ID   BGALA_PENEN             Reviewed;        1011 AA.
AC   B8QGZ3;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Probable beta-galactosidase A;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase A;
DE   Flags: Precursor;
GN   Name=lacA;
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=F3;
RA   Li Y.M., Xiao M.;
RT   "Purification and molecular cloning of beta-galactosidase from Penicillium
RT   expansum F3.";
RL   Submitted (MAR-2008) 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   ---------------------------------------------------------------------------
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; EU543998; ACD75821.1; -; mRNA.
DR   EMBL; EU543999; ACD75822.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8QGZ3; -.
DR   SMR; B8QGZ3; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
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; IPR019801; Glyco_hydro_35_CS.
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.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1011
FT                   /note="Probable beta-galactosidase A"
FT                   /id="PRO_0000395222"
FT   ACT_SITE        200
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        299
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
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         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        625
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        763
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        780
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        917
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        205..206
FT                   /evidence="ECO:0000250"
FT   DISULFID        267..316
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1011 AA;  110414 MW;  9362248E6B7B2552 CRC64;
     MKLLSSLALA ALAAQVSGAA ISHKLDGFTL REHADASKRE LLQKYVTWDK HSIFINGERL
     MMFSGEVHPY RLPVASLYID VFEKIKALGF NCVSFYVDWA LLEGKPGHYT AEGIFDLQPF
     FDAAKEAGIY LLARPGPYIN AEVSGGGFPG WLQRVNGTLR TSIGDYLKST DNYASHIAKT
     IAKAQITNGG PIILYQPENE YSGACCGYED FPDGSYMQYI EDHARDAGIV VPFISNDAYA
     GGHNAPGTGK GAVDIYGHDG YPLGFDCANP SVWPDGNLPT NYHTLHEEQS PTTPFSVVEF
     QGGAFDPWGG VGFAKCAHLL NHEFERVFYK NDFSFGVTFF NLYMIFGGTN WGNLGHPGGY
     TSYDYGSAIS ESRNVTREKY SELKLLGNFA KVSPGYVVAN PGNLTTSKYT KTADLTVTPL
     LGESSSAGSF FVIRHSNYNS QASVKYQLTL PTSAGELTIP QLGGELTLSG RDSKIHVTDY
     DVAGSNILYS TAEVFTWKKF DNGKVLILYG GPGEHHEFAV TGASASSVIE GSSSGITSKK
     IGDALVVAWD VSSKRRIIKI GDLKVFLLDR NSAYNYWVPH LPTKGKAPGY VSKKAIDSSI
     IVKAGYLVRS AFLSGKDLHI QADFNATTPI EIIGAPSSAK NLVINGKKTK TNVDDNGIWS
     ASVSYSTPEI HLPSLKDLKW QSIDTLPEVK NSYDDSAWTS ADQPHTLNTA HELQTPTTLF
     SSDYGYHTGT LLYRGHFVAN GKESIFFIQT QGGSAYGHSV WVNETYVGSW EGSGSNDNYN
     ATYTLPSLAT GKKYAITVVI DNMGLDVNWV IGQEGMKNPR GIIRYNLAGH DASAISWKLT
     GNLGGEDYRD TVRGPLNEGG LYAERQGFHQ PKPSTKNWDS SSPFTGLTKP GIRFYSASFD
     LDLPSGYDIP LYFNFGNSTA PPDAYRVQLF VNGYQYGKYV NNVGPQTSFP VPEGILNYHG
     TNWIALSLWA QQESGAKLNS FELINTTPVL TSLDKVKSVD QPKYKSRKGA Y