ID   BGALE_ASPFC             Reviewed;        1011 AA.
AC   B0XXE7;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Probable beta-galactosidase E;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase E;
DE   Flags: Precursor;
GN   Name=lacE; ORFNames=AFUB_048070;
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; DS499596; EDP53621.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XXE7; -.
DR   SMR; B0XXE7; -.
DR   EnsemblFungi; EDP53621; EDP53621; AFUB_048070.
DR   VEuPathDB; FungiDB:AFUB_048070; -.
DR   HOGENOM; CLU_005732_2_0_1; -.
DR   PhylomeDB; B0XXE7; -.
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; 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   3: Inferred from homology;
KW   Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1011
FT                   /note="Probable beta-galactosidase E"
FT                   /id="PRO_0000395242"
FT   ACT_SITE        196
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        299
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   BINDING         92
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         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
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        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        455
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        588
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        622
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        704
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        745
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        759
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        772
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        778
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        913
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        267..316
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1011 AA;  111734 MW;  6312E4B521800294 CRC64;
     MKSLLKRLIA LAAAYSVAAA PSFSHHSSQD AANKRELLQD LVTWDQHSLF VRGERLMIFS
     GEFHPFRLPV PGLWFDVFQK IKSLGFNAVS FYTDWGLMEG NPGHVVTDGI WSLDEFFTAA
     REAGLYLIAR PGPYINAETS AGGIPGWVLR RKGIIRSNSE DYLRATDTYM ATLGKIIAKA
     QITNGGPVIL VQPENEYTTW PNVSESEFPT TMNQEVMAYA EKQLRDAGVV VPTVVNDNKN
     LGYFAPGTGL GETDLYGIDA YPMRYDCGNP YVWPTYRFPR DWQHEHRNHS PTTPFAIMEF
     QGGSGDGWGG VTEDGCAILV NNEAVRVVYK NNYGFGVRVF NIYMTYGGTN WGNLGYYGGY
     TSYDYGAAIT EDRQIWREKY SEEKLQANFL KVSPAYLTST PGNGVNGSYT GNKDITVTPL
     FGNGTTTNLY LVRHADFTST GSAQYNLSIS TSVGNVTIPQ LGGSLSLNGR DSKFHITDYD
     VGGFNLIYSS AEVFTWAKGD NKKRVLVLYG GAGELHEFAL PKHLPRPTVV EGSYVKIAKQ
     GSAWVVQWEV AAQRRVLRAG KLEIHLLWRN DAYQHWVLEL PAKQPIANYS SPSKETVIVK
     GGYLLRSAWI TDNDLHLTGD VNVTTPLEVI SAPKRFDGIV FNGQSLKSTR SKIGNLAATV
     HYQPPAISLP DLKRLDWKYI DSLPEISTEY NDEGWTPLTN TYTNNTREFT GPTCLYADDY
     GYHGGSLIYR GHFTANGDES WVFLNTSGGV GFANSVWLNQ TFLGSWTGSG RNMTYPRNIS
     LPHELSPGEP YVFTVVIDHM GQDEEAPGTD AIKFPRGILD YALSGHELSD LRWKMTGNLG
     GEQYQDLTRG PLNEGAMYAE RQGYHLPSPP TSSWKSSNPI KEGLTGAGIG FYATSFSLDL
     PEGYDIPLSF RFNNSASAAR SGTSYRCQLF VNGYQFGKYV NDLGPQTKFP VPEGILNYNG
     VNYVAVSLWA LESQGALIGG LDLVASTPIL SGYRKPAPAP QPGWKPRRGA Y