RT "Complete sequence of Micromonospora aurantiaca ATCC 27029."; RL Submitted (AUG-2010) 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 --------------------------------------------------------------------------- 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; CP002162; ADL46676.1; -; Genomic_DNA. DR RefSeq; WP_013286302.1; NC_014391.1. DR AlphaFoldDB; D9TCH8; -. DR STRING; 644283.Micau_3147; -. DR CAZy; GH42; Glycoside Hydrolase Family 42. DR KEGG; mau:Micau_3147; -. DR eggNOG; COG1874; Bacteria. DR HOGENOM; CLU_012430_1_1_11; -. DR OrthoDB; 9800974at2; -. DR Proteomes; UP000001908; Chromosome. 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, ECO:0000313|EMBL:ADL46676.1}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ADL46676.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3}; KW Reference proteome {ECO:0000313|Proteomes:UP000001908}; KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}. FT DOMAIN 17..388 FT /note="Glycoside hydrolase family 42 N-terminal" FT /evidence="ECO:0000259|Pfam:PF02449" FT DOMAIN 400..600 FT /note="Beta-galactosidase trimerisation" FT /evidence="ECO:0000259|Pfam:PF08532" FT DOMAIN 612..663 FT /note="Beta-galactosidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF08533" FT ACT_SITE 153 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1" FT ACT_SITE 312 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1" FT BINDING 114 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2" FT BINDING 118 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3" FT BINDING 152 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" SQ SEQUENCE 666 AA; 72216 MW; D6C588739D9D1214 CRC64; MPTKALWDDG RLCYGGDWNP EQWPPDVWRE DVALMRAAGV NLVTVGVFAW SRLEPEPGRY TLDWLDDVLD LLHTGGIRAA LATPTASPPP WFSLRHPDAL PLTADGVRLH HGSRDTYCAA APAYRDAARG IAEVLAARYA HHPALALWHV HNEYGTTCHC PHAETAFRHW LTTRYGDLDA LNDAWVTSFW SQHYSDWAQV GTPRATQYLA NPGQLLDFRR FWSDTLLSAY TEQRDLLRAA NPAVPVTTNY VLGDWVPVDH ARWAREVDLV AIDHYPSATD LGAEEQTAFA ADLARGWARH GAGRPVPWLL MESAPNQIHT AGRMHTKEPG RMIRHSLAHI ARGSAGVMFF QWRAPAGGAE RFHSAVVSHA GPDTRVFREA ADLGAALGRL AGAAPGRVQA AVAIAYDAAS GWALRHPGMP RDGLDHPGEA AAVHRALWHA GVTADVVPPG APLDGARLLV LPALYLASDA TVDWVRRHVH DGGHLLVTWL SGVADEHARV RLGGYPGAYR DLLGVRVEEF HPLADDEHVP LTGGGTGRIW SETVHPAGAE TVSAYAGGVP AGRPAITRNR VGDAYAWYVS TRPDDDTYRR LLTEAARLAG VAPACPGAPE GVEAVRRHDG LLYLLNHTDR PQRVPAAGFE LLTGAAVDGE LTVAPGAVAV VREKTP //