ID BGALB_PYRTR Reviewed; 1009 AA. AC B2W791; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 64. 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=PTRG_05679; OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus) OS (Drechslera tritici-repentis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; OC Pyrenophora. OX NCBI_TaxID=426418; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pt-1C-BFP; RX PubMed=23316438; DOI=10.1534/g3.112.004044; RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B., RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H., RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W., RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S., RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.; RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici- RT repentis, reveals transduplication and the impact of repeat elements on RT pathogenicity and population divergence."; RL G3 (Bethesda) 3:41-63(2013). 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 --------------------------------------------------------------------------- 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; DS231619; EDU48599.1; -; Genomic_DNA. DR RefSeq; XP_001936012.1; XM_001935977.1. DR AlphaFoldDB; B2W791; -. DR SMR; B2W791; -. DR STRING; 426418.B2W791; -. DR GlyCosmos; B2W791; 13 sites, No reported glycans. DR EnsemblFungi; EDU48599; EDU48599; PTRG_05679. DR GeneID; 6343933; -. DR eggNOG; KOG0496; Eukaryota. DR HOGENOM; CLU_005732_2_1_1; -. DR InParanoid; B2W791; -. DR OMA; GGCPGDI; -. DR OrthoDB; 1032627at2759; -. DR Proteomes; UP000001471; 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..27 FT /evidence="ECO:0000255" FT CHAIN 28..1009 FT /note="Probable beta-galactosidase B" FT /id="PRO_0000395232" FT ACT_SITE 202 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 314 FT /note="Nucleophile" FT /evidence="ECO:0000255" FT BINDING 96 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 141 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 142 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 143 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 201 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 271 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 379 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 106 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 467 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 495 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 547 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 593 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 632 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 672 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 707 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 775 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 782 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 789 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 795 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 914 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 277..330 FT /evidence="ECO:0000250" SQ SEQUENCE 1009 AA; 109564 MW; 572EAEC64D06F663 CRC64; MKTIAGLSWI SALSSLASLP NGLGVSAQNN TPSTWPLHDN GLSDVVQWDH YSFKVNGKRL FVFSGEIHYW RIPVYEVWED LLEKIKAAGF TAFAFYGNWA YHSANNKTLD FESGAHDFSK LFEIAHRVGL YVITRPGPYV NAEANAGGFP LWLTTGAYGK LRDDDPRYLQ ALDPYFSKFS ELTSKHLVTN GGNALVYQIE NEYGEQWKDR TKKIPNDAAG RYMQALEDSA RANGIEIPLI HNDPNMNTKS WSKDYAPGAV GNVDVAGLDS YPSCWSCNLA ECTGTNGKYV AYQVVNYYDH FKEVSPTQPS FFPEFQGGSY NPWGGPEGGC PGDIGADFAN LFYRNLISQR VTAVSLYMMF GGTNWGAIAA PVTATSYDYS SPISENREIG AKFYETKNLA MFTRVADDLT VTDRLGSSSS YTTNPAVTAS ELRNPITKAA FYVTIHSVSS SSTTESFKLH ISTSVGNLTI PQHSGSIVLN GHQSKIISTD FAMGNKTLTY STAEILTYAL IDSSPVVVLS TDVGGSVEFH VKGATKGSLA SSGFTSNATF RAEAGGVTTN IERVTGMGVY QFNNGVKVVL ADKPTAYLFW APNLSNDPFA PVDQSVLIQG PYLVRGAALD GDVVALKGDV KNSTTIEVFA HETALTLSWN GKKLETSRTP YGSLKAQISA FNGTIPLPSL NDWKVNEGLP EKMPEYDDNG AAWVVANHTT TPNPTKPDTL PVLYVDEYGF HNSFHLFRGY FEGSATGAQL SVQGGLAFGW SAWLNGDLVG SWLGNTTLGV GNMTLSFANA TVHANGTNVL LIAQDNTGHD LRGGATDPRG ILRATLDGAD FTSWKIAGEA GGENIQLDPV RGPLAEGGLT AERLGWHLSG FSDCDWASAS PSTGFSGADI KFYRTTFPLD IPEDVDASFA FILNATGPKT VRVQLFVNGY QYARFNPYVG NEVKFPIPPG ILNYAGDNVI GLSVWAQGND GAKVDVEFVQ EYAVESSWSS RFDSEYLRPE WTEERLAYA //