ID D3EI13_GEOS4 Unreviewed; 1032 AA. AC D3EI13; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAR-2024, entry version 75. DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, ECO:0000256|RuleBase:RU361154}; DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154}; DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154}; GN OrderedLocusNames=GYMC10_1195 {ECO:0000313|EMBL:ACX63484.1}; OS Geobacillus sp. (strain Y412MC10). OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX63484.1, ECO:0000313|Proteomes:UP000002381}; RN [1] {ECO:0000313|Proteomes:UP000002381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA Brumm P., Mead D.; RT "Complete sequence of Geobacillus sp. Y412MC10."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACX63484.1, ECO:0000313|Proteomes:UP000002381} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y412MC10 {ECO:0000313|EMBL:ACX63484.1, RC ECO:0000313|Proteomes:UP000002381}; RX PubMed=23408395; DOI=10.4056/sigs.2605792; RA Mead D.A., Lucas S., Copeland A., Lapidus A., Cheng J.F., Bruce D.C., RA Goodwin L.A., Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C.S., RA Tapia R., Land M., Hauser L.J., Chang Y.J., Kyrpides N.C., Ivanova N.N., RA Ovchinnikova G., Woyke T., Brumm C., Hochstein R., Schoenfeld T., Brumm P.; RT "Complete Genome Sequence of Paenibacillus strain Y4.12MC10, a Novel RT Paenibacillus lautus strain Isolated from Obsidian Hot Spring in RT Yellowstone National Park."; RL Stand. Genomic Sci. 6:381-400(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|RuleBase:RU361154}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}. 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; CP001793; ACX63484.1; -; Genomic_DNA. DR AlphaFoldDB; D3EI13; -. DR STRING; 481743.GYMC10_1195; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR KEGG; gym:GYMC10_1195; -. DR HOGENOM; CLU_002346_0_2_9; -. DR Proteomes; UP000002381; 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:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt. DR Gene3D; 2.70.98.10; -; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR004199; B-gal_small/dom_5. DR InterPro; IPR036156; Beta-gal/glucu_dom_sf. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR014718; GH-type_carb-bd. DR InterPro; IPR006101; Glyco_hydro_2. DR InterPro; IPR023232; Glyco_hydro_2_AS. DR InterPro; IPR006103; Glyco_hydro_2_cat. DR InterPro; IPR023230; Glyco_hydro_2_CS. DR InterPro; IPR006102; Glyco_hydro_2_Ig-like. DR InterPro; IPR006104; Glyco_hydro_2_N. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR032312; LacZ_4. DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1. DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1. DR Pfam; PF02929; Bgal_small_N; 1. DR Pfam; PF00703; Glyco_hydro_2; 1. DR Pfam; PF02836; Glyco_hydro_2_C; 1. DR Pfam; PF02837; Glyco_hydro_2_N; 1. DR Pfam; PF16353; LacZ_4; 1. DR PRINTS; PR00132; GLHYDRLASE2. DR SMART; SM01038; Bgal_small_N; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1. DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1. PE 3: Inferred from homology; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}. FT DOMAIN 737..1008 FT /note="Beta galactosidase small chain/" FT /evidence="ECO:0000259|SMART:SM01038" SQ SEQUENCE 1032 AA; 116820 MW; AE78F67022EBA170 CRC64; MKDHRIGRDW DDLSVLERNR AKSRAYFIPF ADADGALSYD RGSSAWYQSL NGVWKFHYAE EPESAPEAFY GEDYDVSAWD DLPVPGHWQL QGYGHPHYTD LYYPFPVDPP HVPNANPTGS YVREFKLPQH WDGRKICVKF DGVDSAFHVW LNGSFIGYSQ GSRLTSEFDL TPYVKPGVNK MSVRVYQWSD GSYLEDQDMW WMSGIFRDVY LIAEPSALRV NDFRVTTELD AEYRNAKLQV RLELEGTERG SVQLRLLNGA GAEMGSTGKD VGHSSVENFE IEVAGPDLWS AESPALYHLV ITLLDNQGET LETVAQRVGF RSIEVKDGQL LVNGRAILLK GVNRHDHHPD TGRTVTLSTM LEDIRLMKQH NINAVRTAHY PNDPRFYELC DVYGLYVMEE TDLETHGFEP LGNISRLSDD PDWKEAYVDR VRRMVERDKN HPSVLFWSLG NESGFGCNFR AMAEWCREHD PTRLIHYEED REAEVCDVVS TMYSSVEKME GFGKMADHPK PHILCEFAHA MGNGPGGLRP YFDAFEAHPR LAGGFVWEWI DHGLSRRTPD GRMDYAYGGD YGDVPNNSNF VIDGLVRPDR TPSPGLLEYK KVIEPVRMSM RRHGVLHIMN RYDFISLDHL QAHYRVLSDG QLVHSEALDL PRIEAGTSAE LSLLKALEQA TIGVNPFAEL WLEVSLSLAA DCRWAERGHE VAWSQFLLRE SSKPEFEPTA ALQRGALQIS EEKHGLHVGN GSFQLSLSAL HAGFETLSMH GKRIALGGPA LNFWRPPIDN DMYVLPDWRK AHLDRLSERV DHFEWKRLDR ECVEVKRVSR IAPPVYDWGF RCETTYTITS SGLIIIDVKG EPIGTPPGML PKIGLQMQVA GDMEHVRWYG RGPGESYPDS LEAGRFGEYR STVDGLFTPY IYPQENGNRS DVRWVSLADG AGLGLLAVGE PSLNFSASRY TDQDVESAAH ASDLVPQRFI TLNLDYRQNG LGSNSCGPAQ APEHSIKPEP FSFRMLLKPY AAEDTDPVRL SRRMRSEAGL YE //