ID   BGALE_NEOFI             Reviewed;        1011 AA.
AC   A1DJ58;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=NFIA_000910;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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; DS027697; EAW16747.1; -; Genomic_DNA.
DR   RefSeq; XP_001258644.1; XM_001258643.1.
DR   AlphaFoldDB; A1DJ58; -.
DR   SMR; A1DJ58; -.
DR   STRING; 36630.CADNFIAP00000075; -.
DR   EnsemblFungi; EAW16747; EAW16747; NFIA_000910.
DR   GeneID; 4585646; -.
DR   KEGG; nfi:NFIA_000910; -.
DR   VEuPathDB; FungiDB:NFIA_000910; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_005732_2_0_1; -.
DR   OMA; IDAYPMR; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000006702; 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; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1011
FT                   /note="Probable beta-galactosidase E"
FT                   /id="PRO_0000395244"
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        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;  111421 MW;  2E6518FE3F132FAC CRC64;
     MKFLLRRFIA LAAASSVVAA PSVSHLSLQD AANRRELLQD LVTWDQHSLF VRGERLMIFS
     GEFHPFRLPV PGLWFDVFQK ITSLGFNAVS FYTDWGLMEG NPGHVVTDGI WSLDEFFTAA
     SEAGIYLIAR PGPYINAETS AGGIPGWVLR LKGIIRSNSE DYLRATDTYM ATLGKIIAKA
     QITNGGPVIL VQPENEYTTW PNVSESEFPT TMNKEVMAYA EKQLRDAGVV VPTVVNDNKN
     LGYFAPGTGL GETDLYGIDA YPMRYDCGNP YVWPTYRFPR DWQHTHRNHS PTTPFAIMEF
     QGGSGDGWGG VTEDGCAILV NNEAVRVVYK NNYGFGVGVF NIYMTYGGTN WGNLGYHGGY
     TSYDYGAAIT EDRQIWREKY SEEKLQANFL KVSPAYLTAT PGNGVNGSYT GNKDIAVTPL
     FGNGTTTNFY LVRHADFTST GSVQYQLSVS TSVGNVTIPQ LGGSLSLNGR DSKFHVTDYD
     VGEFNLIYSS AEIFTWAKGD NKKRVLVLYG GAGELHEFAL PKHLPRPTVV DGSDVKMAKK
     GSAWVVQWEV TAQRRVLRAG KLEIHLLWRN DAYQHWVLEL PAKQPIANYS SPSKETVLVK
     GGYLLRSACI TNNKLHLTGD VNATTPLEVI SAPKRFDGIV FNGQSLKSTR SKIGNLAATV
     RYQPPAISLP DLKRLDWKYL DSLPEISPDY SDEGWMSLTN TYTNNTRKFT GPTCLYADDY
     GYHGGSLIYR GHFKANGDES WVFLNTSGGV GFANSVWLNQ TFLGSWTGSG NNMTYPRNIS
     LPHELSPGKP YVFTVVIDHM GQDEEAPGTD AIKFPRGILD YALSGHEVSD LKWKMTGNLG
     GEQYQDSTRG PLNEGAMYAE RRGYHLPNPP TSSWKSSSPI NDGLTGAGIG FYATSFSLDL
     PEGYDIPLSF LFNNSASDAR SGTSYRCQLF VNGYQFGKYV NDLGPQTNFP VPEGILNYNG
     VNYVAVSLWA LEPQGALVGG LELVASTPIL SAYRKPVPAP QPGWKPRRGA Y