ID D5BHW5_ZUNPS Unreviewed; 1033 AA. AC D5BHW5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAR-2024, entry version 69. DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, 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=ZPR_1008 {ECO:0000313|EMBL:ADF51353.1}; OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia OS profunda). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Zunongwangia. OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF51353.1, ECO:0000313|Proteomes:UP000001654}; RN [1] {ECO:0000313|EMBL:ADF51353.1, ECO:0000313|Proteomes:UP000001654} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87 RC {ECO:0000313|Proteomes:UP000001654}; RX PubMed=20398413; DOI=10.1186/1471-2164-11-247; RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y., RA Zhou B.C., Yu J., Zhang Y.Z.; RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation RT to the deep-sea environment and ecological role in sedimentary organic RT nitrogen degradation."; RL BMC Genomics 11:247-247(2010). 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 -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; 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; CP001650; ADF51353.1; -; Genomic_DNA. DR RefSeq; WP_013070505.1; NC_014041.1. DR AlphaFoldDB; D5BHW5; -. DR STRING; 655815.ZPR_1008; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR KEGG; zpr:ZPR_1008; -. DR eggNOG; COG3250; Bacteria. DR HOGENOM; CLU_002346_0_2_10; -. DR OrthoDB; 9801077at2; -. DR Proteomes; UP000001654; 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 Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..1033 FT /note="Beta-galactosidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003069913" FT DOMAIN 753..1027 FT /note="Beta galactosidase small chain/" FT /evidence="ECO:0000259|SMART:SM01038" SQ SEQUENCE 1033 AA; 117408 MW; 69EBB1CE0A90D124 CRC64; MNLTASLYFI LFCCFAGLAQ EVNEWENPLV YERNKLQPHT DFIAYTTETD ARADVFSTSP YYQSLNGTWK FNFVKKPEDR PRDFYKTGFD DSGWDRISVP GNWELEGFGI PIYTNIDYPF PKNPPFVDNS YNPVGTYRRS FEIPETWGDK EVILNLSSVS GYARVFVNGK EAGMTKVAKS PSEFDITSLL VKGKNQLAIQ VFRWHDGSYL EDQDFWRLSG LEQDVFLYAL PKTSIWDFFL KAGLENNYKD GVFDASVSLK SFDNAAQSGS LQLEIIPANA SKPVYSATKK FTTADTPLNF QTTIKNVKSW SAETPNLYDV VLTLKDAAGK TLMLTSEQIG FREIELKNAQ LLVNGMPVLI KGVNLHIHDD VKGHVPSREV MLKDLKLMKQ NNINAVRTSH YPQNPLWYKL CDQYGMYLVD EANIESHGMG ANVHAVKNKD RHPAYQPEWF PAQMDRIQRL VERDKNHPSV IIWSLGNECG NGIFFPQAYD WVKAHDTTRL VQFEQANEER NTDVVCPMYP SIDYMREYAA ATDKYRPYIM CEYAHAMGNS TGNFTEYWDI IRSSDQMQGG FIWDWVDQGI KTQDDMGTYW AYGGDLGGLN FQNDENFCAN GLVSSNRTPH PALEEVKLIY QNVQFDFDKE SKKLSVFNEF DFTNLKEYQF QWELLKDGAV VKTEDFSLAV APQTSGTAKI KLPKLDADAE YLLNVYAFTK IATALVPAGH ELAKAQFSLT EPVFTTAKTN QSLEVKTEGN QLVFDSGSTH GTFDLKTGEF TSYTNGEVRL EGLPQPFFWR APTDNDFGNN MPEELNIWRS AHSNITLQDV KVEKQTEAGL PIEVTYHLDD IDLPYTLAYV IQNEGSIRVT AKLDLKAKKL PELPRFGMRM QLPAGFENLE YYGRGPEENY ADRNSAAFIG IYKAQVDSLK MPYIRPQEYG YHTDTRWLKL TDAGGNGIEV EGLQPLSFSA LPIKTEALDP GETKKNQHPT DLRYGDETTL HIDWAQRGLG GDTSWGAYPH SQYLLTKDGY TYSYVLKLIK PKP //