ID   BGALB_NEOFI             Reviewed;        1015 AA.
AC   A1D199;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=NFIA_008690;
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; DS027688; EAW22192.1; -; Genomic_DNA.
DR   RefSeq; XP_001264089.1; XM_001264088.1.
DR   AlphaFoldDB; A1D199; -.
DR   SMR; A1D199; -.
DR   STRING; 36630.CADNFIAP00001723; -.
DR   EnsemblFungi; EAW22192; EAW22192; NFIA_008690.
DR   GeneID; 4591479; -.
DR   KEGG; nfi:NFIA_008690; -.
DR   VEuPathDB; FungiDB:NFIA_008690; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_005732_2_1_1; -.
DR   OMA; GHQSKII; -.
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; 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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1015
FT                   /note="Probable beta-galactosidase B"
FT                   /id="PRO_0000395230"
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        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        441
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   CARBOHYD        878
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        271..324
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1015 AA;  111471 MW;  7BDC616E2D3A2DFF CRC64;
     MAHIYRLLLL LLSNLWFSAA AQNQSETEWP LHDNGLSKVV QWDHYSFQVN GQRIFIFSGE
     FHYWRIPVPE LWRDILEKVK ATGFTAFAFY SSWAYHAPNN RTVDFSTGAR DITPIFELAK
     ELGMYMIVRP GPYVNAEASA GGFPLWLTTG EYGSLRNDDP RYTAAWTPYF ANMSQITSKY
     QVTDGHNTLV YQIENEYGQQ WIGDPKDRNP NKTAVAYMEL LEASALENGI TVPLTSNDPN
     MNSKSWGSDW SNAGGNVDVA GLDSYPSCWT CDVSQCTSTN GEYVPYKVID YYDYFQEVQP
     TLPSFMPEFQ GGSYNPWAGP EGGCPQDTGA EFANLFYRWN IGQRVTAMSL YMLYGGTNWG
     AIAAPVTATS YDYSAPISED RSIGAKYSET KLLALFTRTA KDLTMTEAIG NGTQYTTNTA
     VRAFELRNPQ TNAGFYVTFH NDTTVGGNQA FKLHVNTSVG ALTVPKNEGV IQLNGHQSKI
     IVTDFTLGKR TLLYSTAEVL TYAVFENRPT LVLWVPTGES GEFAIKGTKS GKVENGDGCS
     GINFKREKDY LVVNFSQAKG LSVLRLDNGV RVVLLDKAAA YRFWAPALTD DPIVQETETV
     LVHGPYLVRS ASVSKSTLAL RGDSVEKTTL EIFAPHSVRK ITWNGKEVKT SQTPYGSLKA
     TLAAPPTIKL PALTSWRSND SLPERLPSYD DSGPAWIEAN HMTTSNPSPP ATLPVLYADE
     YGFHNGVRLW RGYFNGSASG VFLNIQGGSA FGWSAWLNGH FLDSHLGTAT TSQANKTLTF
     SSSILNPTEN VLLIVHDDTG HDQTTGALNP RGIIEARLLS NDTSSPAPGF TQWRIAGTAG
     GESNLDPIRG VFNEDGLFAE RMGWHLPGFD DSAWTPENST TSASSALSFT GATVRFFRTV
     VPLDIPAGLD VSISFVLSTP SAAPKGYRAQ LFVNGYQYGR YNPHIGNQVV FPVPPGILDY
     QGDNTIGLAV WAQTEEGAGI QVDWKVNYVA DSSLSVAGFG KGLRPGWTEE RLKFA