ID BGALB_ASPTN Reviewed; 1022 AA. AC Q0CMF3; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 2. DT 27-MAR-2024, entry version 78. 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=ATEG_05131; OS Aspergillus terreus (strain NIH 2624 / FGSC A1156). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=341663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIH 2624 / FGSC A1156; RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K., RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W., RA Nierman W.C., Milne T., Madden K.; RT "Annotation of the Aspergillus terreus NIH2624 genome."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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=EAU34200.1; 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; CH476600; EAU34200.1; ALT_SEQ; Genomic_DNA. DR RefSeq; XP_001214309.1; XM_001214309.1. DR AlphaFoldDB; Q0CMF3; -. DR SMR; Q0CMF3; -. DR STRING; 341663.Q0CMF3; -. DR GlyCosmos; Q0CMF3; 13 sites, No reported glycans. DR GeneID; 4320669; -. DR eggNOG; KOG0496; Eukaryota. DR OrthoDB; 1032627at2759; -. DR Proteomes; UP000007963; Unassembled WGS sequence. 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..1022 FT /note="Probable beta-galactosidase B" FT /id="PRO_0000395227" 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 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 456 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 541 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 554 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 626 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 790 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 832 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 880 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 881 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 271..324 FT /evidence="ECO:0000250" SQ SEQUENCE 1022 AA; 111471 MW; 032C051812784E46 CRC64; MARFPQLLFL LLASIGLLSA AQNHSDSEWP LHDNGLSTVV QWDHYSFHVH GQRIFVFSGE FHYWRIPVPG LWRDILEKIK AAGFTAFAFY SSWGYHAPNN HTVDFSTGAR DITPIYELAK ELGMYIIVRP GPYVNAEASA GGYPLWVTTG AYGSLRNDDA RYTAAWKPYF AKMSEITSQY QVTDGHNTFC YQIENEYGQQ WIGDPVDRNP NQTAVAYMEL LEASARENGI VVPLTANDPN MNTKSWGSDW SHAGGNVDVV GLDSYPSCWT CDVTQCTSTN GEYVPYKVMQ YYDYFQEVQP TMPGFMPEFQ GGSYNPWAGP EGGCPGDTGV DFANLFYRWN IAQRVTAMSL YMLYGGTNWG AIAAPVTATS YDYSSPISED RSIGSKYYET KLLALFTRSA TDLTMTDRIG NGTHYTNNPA VAAYELRNPV TNGAFYVTIH ADSTVGTDES FRLNVNTSAG ALTVPSKGSI RLNGHQSKII VTDFRFGPSH TLLYSTAEVL THAVMDKKAT LVLWVPTGES GEFAVKGAKS GKVERCPQCS NATFTRKKDV LVVNFTQAGG MSVLQLNNGV RVVLLDRAAA YKFWAPPLTD DPFAPETDLV LVQGPYLVRS ASLSGSTLAL RGDSANETAL EVFASKKVHT VTWNGKRIKT SRSSYGSLTA SLAAPPAVSL PALSSAQWKS QDSLPERLPS YDDSGPAWVD ANHMTTQNPR TPDTLPVLYA DEYGFHNGIR LWRGSFTDAA SGVYLNVQGG AAFGWSAYLN GHFLGSHLGT ATTSQANKTL LFPAGTLRKN TTNTILVIHD DTGHDQTTGA LNPRGILAAR LLAPSDSSTA PNFTQWRVAG TAGGESDLDP VRGVYNEDGL FAERMGWHLP GFDDADWPAN NSTTTRGAQV SLSVTGATVR FFRAVVPLHL PRGVDASISF MLGTPAGAST AYRAQLFVNG YQYGRFYPHI GNQVVYPVPA GVLDYDGENT IGVAVWAQSE AGAEMSLDWR VNYVADSSLD AVRVAAEGAL RPGWSEERLQ YA //