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   03-AUG-2022, entry version 59.
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}.
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DR   EMBL; DS231619; EDU48599.1; -; Genomic_DNA.
DR   RefSeq; XP_001936012.1; XM_001935977.1.
DR   AlphaFoldDB; B2W791; -.
DR   SMR; B2W791; -.
DR   STRING; 45151.EDU48599; -.
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; GHQSKII; -.
DR   OrthoDB; 179316at2759; -.
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; -; 1.
DR   Gene3D; 2.60.390.10; -; 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; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 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