ID BGALB_ASPNC Reviewed; 1017 AA. AC A2QA64; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 2. DT 27-MAR-2024, entry version 86. DE RecName: Full=Probable beta-galactosidase B; DE EC=3.2.1.23; DE AltName: Full=Lactase B; DE Flags: Precursor; GN Name=lacB; ORFNames=An01g10350; OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=425011; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513; RX PubMed=17259976; DOI=10.1038/nbt1282; RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M., RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.; RT "Genome sequencing and analysis of the versatile cell factory Aspergillus RT niger CBS 513.88."; RL Nat. Biotechnol. 25:221-231(2007). CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from CC gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000250}. 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAK37216.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; AM269980; CAK37216.1; ALT_SEQ; Genomic_DNA. DR AlphaFoldDB; A2QA64; -. DR SMR; A2QA64; -. DR CAZy; GH35; Glycoside Hydrolase Family 35. DR GlyCosmos; A2QA64; 15 sites, No reported glycans. DR EnsemblFungi; CAK37216; CAK37216; An01g10350. DR Proteomes; UP000006706; Chromosome 2R. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1. DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR018954; Betagal_dom2. DR InterPro; IPR037110; Betagal_dom2_sf. DR InterPro; IPR025972; BetaGal_dom3. DR InterPro; IPR036833; BetaGal_dom3_sf. DR InterPro; IPR025300; BetaGal_jelly_roll_dom. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR031330; Gly_Hdrlase_35_cat. DR InterPro; IPR001944; Glycoside_Hdrlase_35. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR23421:SF64; BETA-GALACTOSIDASE (EUROFUNG)-RELATED; 1. DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1. DR Pfam; PF13364; BetaGal_ABD2; 2. DR Pfam; PF10435; BetaGal_dom2; 1. DR Pfam; PF13363; BetaGal_dom3; 1. DR Pfam; PF01301; Glyco_hydro_35; 1. DR PRINTS; PR00742; GLHYDRLASE35. DR SMART; SM01029; BetaGal_dom2; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 2. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..1017 FT /note="Probable beta-galactosidase B" FT /id="PRO_5000219426" FT ACT_SITE 196 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 308 FT /note="Nucleophile" FT /evidence="ECO:0000255" FT BINDING 90 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 136 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 137 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 195 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 265 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 373 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 23 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 100 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 158 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 211 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 411 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 417 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 456 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 628 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 681 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 737 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 770 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 777 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 785 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 828 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 829 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 271..324 FT /evidence="ECO:0000250" SQ SEQUENCE 1017 AA; 111810 MW; 3ACF69B3DFD08D04 CRC64; MTRITKLCVL LLSSIGLLAA AQNQTETGWP LHDDGLTTDV QWDHYSFKVH GERIFVFSGE FHYWRIPVPG LWRDILEKIK AAGFTTFAFY SSWAWHAPNN HTVDFSTGAR DITPIFELAK ELGMYIIVRP GPYINAEASA GGFPLWLTTG DYGTLRNNDS RYTEAWKPYF EKMTEITSRY QITNGHNTFC YQIENEYGDQ WLSDPSERVP NETAIAYMEL LESSARENGI LVPFTANDPN MNAMAWSRDW SNAGGNVDVV GLDSYPSCWT CDVSQCTSTN GEYVAYQVVE YYDYFLDFSP TMPSFMPEFQ GGSYNPWAGP EGGCGDDTGV DFVNLFYRWN IAQRVTAMSL YMLYGGTNWG AIAAPVTATS YDYSSPISED RSISSKYYET KLLSLFTRSA RDLTMTDLIG NGTQYTNNTA VKAYELRNPT TNAGFYVTLH EDSTVGTNEA FSLRVNTSAG NLIVPRLGGS IRLNGHQSKI IVTDFTFGSE TLLYSTAEVL TYAVIDKKPT LVLWVPTDES GEFAVKGAKS GSVVSKCQSC PAINFHQQGG NLIVGFTQSQ GMSVVQIDND IRVVLLDRTA AYKFWAPALT EDPLVPEDEA VVLIQGPYLV RSASLEKSTL AIKGDSINET AVEIFAPENV KTITWNGKQL KTSKSSYGSL KATIAAPASI QLPAFTSWKV NDSLPERLPT YDASGPAWVD ANHMTTANPS KPATLPVLYA DEYGFHNGVR LWRGYFNGTA SGVFLNVQGG SAFGFSAYLN GHFLGSYLGN ASIEQANQTF LFPNNITHPT TQNTLLVIHD DTGHDETTGA LNPRGILEAR LLPSDTTNNS TSPEFTHWRI AGTAGGESNL DPVRGAWNED GLYAERVGWH LPGFDDSTWS SVSSSSSLSF TGATVKFFRT TIPLDIPRGL DVSISFVLGT PDNAPNAYRA QLFVNGYQYG RFNPYIGNQV VFPVPVGVLD YTGENTIGVA VWAQTEDGAG ITVDWKVNYV ADSSLDVSGL ETGELRPGWS AERLKFA //