ID BGALB_ASPOR Reviewed; 1022 AA. AC Q2U6P1; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 2. DT 27-MAR-2024, entry version 90. 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=AO090120000158; OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=510516; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42149 / RIB 40; RX PubMed=16372010; DOI=10.1038/nature04300; RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E., RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., RA Kikuchi H.; RT "Genome sequencing and analysis of Aspergillus oryzae."; RL Nature 438:1157-1161(2005). 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=BAE62774.1; 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; AP007166; BAE62774.1; ALT_SEQ; Genomic_DNA. DR AlphaFoldDB; Q2U6P1; -. DR SMR; Q2U6P1; -. DR STRING; 510516.Q2U6P1; -. DR Allergome; 1261; Asp o Lactase. DR CAZy; GH35; Glycoside Hydrolase Family 35. DR GlyCosmos; Q2U6P1; 17 sites, No reported glycans. DR OrthoDB; 1032627at2759; -. DR Proteomes; UP000006564; Chromosome 5. 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..22 FT /evidence="ECO:0000255" FT CHAIN 23..1022 FT /note="Probable beta-galactosidase B" FT /id="PRO_0000395226" FT ACT_SITE 196 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 309 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 264 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 374 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 172 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 210 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 251 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 271 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 412 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 457 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 551 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 598 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 627 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 704 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 749 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 787 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 821 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 882 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 921 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 270..325 FT /evidence="ECO:0000250" SQ SEQUENCE 1022 AA; 112493 MW; E18455942DAA8A62 CRC64; MLISKTVLSG LALGASFVGV SAQQNSTRWP LHDNGLTDTV EWDHYSFLIN GQRHFVFSGE FHYWRIPVPE LWRDLLEKIK AAGFTAFSIY NHWGYHSPKP GVLDFENGAH NFTSIMTLAK EIGLYMIIRP GPYVNAEANA GGLPLWTTTG AYGKLRDNDP RYLEALTPYW ANISKIIAPH LITNDGNVIL YQIENEYAEQ WLDEETHEPN TSGQEYMQYL EDVARENGID APLIHNLPNM NGHSWSKDLS NATGNVDVIG VDSYPTCWTC NVSECASTNG EYIPYLKLTY PQISYFKELS PTQPSFMPEF QGGSYNPWGG PQGGCPDDLG PDFANLFYRN LISQRVSAIS LYMLYGGTNW GWHASTDVAT SYDYSSPISE NRKLIEKYYE TKVLTQFTKI AQDLSKVDRL GNSTKYSSNP AVSVAELRNP DTGAAFYVTQ HEYTPSGTVE KFTVKVNTSE GALTIPQYGS QITLNGHQSK IIVTDFKFGS KTLLYSTAEV LTYAVIDGKE VLALWVPTGE SGEFTVKGVN SAKFADKGRT ANIEIHPGTN NVTVSFMQRS GMSLVELGDG TRIVLLDRSA AHVFWSTPLN NDPAEAGNNT VLVHGPYLVR SAKLEGCDLK LTGDIQNSTE VSIFAPKSVC SVNWNGKKTS VKSAKGGVIT TTLGGDAKFE LPTISGWKSA DSLPEIAKDY SATSKAWVVA TKTNSSNPTP PAPNNPVLYV DENDIHVGNH IYRATFPSTD EPPTDVYLNI TGGRAFGYSV WLNSDFIGSW LGTATTEQND QTFSFSNATL STDEDNILVV VMDNSAHDLR DGALNPRGIT NATLIGPGSY SFTEWKLAGN AGFEDHLDPV RAPLNEGSLY AERVGIHLPG YEFDEAEEVS SNSTSLTVPG AGIRVFRTVV PLSVPQGLDV SISFRLTAPS NVTFTSAEGY TNQLRALLFV NGYQYGRFNP YIGHQIDFPV PPGVLDYNGD NTIAVTVWSQ SVDGAEIKVD WNVDYVHETS FDMNFDGAYL RPGWIEERRE YA //