ID   BGALB_ASPFC             Reviewed;        1015 AA.
AC   B0XNY2;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=AFUB_016080;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499594; EDP56886.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XNY2; -.
DR   SMR; B0XNY2; -.
DR   EnsemblFungi; EDP56886; EDP56886; AFUB_016080.
DR   VEuPathDB; FungiDB:AFUB_016080; -.
DR   HOGENOM; CLU_005732_2_1_1; -.
DR   PhylomeDB; B0XNY2; -.
DR   Proteomes; UP000001699; 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; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1015
FT                   /note="Probable beta-galactosidase B"
FT                   /id="PRO_0000395223"
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        99
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        172
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        554
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        679
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        735
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        821
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        271..324
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1015 AA;  111681 MW;  D9EB8677F99A13A8 CRC64;
     MAHIYRLLLL LLSNLWFSTA AQNQSETEWP LHDNGLSKVV QWDHYSFQVN GQRIFIFSGE
     FHYWRIPVPE LWRDILEKVK ATGFTAFAFY SSWAYHAPNN STVDFSTGAR DITPIFELAK
     ELGMYMIVRP GPYVNAEASA GGFPLWLMTG EYGSLRNDDP RYTAAWTPYF ANMSQITSKY
     QVTDGHNTLV YQIENEYGQQ WIGDPKNRNP NKTAVAYMEL LEASARENGI TVPLTSNDPN
     MNSKSWGSDW SNAGGNVDVA GLDSYPSCWT CDVSQCTSTN GEYVPYKVID YYDYFQEVQP
     TLPSFMPEFQ GGSYNPWAGP EGGCPQDTSA EFANLFYRWN IGQRVTAMSL YMLYGGTNWG
     AIAAPVTATS YDYSAPISED RSIGAKYSET KLLALFTRTA KDLTMTEAIG NGTQYTTNTA
     VRAFELRNPQ TNAGFYVTFH TDTTVGGNQA FKLHVNTSVG ALTVPKNEGL IQLNGHQSKI
     IVTDFTLGKR TLLYSTAEVL TYAVFENRPT LVLWVPTGES GEFAIKGAKS GKVENGDGCS
     GIKFKREKDY LVVNFSQAKG LSVLRLDNGV RVVLLDKAAA YRFWAPALTD DPNVQETETV
     LVHGPYLVRS ASISKTTLAL RGDSVEKTTL EIFAPHSVRK ITWNGKEVQT SHTPYGSLKA
     TLAAPPDIKL PALTSWRSND SLPERLPSYD DSGPAWIEAN HMTTSNPSPP ATFPVLYADE
     YGFHNGVRLW RGYFNGSASG VFLNIQGGSA FGWSAWLNGH FLDSHLGTAT TSQANKTLTF
     PSSILNPTEN VLLIVHDDTG HDQTTGALNP RGILEARLLS NDTSSPPPEF THWRLAGTAG
     GESNLDPIRG VFNEDGLFAE RMGWHLPGFD DSAWTSENSA TSASSALSFT GATVRFFRSV
     VPLNIPAGLD VSISFVLSTP TAAPKGYRAQ LFVNGYQYGR YNPHIGNQVV FPVPPGILDY
     QGDNTIGLAV WAQTEEGAGI QVDWKVNYVA DSSLSVAGFG KGLRPGWTEE RLKFA